Copper-Containing Amine Oxidases and FAD-Dependent Polyamine Oxidases Are Key Players in Plant Tissue Differentiation and Organ Development
Identifieur interne : 000427 ( Pmc/Corpus ); précédent : 000426; suivant : 000428Copper-Containing Amine Oxidases and FAD-Dependent Polyamine Oxidases Are Key Players in Plant Tissue Differentiation and Organ Development
Auteurs : Paraskevi Tavladoraki ; Alessandra Cona ; Riccardo AngeliniSource :
- Frontiers in Plant Science [ 1664-462X ] ; 2016.
Abstract
Plant polyamines are catabolized by two classes of amine oxidases, the copper amine oxidases (CuAOs) and the flavin adenine dinucleotide (FAD)-dependent polyamine oxidases (PAOs). These enzymes differ to each other in substrate specificity, catalytic mechanism and subcellular localization. CuAOs and PAOs contribute to several physiological processes both through the control of polyamine homeostasis and as sources of biologically-active reaction products. CuAOs and PAOs have been found at high level in the cell-wall of several species belonging to Fabaceae and Poaceae families, respectively, especially in tissues fated to undertake extensive wall loosening/stiffening events and/or in cells undergoing programmed cell death (PCD). Apoplastic CuAOs and PAOs have been shown to play a key role as a source of H2O2 in light- or developmentally-regulated differentiation events, thus influencing cell-wall architecture and maturation as well as PCD. Moreover, growing evidence suggests a key role of intracellular CuAOs and PAOs in several facets of plant development. Here, we discuss recent advances in understanding the contribution of different CuAOs/PAOs, as well as their cross-talk with different intracellular and apoplastic metabolic pathways, in tissue differentiation and organ development.
Url:
DOI: 10.3389/fpls.2016.00824
PubMed: 27446096
PubMed Central: 4923165
Links to Exploration step
PMC:4923165Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Copper-Containing Amine Oxidases and FAD-Dependent Polyamine Oxidases Are Key Players in Plant Tissue Differentiation and Organ Development</title><author><name sortKey="Tavladoraki, Paraskevi" sort="Tavladoraki, Paraskevi" uniqKey="Tavladoraki P" first="Paraskevi" last="Tavladoraki">Paraskevi Tavladoraki</name></author><author><name sortKey="Cona, Alessandra" sort="Cona, Alessandra" uniqKey="Cona A" first="Alessandra" last="Cona">Alessandra Cona</name></author><author><name sortKey="Angelini, Riccardo" sort="Angelini, Riccardo" uniqKey="Angelini R" first="Riccardo" last="Angelini">Riccardo Angelini</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">27446096</idno><idno type="pmc">4923165</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4923165</idno><idno type="RBID">PMC:4923165</idno><idno type="doi">10.3389/fpls.2016.00824</idno><date when="2016">2016</date><idno type="wicri:Area/Pmc/Corpus">000427</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Copper-Containing Amine Oxidases and FAD-Dependent Polyamine Oxidases Are Key Players in Plant Tissue Differentiation and Organ Development</title><author><name sortKey="Tavladoraki, Paraskevi" sort="Tavladoraki, Paraskevi" uniqKey="Tavladoraki P" first="Paraskevi" last="Tavladoraki">Paraskevi Tavladoraki</name></author><author><name sortKey="Cona, Alessandra" sort="Cona, Alessandra" uniqKey="Cona A" first="Alessandra" last="Cona">Alessandra Cona</name></author><author><name sortKey="Angelini, Riccardo" sort="Angelini, Riccardo" uniqKey="Angelini R" first="Riccardo" last="Angelini">Riccardo Angelini</name></author></analytic><series><title level="j">Frontiers in Plant Science</title><idno type="eISSN">1664-462X</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Plant polyamines are catabolized by two classes of amine oxidases, the copper amine oxidases (CuAOs) and the flavin adenine dinucleotide (FAD)-dependent polyamine oxidases (PAOs). These enzymes differ to each other in substrate specificity, catalytic mechanism and subcellular localization. CuAOs and PAOs contribute to several physiological processes both through the control of polyamine homeostasis and as sources of biologically-active reaction products. CuAOs and PAOs have been found at high level in the cell-wall of several species belonging to Fabaceae and Poaceae families, respectively, especially in tissues fated to undertake extensive wall loosening/stiffening events and/or in cells undergoing programmed cell death (PCD). Apoplastic CuAOs and PAOs have been shown to play a key role as a source of H<sub>2</sub>O<sub>2</sub> in light- or developmentally-regulated differentiation events, thus influencing cell-wall architecture and maturation as well as PCD. Moreover, growing evidence suggests a key role of intracellular CuAOs and PAOs in several facets of plant development. Here, we discuss recent advances in understanding the contribution of different CuAOs/PAOs, as well as their cross-talk with different intracellular and apoplastic metabolic pathways, in tissue differentiation and organ development.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Agudelo Romero, P" uniqKey="Agudelo Romero P">P. Agudelo-Romero</name></author><author><name sortKey="Bortolloti, C" uniqKey="Bortolloti C">C. Bortolloti</name></author><author><name sortKey="Pais, M S" uniqKey="Pais M">M. S. Pais</name></author><author><name sortKey="Tiburcio, A F" uniqKey="Tiburcio A">A. F. Tiburcio</name></author><author><name sortKey="Fortes, A M" uniqKey="Fortes A">A. M. Fortes</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ahou, A" uniqKey="Ahou A">A. Ahou</name></author><author><name sortKey="Martignago, D" uniqKey="Martignago D">D. Martignago</name></author><author><name sortKey="Alabdallah, O" uniqKey="Alabdallah O">O. Alabdallah</name></author><author><name sortKey="Tavazza, R" uniqKey="Tavazza R">R. Tavazza</name></author><author><name sortKey="Stano, P" uniqKey="Stano P">P. Stano</name></author><author><name sortKey="Macone, A" uniqKey="Macone A">A. Macone</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Aloisi, I" uniqKey="Aloisi I">I. Aloisi</name></author><author><name sortKey="Cai, G" uniqKey="Cai G">G. Cai</name></author><author><name sortKey="Tumiatti, V" uniqKey="Tumiatti V">V. Tumiatti</name></author><author><name sortKey="Minarini, A" uniqKey="Minarini A">A. Minarini</name></author><author><name sortKey="Del Duca, S" uniqKey="Del Duca S">S. Del Duca</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="An, Z" uniqKey="An Z">Z. An</name></author><author><name sortKey="Jing, W" uniqKey="Jing W">W. Jing</name></author><author><name sortKey="Liu, Y" uniqKey="Liu Y">Y. Liu</name></author><author><name sortKey="Zhang, W" uniqKey="Zhang W">W. Zhang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Andronis, E A" uniqKey="Andronis E">E. A. Andronis</name></author><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Toumi, I" uniqKey="Toumi I">I. Toumi</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Fincato, P" uniqKey="Fincato P">P. Fincato</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author><author><name sortKey="Rea, G" uniqKey="Rea G">G. Rea</name></author><author><name sortKey="Chen, M M" uniqKey="Chen M">M. M. Chen</name></author><author><name sortKey="Botta, M" uniqKey="Botta M">M. Botta</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bollhoner, B" uniqKey="Bollhoner B">B. Bollhöner</name></author><author><name sortKey="Prestele, J" uniqKey="Prestele J">J. Prestele</name></author><author><name sortKey="Tuominen, H" uniqKey="Tuominen H">H. Tuominen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Boudart, G" uniqKey="Boudart G">G. Boudart</name></author><author><name sortKey="Jamet, E" uniqKey="Jamet E">E. Jamet</name></author><author><name sortKey="Rossignol, M" uniqKey="Rossignol M">M. Rossignol</name></author><author><name sortKey="Lafitte, C" uniqKey="Lafitte C">C. Lafitte</name></author><author><name sortKey="Borderies, G" uniqKey="Borderies G">G. Borderies</name></author><author><name sortKey="Jauneau, A" uniqKey="Jauneau A">A. Jauneau</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Campestre, M P" uniqKey="Campestre M">M. P. Campestre</name></author><author><name sortKey="Bordenave, C D" uniqKey="Bordenave C">C. D. Bordenave</name></author><author><name sortKey="Origone, A C" uniqKey="Origone A">A. C. Origone</name></author><author><name sortKey="Menendez, A B" uniqKey="Menendez A">A. B. Menéndez</name></author><author><name sortKey="Ruiz, O A" uniqKey="Ruiz O">O. A. Ruiz</name></author><author><name sortKey="Rodriguez, A A" uniqKey="Rodriguez A">A. A. Rodríguez</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cervelli, M" uniqKey="Cervelli M">M. Cervelli</name></author><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Polticelli, F" uniqKey="Polticelli F">F. Polticelli</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Mariottini, P" uniqKey="Mariottini P">P. Mariottini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cheng, W H" uniqKey="Cheng W">W. H. Cheng</name></author><author><name sortKey="Wang, F L" uniqKey="Wang F">F. L. Wang</name></author><author><name sortKey="Cheng, X Q" uniqKey="Cheng X">X. Q. Cheng</name></author><author><name sortKey="Zhu, Q H" uniqKey="Zhu Q">Q. H. Zhu</name></author><author><name sortKey="Sun, Y Q" uniqKey="Sun Y">Y. Q. Sun</name></author><author><name sortKey="Zhu, H G" uniqKey="Zhu H">H. G. Zhu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Clay, N K" uniqKey="Clay N">N. K. Clay</name></author><author><name sortKey="Nelson, T" uniqKey="Nelson T">T. Nelson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Cenci, F" uniqKey="Cenci F">F. Cenci</name></author><author><name sortKey="Cervelli, M" uniqKey="Cervelli M">M. Cervelli</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Mariottini, P" uniqKey="Mariottini P">P. Mariottini</name></author><author><name sortKey="Moreno, S" uniqKey="Moreno S">S. Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Rea, G" uniqKey="Rea G">G. Rea</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Rea, G" uniqKey="Rea G">G. Rea</name></author><author><name sortKey="Botta, M" uniqKey="Botta M">M. Botta</name></author><author><name sortKey="Corelli, F" uniqKey="Corelli F">F. Corelli</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author><author><name sortKey="Ghuge, S A" uniqKey="Ghuge S">S. A. Ghuge</name></author><author><name sortKey="Franchi, S" uniqKey="Franchi S">S. Franchi</name></author><author><name sortKey="De Lorenzo, G" uniqKey="De Lorenzo G">G. De Lorenzo</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Delis, C" uniqKey="Delis C">C. Delis</name></author><author><name sortKey="Dimou, M" uniqKey="Dimou M">M. Dimou</name></author><author><name sortKey="Flemetakis, E" uniqKey="Flemetakis E">E. Flemetakis</name></author><author><name sortKey="Aivalakis, G" uniqKey="Aivalakis G">G. Aivalakis</name></author><author><name sortKey="Katinakis, P" uniqKey="Katinakis P">P. Katinakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="De Pinto, M C" uniqKey="De Pinto M">M. C. De Pinto</name></author><author><name sortKey="Locato, V" uniqKey="Locato V">V. Locato</name></author><author><name sortKey="De Gara, L" uniqKey="De Gara L">L. De Gara</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Dewey, R E" uniqKey="Dewey R">R. E. Dewey</name></author><author><name sortKey="Xie, J" uniqKey="Xie J">J. Xie</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fincato, P" uniqKey="Fincato P">P. Fincato</name></author><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Ahou, A" uniqKey="Ahou A">A. Ahou</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fincato, P" uniqKey="Fincato P">P. Fincato</name></author><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Spedaletti, V" uniqKey="Spedaletti V">V. Spedaletti</name></author><author><name sortKey="Tavazza, R" uniqKey="Tavazza R">R. Tavazza</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fuell, C" uniqKey="Fuell C">C. Fuell</name></author><author><name sortKey="Elliot, K A" uniqKey="Elliot K">K. A. Elliot</name></author><author><name sortKey="Hanfrey, C C" uniqKey="Hanfrey C">C. C. Hanfrey</name></author><author><name sortKey="Franceschetti, M" uniqKey="Franceschetti M">M. Franceschetti</name></author><author><name sortKey="Michael, A J" uniqKey="Michael A">A. J. Michael</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ge, C" uniqKey="Ge C">C. Ge</name></author><author><name sortKey="Cui, X" uniqKey="Cui X">X. Cui</name></author><author><name sortKey="Wang, Y" uniqKey="Wang Y">Y. Wang</name></author><author><name sortKey="Hu, Y" uniqKey="Hu Y">Y. Hu</name></author><author><name sortKey="Fu, Z" uniqKey="Fu Z">Z. Fu</name></author><author><name sortKey="Zhang, D" uniqKey="Zhang D">D. Zhang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ghuge, S A" uniqKey="Ghuge S">S. A. Ghuge</name></author><author><name sortKey="Carucci, A" uniqKey="Carucci A">A. Carucci</name></author><author><name sortKey="Rodrigues Pousada, R A" uniqKey="Rodrigues Pousada R">R. A. Rodrigues-Pousada</name></author><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author><author><name sortKey="Franchi, S" uniqKey="Franchi S">S. Franchi</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ghuge, S A" uniqKey="Ghuge S">S. A. Ghuge</name></author><author><name sortKey="Carucci, A" uniqKey="Carucci A">A. Carucci</name></author><author><name sortKey="Rodrigues Pousada, R A" uniqKey="Rodrigues Pousada R">R. A. Rodrigues-Pousada</name></author><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author><author><name sortKey="Franchi, S" uniqKey="Franchi S">S. Franchi</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ghuge, S A" uniqKey="Ghuge S">S. A. Ghuge</name></author><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author><author><name sortKey="Carucci, A" uniqKey="Carucci A">A. Carucci</name></author><author><name sortKey="Rodrigues Pousada, R A" uniqKey="Rodrigues Pousada R">R. A. Rodrigues-Pousada</name></author><author><name sortKey="Franchi, S" uniqKey="Franchi S">S. Franchi</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gilroy, S" uniqKey="Gilroy S">S. Gilroy</name></author><author><name sortKey="Suzuki, N" uniqKey="Suzuki N">N. Suzuki</name></author><author><name sortKey="Miller, G" uniqKey="Miller G">G. Miller</name></author><author><name sortKey="Choi, W G" uniqKey="Choi W">W. G. Choi</name></author><author><name sortKey="Toyota, M" uniqKey="Toyota M">M. Toyota</name></author><author><name sortKey="Devireddy, A R" uniqKey="Devireddy A">A. R. Devireddy</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Heim, W G" uniqKey="Heim W">W. G. Heim</name></author><author><name sortKey="Sykes, K A" uniqKey="Sykes K">K. A. Sykes</name></author><author><name sortKey="Hildreth, S B" uniqKey="Hildreth S">S. B. Hildreth</name></author><author><name sortKey="Sun, J" uniqKey="Sun J">J. Sun</name></author><author><name sortKey="Lu, R H" uniqKey="Lu R">R.-H. Lu</name></author><author><name sortKey="Jelesko, J G" uniqKey="Jelesko J">J. G. Jelesko</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hou, Z H" uniqKey="Hou Z">Z.-H. Hou</name></author><author><name sortKey="Liu, G H" uniqKey="Liu G">G.-H. Liu</name></author><author><name sortKey="Wang, L X" uniqKey="Wang L">L.-X. Wang</name></author><author><name sortKey="Liu, X" uniqKey="Liu X">X. Liu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Jammes, F" uniqKey="Jammes F">F. Jammes</name></author><author><name sortKey="Leonhardt, N" uniqKey="Leonhardt N">N. Leonhardt</name></author><author><name sortKey="Tran, D" uniqKey="Tran D">D. Tran</name></author><author><name sortKey="Bousserouel, H" uniqKey="Bousserouel H">H. Bousserouel</name></author><author><name sortKey="Very, A A" uniqKey="Very A">A. A. Véry</name></author><author><name sortKey="Renou, J P" uniqKey="Renou J">J. P. Renou</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Jimenez Bremont, J F" uniqKey="Jimenez Bremont J">J. F. Jiménez-Bremont</name></author><author><name sortKey="Marina, M" uniqKey="Marina M">M. Marina</name></author><author><name sortKey="Guerrero Gonzalez, M" uniqKey="Guerrero Gonzalez M">M. Guerrero-González</name></author><author><name sortKey="De, L" uniqKey="De L">L. de</name></author><author><name sortKey="Rossi, F R" uniqKey="Rossi F">F. R. Rossi</name></author><author><name sortKey="Sanchez Rangel, D" uniqKey="Sanchez Rangel D">D. Sánchez-Rangel</name></author><author><name sortKey="Rodriguez Kessler, M" uniqKey="Rodriguez Kessler M">M. Rodríguez-Kessler</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kamada Nobusada, T" uniqKey="Kamada Nobusada T">T. Kamada-Nobusada</name></author><author><name sortKey="Hayashi, M" uniqKey="Hayashi M">M. Hayashi</name></author><author><name sortKey="Fukazawa, M" uniqKey="Fukazawa M">M. Fukazawa</name></author><author><name sortKey="Sakakibara, H" uniqKey="Sakakibara H">H. Sakakibara</name></author><author><name sortKey="Nishimura, M" uniqKey="Nishimura M">M. Nishimura</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="K Rkonen, A" uniqKey="K Rkonen A">A. Kärkönen</name></author><author><name sortKey="Kuchitsu, K" uniqKey="Kuchitsu K">K. Kuchitsu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Katoh, A" uniqKey="Katoh A">A. Katoh</name></author><author><name sortKey="Shoji, T" uniqKey="Shoji T">T. Shoji</name></author><author><name sortKey="Hashimoto, T" uniqKey="Hashimoto T">T. Hashimoto</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kim, D W" uniqKey="Kim D">D. W. Kim</name></author><author><name sortKey="Watanabe, K" uniqKey="Watanabe K">K. Watanabe</name></author><author><name sortKey="Murayama, C" uniqKey="Murayama C">C. Murayama</name></author><author><name sortKey="Izawa, S" uniqKey="Izawa S">S. Izawa</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Michael, A J" uniqKey="Michael A">A. J. Michael</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kollist, H" uniqKey="Kollist H">H. Kollist</name></author><author><name sortKey="Nuhkat, M" uniqKey="Nuhkat M">M. Nuhkat</name></author><author><name sortKey="Roelfsema, M R" uniqKey="Roelfsema M">M. R. Roelfsema</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kuehn, G D" uniqKey="Kuehn G">G. D. Kuehn</name></author><author><name sortKey="Rodriguez Garay, B" uniqKey="Rodriguez Garay B">B. Rodriguez-Garay</name></author><author><name sortKey="Bagga, S" uniqKey="Bagga S">S. Bagga</name></author><author><name sortKey="Phillips, G C" uniqKey="Phillips G">G. C. Phillips</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lim, T S" uniqKey="Lim T">T. S. Lim</name></author><author><name sortKey="Chitra, T R" uniqKey="Chitra T">T. R. Chitra</name></author><author><name sortKey="Han, P" uniqKey="Han P">P. Han</name></author><author><name sortKey="Pua, E C" uniqKey="Pua E">E. C. Pua</name></author><author><name sortKey="Yu, H" uniqKey="Yu H">H. Yu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Liu, T" uniqKey="Liu T">T. Liu</name></author><author><name sortKey="Kim, D W" uniqKey="Kim D">D. W. Kim</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Berberich, T" uniqKey="Berberich T">T. Berberich</name></author><author><name sortKey="Kusano, T" uniqKey="Kusano T">T. Kusano</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Liu, T" uniqKey="Liu T">T. Liu</name></author><author><name sortKey="Kim, D W" uniqKey="Kim D">D. W. Kim</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Berberich, T" uniqKey="Berberich T">T. Berberich</name></author><author><name sortKey="Kusano, T" uniqKey="Kusano T">T. Kusano</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Liu, T" uniqKey="Liu T">T. Liu</name></author><author><name sortKey="Kim, D W" uniqKey="Kim D">D. W. Kim</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Maeda, S" uniqKey="Maeda S">S. Maeda</name></author><author><name sortKey="Watanabe, S" uniqKey="Watanabe S">S. Watanabe</name></author><author><name sortKey="Kamio, Y" uniqKey="Kamio Y">Y. Kamio</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Marina, M" uniqKey="Marina M">M. Marina</name></author><author><name sortKey="Sirera, F V" uniqKey="Sirera F">F. V. Sirera</name></author><author><name sortKey="Rambla, J L" uniqKey="Rambla J">J. L. Rambla</name></author><author><name sortKey="Gonzalez, M E" uniqKey="Gonzalez M">M. E. Gonzalez</name></author><author><name sortKey="Blazquez, M A" uniqKey="Blazquez M">M. A. Blázquez</name></author><author><name sortKey="Carbonell, J" uniqKey="Carbonell J">J. Carbonell</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mcwilliam, H" uniqKey="Mcwilliam H">H. McWilliam</name></author><author><name sortKey="Li, W" uniqKey="Li W">W. Li</name></author><author><name sortKey="Uludag, M" uniqKey="Uludag M">M. Uludag</name></author><author><name sortKey="Squizzato, S" uniqKey="Squizzato S">S. Squizzato</name></author><author><name sortKey="Park, Y M" uniqKey="Park Y">Y. M. Park</name></author><author><name sortKey="Buso, N" uniqKey="Buso N">N. Buso</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Medda, R" uniqKey="Medda R">R. Medda</name></author><author><name sortKey="Bellelli, A" uniqKey="Bellelli A">A. Bellelli</name></author><author><name sortKey="Pe, P" uniqKey="Pe P">P. Peč</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Floris, G" uniqKey="Floris G">G. Floris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Medda, R" uniqKey="Medda R">R. Medda</name></author><author><name sortKey="Padiglia, A" uniqKey="Padiglia A">A. Padiglia</name></author><author><name sortKey="Finazzi Agr, A" uniqKey="Finazzi Agr A">A. Finazzi Agrò</name></author><author><name sortKey="Pedersen, J Z" uniqKey="Pedersen J">J. Z. Pedersen</name></author><author><name sortKey="Lorrai, A" uniqKey="Lorrai A">A. Lorrai</name></author><author><name sortKey="Floris, G" uniqKey="Floris G">G. Floris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mo, H" uniqKey="Mo H">H. Mo</name></author><author><name sortKey="Wang, X" uniqKey="Wang X">X. Wang</name></author><author><name sortKey="Zhang, Y" uniqKey="Zhang Y">Y. Zhang</name></author><author><name sortKey="Zhang, G" uniqKey="Zhang G">G. Zhang</name></author><author><name sortKey="Zhang, J F" uniqKey="Zhang J">J. F. Zhang</name></author><author><name sortKey="Ma, Z Y" uniqKey="Ma Z">Z. Y. Ma</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="M Ller, S G" uniqKey="M Ller S">S. G. Møller</name></author><author><name sortKey="Mcpherson, M J" uniqKey="Mcpherson M">M. J. McPherson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Monshausen, G B" uniqKey="Monshausen G">G. B. Monshausen</name></author><author><name sortKey="Bibikova, T N" uniqKey="Bibikova T">T. N. Bibikova</name></author><author><name sortKey="Messerli, M A" uniqKey="Messerli M">M. A. Messerli</name></author><author><name sortKey="Shi, C" uniqKey="Shi C">C. Shi</name></author><author><name sortKey="Gilroy, S" uniqKey="Gilroy S">S. Gilroy</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Paschalidis, K A" uniqKey="Paschalidis K">K. A. Paschalidis</name></author><author><name sortKey="Delis, I D" uniqKey="Delis I">I. D. Delis</name></author><author><name sortKey="Andriopoulou, A H" uniqKey="Andriopoulou A">A. H. Andriopoulou</name></author><author><name sortKey="Lagiotis, G D" uniqKey="Lagiotis G">G. D. Lagiotis</name></author><author><name sortKey="Yakoumakis, D I" uniqKey="Yakoumakis D">D. I. Yakoumakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Sanmartin, M" uniqKey="Sanmartin M">M. Sanmartin</name></author><author><name sortKey="Andriopoulou, A H" uniqKey="Andriopoulou A">A. H. Andriopoulou</name></author><author><name sortKey="Rojo, E" uniqKey="Rojo E">E. Rojo</name></author><author><name sortKey="Sanchez Serrano, J J" uniqKey="Sanchez Serrano J">J. J. Sanchez-Serrano</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Wu, J" uniqKey="Wu J">J. Wu</name></author><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Muller, K" uniqKey="Muller K">K. Müller</name></author><author><name sortKey="Linkies, A" uniqKey="Linkies A">A. Linkies</name></author><author><name sortKey="Vreeburg, R A" uniqKey="Vreeburg R">R. A. Vreeburg</name></author><author><name sortKey="Fry, S C" uniqKey="Fry S">S. C. Fry</name></author><author><name sortKey="Krieger Liszkay, A" uniqKey="Krieger Liszkay A">A. Krieger-Liszkay</name></author><author><name sortKey="Leubner Metzger, G" uniqKey="Leubner Metzger G">G. Leubner-Metzger</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Murata, Y" uniqKey="Murata Y">Y. Murata</name></author><author><name sortKey="Mori, I C" uniqKey="Mori I">I. C. Mori</name></author><author><name sortKey="Munemasa, S" uniqKey="Munemasa S">S. Munemasa</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Naconsie, M" uniqKey="Naconsie M">M. Naconsie</name></author><author><name sortKey="Kato, K" uniqKey="Kato K">K. Kato</name></author><author><name sortKey="Shoji, T" uniqKey="Shoji T">T. Shoji</name></author><author><name sortKey="Hashimoto, T" uniqKey="Hashimoto T">T. Hashimoto</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ono, Y" uniqKey="Ono Y">Y. Ono</name></author><author><name sortKey="Kim, D W" uniqKey="Kim D">D. W. Kim</name></author><author><name sortKey="Watanabe, K" uniqKey="Watanabe K">K. Watanabe</name></author><author><name sortKey="Sasaki, A" uniqKey="Sasaki A">A. Sasaki</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Berberich, T" uniqKey="Berberich T">T. Berberich</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Padiglia, A" uniqKey="Padiglia A">A. Padiglia</name></author><author><name sortKey="Medda, R" uniqKey="Medda R">R. Medda</name></author><author><name sortKey="Scanu, T" uniqKey="Scanu T">T. Scanu</name></author><author><name sortKey="Longu, S" uniqKey="Longu S">S. Longu</name></author><author><name sortKey="Rossi, A" uniqKey="Rossi A">A. Rossi</name></author><author><name sortKey="Floris, G" uniqKey="Floris G">G. Floris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pal, M" uniqKey="Pal M">M. Pál</name></author><author><name sortKey="Szalai, G" uniqKey="Szalai G">G. Szalai</name></author><author><name sortKey="Janda, T" uniqKey="Janda T">T. Janda</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Paschalidis, K A" uniqKey="Paschalidis K">K. A. Paschalidis</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Paschalidis, K A" uniqKey="Paschalidis K">K. A. Paschalidis</name></author><author><name sortKey="Toumi, I" uniqKey="Toumi I">I. Toumi</name></author><author><name sortKey="Moschou, N P" uniqKey="Moschou N">N. P. Moschou</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pegg, A E" uniqKey="Pegg A">A. E. Pegg</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pintus, F" uniqKey="Pintus F">F. Pintus</name></author><author><name sortKey="Span, D" uniqKey="Span D">D. Spanò</name></author><author><name sortKey="Floris, G" uniqKey="Floris G">G. Floris</name></author><author><name sortKey="Medda, R" uniqKey="Medda R">R. Medda</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Planas Portell, J" uniqKey="Planas Portell J">J. Planas-Portell</name></author><author><name sortKey="Gallart, M" uniqKey="Gallart M">M. Gallart</name></author><author><name sortKey="Tiburcio, A F" uniqKey="Tiburcio A">A. F. Tiburcio</name></author><author><name sortKey="Altabella, T" uniqKey="Altabella T">T. Altabella</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pottosin, I" uniqKey="Pottosin I">I. Pottosin</name></author><author><name sortKey="Velarde Buendia, A M" uniqKey="Velarde Buendia A">A. M. Velarde-Buendía</name></author><author><name sortKey="Bose, J" uniqKey="Bose J">J. Bose</name></author><author><name sortKey="Zepeda Jazo, I" uniqKey="Zepeda Jazo I">I. Zepeda-Jazo</name></author><author><name sortKey="Shabala, S" uniqKey="Shabala S">S. Shabala</name></author><author><name sortKey="Dobrovinskaya, O" uniqKey="Dobrovinskaya O">O. Dobrovinskaya</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Qu, Y" uniqKey="Qu Y">Y. Qu</name></author><author><name sortKey="An, Z" uniqKey="An Z">Z. An</name></author><author><name sortKey="Zhuang, B" uniqKey="Zhuang B">B. Zhuang</name></author><author><name sortKey="Jing, W" uniqKey="Jing W">W. Jing</name></author><author><name sortKey="Zhang, Q" uniqKey="Zhang Q">Q. Zhang</name></author><author><name sortKey="Zhang, W" uniqKey="Zhang W">W. Zhang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rea, G" uniqKey="Rea G">G. Rea</name></author><author><name sortKey="De Pinto, M C" uniqKey="De Pinto M">M. C. de Pinto</name></author><author><name sortKey="Tavazza, R" uniqKey="Tavazza R">R. Tavazza</name></author><author><name sortKey="Biondi, S" uniqKey="Biondi S">S. Biondi</name></author><author><name sortKey="Gobbi, V" uniqKey="Gobbi V">V. Gobbi</name></author><author><name sortKey="Ferrante, P" uniqKey="Ferrante P">P. Ferrante</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rea, G" uniqKey="Rea G">G. Rea</name></author><author><name sortKey="Metoui, O" uniqKey="Metoui O">O. Metoui</name></author><author><name sortKey="Infantino, A" uniqKey="Infantino A">A. Infantino</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Roach, T" uniqKey="Roach T">T. Roach</name></author><author><name sortKey="Colville, L" uniqKey="Colville L">L. Colville</name></author><author><name sortKey="Beckett, R P" uniqKey="Beckett R">R. P. Beckett</name></author><author><name sortKey="Minibayeva, F V" uniqKey="Minibayeva F">F. V. Minibayeva</name></author><author><name sortKey="Havaux, M" uniqKey="Havaux M">M. Havaux</name></author><author><name sortKey="Kranner, I" uniqKey="Kranner I">I. Kranner</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rodriguez, A A" uniqKey="Rodriguez A">A. A. Rodríguez</name></author><author><name sortKey="Maiale, S J" uniqKey="Maiale S">S. J. Maiale</name></author><author><name sortKey="Menendez, A B" uniqKey="Menendez A">A. B. Menéndez</name></author><author><name sortKey="Ruiz, O A" uniqKey="Ruiz O">O. A. Ruiz</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rossi, A" uniqKey="Rossi A">A. Rossi</name></author><author><name sortKey="Petruzzelli, R" uniqKey="Petruzzelli R">R. Petruzzelli</name></author><author><name sortKey="Agr, A F" uniqKey="Agr A">A. F. Agrò</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sagor, G H" uniqKey="Sagor G">G. H. Sagor</name></author><author><name sortKey="Inoue, M" uniqKey="Inoue M">M. Inoue</name></author><author><name sortKey="Kim, D W" uniqKey="Kim D">D. W. Kim</name></author><author><name sortKey="Kojima, S" uniqKey="Kojima S">S. Kojima</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Berberich, T" uniqKey="Berberich T">T. Berberich</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sagor, G H M" uniqKey="Sagor G">G. H. M. Sagor</name></author><author><name sortKey="Zhang, S" uniqKey="Zhang S">S. Zhang</name></author><author><name sortKey="Kojima, S" uniqKey="Kojima S">S. Kojima</name></author><author><name sortKey="Simm, S" uniqKey="Simm S">S. Simm</name></author><author><name sortKey="Berberich, T" uniqKey="Berberich T">T. Berberich</name></author><author><name sortKey="Kusano, T" uniqKey="Kusano T">T. Kusano</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Schopfer, P" uniqKey="Schopfer P">P. Schopfer</name></author><author><name sortKey="Liszkay, A" uniqKey="Liszkay A">A. Liszkay</name></author><author><name sortKey="Bechtold, M" uniqKey="Bechtold M">M. Bechtold</name></author><author><name sortKey="Frahry, G" uniqKey="Frahry G">G. Frahry</name></author><author><name sortKey="Wagner, A" uniqKey="Wagner A">A. Wagner</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sequera Mutiozabal, M I" uniqKey="Sequera Mutiozabal M">M. I. Sequera-Mutiozabal</name></author><author><name sortKey="Erban, A" uniqKey="Erban A">A. Erban</name></author><author><name sortKey="Kopka J, Atanasov K E" uniqKey="Kopka J A">Atanasov, K. E. Kopka J</name></author><author><name sortKey="Bastida, J" uniqKey="Bastida J">J. Bastida</name></author><author><name sortKey="Fotopoulos, V" uniqKey="Fotopoulos V">V. Fotopoulos</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Shoresh, M" uniqKey="Shoresh M">M. Shoresh</name></author><author><name sortKey="Spivak, M" uniqKey="Spivak M">M. Spivak</name></author><author><name sortKey="Bernstein, N" uniqKey="Bernstein N">N. Bernstein</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Strohm, A K" uniqKey="Strohm A">A. K. Strohm</name></author><author><name sortKey="Vaughn, L M" uniqKey="Vaughn L">L. M. Vaughn</name></author><author><name sortKey="Masson, P H" uniqKey="Masson P">P. H. Masson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Takahashi, T" uniqKey="Takahashi T">T. Takahashi</name></author><author><name sortKey="Kakehi, J" uniqKey="Kakehi J">J. Kakehi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Takahashi, Y" uniqKey="Takahashi Y">Y. Takahashi</name></author><author><name sortKey="Cong, R" uniqKey="Cong R">R. Cong</name></author><author><name sortKey="Sagor, G H" uniqKey="Sagor G">G. H. Sagor</name></author><author><name sortKey="Niitsu, M" uniqKey="Niitsu M">M. Niitsu</name></author><author><name sortKey="Berberich, T" uniqKey="Berberich T">T. Berberich</name></author><author><name sortKey="Kusano, T" uniqKey="Kusano T">T. Kusano</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tamura, K" uniqKey="Tamura K">K. Tamura</name></author><author><name sortKey="Peterson, D" uniqKey="Peterson D">D. Peterson</name></author><author><name sortKey="Peterson, N" uniqKey="Peterson N">N. Peterson</name></author><author><name sortKey="Stecher, G" uniqKey="Stecher G">G. Stecher</name></author><author><name sortKey="Nei, M" uniqKey="Nei M">M. Nei</name></author><author><name sortKey="Kumar, S" uniqKey="Kumar S">S. Kumar</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Tempera, G" uniqKey="Tempera G">G. Tempera</name></author><author><name sortKey="Viceconte, N" uniqKey="Viceconte N">N. Viceconte</name></author><author><name sortKey="Saccoccio, S" uniqKey="Saccoccio S">S. Saccoccio</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author><author><name sortKey="Rossi, M N" uniqKey="Rossi M">M. N. Rossi</name></author><author><name sortKey="Saccuti, G" uniqKey="Saccuti G">G. Saccuti</name></author><author><name sortKey="Perez Amador, M A" uniqKey="Perez Amador M">M. A. Perez-Amador</name></author><author><name sortKey="Polticelli, F" uniqKey="Polticelli F">F. Polticelli</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author><author><name sortKey="Schinina, M E" uniqKey="Schinina M">M. E. Schininà</name></author><author><name sortKey="Cecconi, F" uniqKey="Cecconi F">F. Cecconi</name></author><author><name sortKey="Di Agostino, S" uniqKey="Di Agostino S">S. Di Agostino</name></author><author><name sortKey="Manera, F" uniqKey="Manera F">F. Manera</name></author><author><name sortKey="Rea, G" uniqKey="Rea G">G. Rea</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tiburcio, A F" uniqKey="Tiburcio A">A. F. Tiburcio</name></author><author><name sortKey="Altabella, T" uniqKey="Altabella T">T. Altabella</name></author><author><name sortKey="Bitrian, M" uniqKey="Bitrian M">M. Bitrián</name></author><author><name sortKey="Alcazar, R" uniqKey="Alcazar R">R. Alcázar</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tipping, A J" uniqKey="Tipping A">A. J. Tipping</name></author><author><name sortKey="Mcpherson, M J" uniqKey="Mcpherson M">M. J. McPherson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tisi, A" uniqKey="Tisi A">A. Tisi</name></author><author><name sortKey="Federico, R" uniqKey="Federico R">R. Federico</name></author><author><name sortKey="Moreno, S" uniqKey="Moreno S">S. Moreno</name></author><author><name sortKey="Lucretti, S" uniqKey="Lucretti S">S. Lucretti</name></author><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Roubelakis Angelakis, K A" uniqKey="Roubelakis Angelakis K">K. A. Roubelakis-Angelakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tsaniklidis, G" uniqKey="Tsaniklidis G">G. Tsaniklidis</name></author><author><name sortKey="Kotsiras, A" uniqKey="Kotsiras A">A. Kotsiras</name></author><author><name sortKey="Tsafouros, A" uniqKey="Tsafouros A">A. Tsafouros</name></author><author><name sortKey="Roussos, P A" uniqKey="Roussos P">P. A. Roussos</name></author><author><name sortKey="Aivalakis, G" uniqKey="Aivalakis G">G. Aivalakis</name></author><author><name sortKey="Katinakis, P" uniqKey="Katinakis P">P. Katinakis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tsukagoshi, H" uniqKey="Tsukagoshi H">H. Tsukagoshi</name></author><author><name sortKey="Busch, W" uniqKey="Busch W">W. Busch</name></author><author><name sortKey="Benfey, P N" uniqKey="Benfey P">P. N. Benfey</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tun, N N" uniqKey="Tun N">N. N. Tun</name></author><author><name sortKey="Santa Catarina, C" uniqKey="Santa Catarina C">C. Santa-Catarina</name></author><author><name sortKey="Begum, T" uniqKey="Begum T">T. Begum</name></author><author><name sortKey="Silveira, V" uniqKey="Silveira V">V. Silveira</name></author><author><name sortKey="Handro, W" uniqKey="Handro W">W. Handro</name></author><author><name sortKey="Floh, E I" uniqKey="Floh E">E. I. Floh</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wang, W" uniqKey="Wang W">W. Wang</name></author><author><name sortKey="Liu, J H" uniqKey="Liu J">J. H. Liu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wimalasekera, R" uniqKey="Wimalasekera R">R. Wimalasekera</name></author><author><name sortKey="Schaarschmidt, F" uniqKey="Schaarschmidt F">F. Schaarschmidt</name></author><author><name sortKey="Angelini, R" uniqKey="Angelini R">R. Angelini</name></author><author><name sortKey="Cona, A" uniqKey="Cona A">A. Cona</name></author><author><name sortKey="Tavladoraki, P" uniqKey="Tavladoraki P">P. Tavladoraki</name></author><author><name sortKey="Scherer, G F" uniqKey="Scherer G">G. F. Scherer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wimalasekera, R" uniqKey="Wimalasekera R">R. Wimalasekera</name></author><author><name sortKey="Villar, C" uniqKey="Villar C">C. Villar</name></author><author><name sortKey="Begum, T" uniqKey="Begum T">T. Begum</name></author><author><name sortKey="Scherer, G F" uniqKey="Scherer G">G. F. Scherer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wu, J" uniqKey="Wu J">J. Wu</name></author><author><name sortKey="Shang, Z" uniqKey="Shang Z">Z. Shang</name></author><author><name sortKey="Wu, J" uniqKey="Wu J">J. Wu</name></author><author><name sortKey="Jiang, X" uniqKey="Jiang X">X. Jiang</name></author><author><name sortKey="Moschou, P N" uniqKey="Moschou P">P. N. Moschou</name></author><author><name sortKey="Sun, W" uniqKey="Sun W">W. Sun</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yoda, H" uniqKey="Yoda H">H. Yoda</name></author><author><name sortKey="Yamaguchi, Y" uniqKey="Yamaguchi Y">Y. Yamaguchi</name></author><author><name sortKey="Sano, H" uniqKey="Sano H">H. Sano</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yoshimoto, K" uniqKey="Yoshimoto K">K. Yoshimoto</name></author><author><name sortKey="Takamura, H" uniqKey="Takamura H">H. Takamura</name></author><author><name sortKey="Kadota, I" uniqKey="Kadota I">I. Kadota</name></author><author><name sortKey="Motose, H" uniqKey="Motose H">H. Motose</name></author><author><name sortKey="Takahashi, T" uniqKey="Takahashi T">T. Takahashi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zarei, A" uniqKey="Zarei A">A. Zarei</name></author><author><name sortKey="Trobacher, C P" uniqKey="Trobacher C">C. P. Trobacher</name></author><author><name sortKey="Cooke, A R" uniqKey="Cooke A">A. R. Cooke</name></author><author><name sortKey="Meyers, A J" uniqKey="Meyers A">A. J. Meyers</name></author><author><name sortKey="Hall, J C" uniqKey="Hall J">J. C. Hall</name></author><author><name sortKey="Shelp, B J" uniqKey="Shelp B">B. J. Shelp</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zarei, A" uniqKey="Zarei A">A. Zarei</name></author><author><name sortKey="Trobacher, C P" uniqKey="Trobacher C">C. P. Trobacher</name></author><author><name sortKey="Shelp, B J" uniqKey="Shelp B">B. J. Shelp</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zarza, X" uniqKey="Zarza X">X. Zarza</name></author><author><name sortKey="Atanasov, K E" uniqKey="Atanasov K">K. E. Atanasov</name></author><author><name sortKey="Marco, F" uniqKey="Marco F">F. Marco</name></author><author><name sortKey="Arbona, V" uniqKey="Arbona V">V. Arbona</name></author><author><name sortKey="Carrasco, P" uniqKey="Carrasco P">P. Carrasco</name></author><author><name sortKey="Kopka, J" uniqKey="Kopka J">J. Kopka</name></author></analytic></biblStruct></listBibl></div1></back></TEI><pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Front Plant Sci</journal-id><journal-id journal-id-type="iso-abbrev">Front Plant Sci</journal-id><journal-id journal-id-type="publisher-id">Front. Plant Sci.</journal-id><journal-title-group><journal-title>Frontiers in Plant Science</journal-title></journal-title-group><issn pub-type="epub">1664-462X</issn><publisher><publisher-name>Frontiers Media S.A.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">27446096</article-id><article-id pub-id-type="pmc">4923165</article-id><article-id pub-id-type="doi">10.3389/fpls.2016.00824</article-id><article-categories><subj-group subj-group-type="heading"><subject>Plant Science</subject><subj-group><subject>Mini Review</subject></subj-group></subj-group></article-categories><title-group><article-title>Copper-Containing Amine Oxidases and FAD-Dependent Polyamine Oxidases Are Key Players in Plant Tissue Differentiation and Organ Development</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Tavladoraki</surname><given-names>Paraskevi</given-names></name><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/135349/overview"></uri></contrib><contrib contrib-type="author"><name><surname>Cona</surname><given-names>Alessandra</given-names></name></contrib><contrib contrib-type="author"><name><surname>Angelini</surname><given-names>Riccardo</given-names></name><xref ref-type="author-notes" rid="fn001"><sup>*</sup></xref><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/188569/overview"></uri></contrib></contrib-group><aff><institution>Laboratory of Biochemistry, Physiology and Biotechnology of Plants, Department of Science, University “Roma Tre”</institution><country>Rome, Italy</country></aff><author-notes><fn fn-type="edited-by"><p>Edited by: Juan Francisco Jimenez Bremont, Instituto Potosino de Investigacion Cientifica y Tecnologica, Mexico</p></fn><fn fn-type="edited-by"><p>Reviewed by: Andres Garriz, Instituto de Investigaciones Biotecnológicas Instituto Tecnológico Chascomús, Argentina; Anna Kärkönen, University of Helsinki, Finland</p></fn><corresp id="fn001">*Correspondence: Riccardo Angelini <email xlink:type="simple">riccardo.angelini@uniroma3.it</email></corresp><fn fn-type="other" id="fn002"><p>This article was submitted to Plant Physiology, a section of the journal Frontiers in Plant Science</p></fn></author-notes><pub-date pub-type="epub"><day>28</day><month>6</month><year>2016</year></pub-date><pub-date pub-type="collection"><year>2016</year></pub-date><volume>7</volume><elocation-id>824</elocation-id><history><date date-type="received"><day>22</day><month>3</month><year>2016</year></date><date date-type="accepted"><day>26</day><month>5</month><year>2016</year></date></history><permissions><copyright-statement>Copyright © 2016 Tavladoraki, Cona and Angelini.</copyright-statement><copyright-year>2016</copyright-year><copyright-holder>Tavladoraki, Cona and Angelini</copyright-holder><license xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</license-p></license></permissions><abstract><p>Plant polyamines are catabolized by two classes of amine oxidases, the copper amine oxidases (CuAOs) and the flavin adenine dinucleotide (FAD)-dependent polyamine oxidases (PAOs). These enzymes differ to each other in substrate specificity, catalytic mechanism and subcellular localization. CuAOs and PAOs contribute to several physiological processes both through the control of polyamine homeostasis and as sources of biologically-active reaction products. CuAOs and PAOs have been found at high level in the cell-wall of several species belonging to Fabaceae and Poaceae families, respectively, especially in tissues fated to undertake extensive wall loosening/stiffening events and/or in cells undergoing programmed cell death (PCD). Apoplastic CuAOs and PAOs have been shown to play a key role as a source of H<sub>2</sub>O<sub>2</sub> in light- or developmentally-regulated differentiation events, thus influencing cell-wall architecture and maturation as well as PCD. Moreover, growing evidence suggests a key role of intracellular CuAOs and PAOs in several facets of plant development. Here, we discuss recent advances in understanding the contribution of different CuAOs/PAOs, as well as their cross-talk with different intracellular and apoplastic metabolic pathways, in tissue differentiation and organ development.</p></abstract><kwd-group><kwd>polyamines</kwd><kwd>copper amine oxidases</kwd><kwd>FAD-dependent polyamine oxidases</kwd><kwd>cell-wall</kwd><kwd>tissue differentiation</kwd><kwd>reactive oxygen species</kwd><kwd>growth regulation</kwd><kwd>programmed cell death</kwd></kwd-group><counts><fig-count count="1"></fig-count><table-count count="1"></table-count><equation-count count="0"></equation-count><ref-count count="98"></ref-count><page-count count="11"></page-count><word-count count="7879"></word-count></counts></article-meta></front><body><sec id="s1"><title>Copper-containing amine oxidases and FAD-dependent polyamine oxidases: a complex network</title><p>In plants, the polyamines (PAs) putrescine (Put), cadaverine (Cad), spermidine (Spd), spermine (Spm), and thermospermine (Therm-Spm) are involved in several physiological processes, such as cell proliferation, differentiation and defense responses (Takahashi and Kakehi, <xref rid="B78" ref-type="bibr">2010</xref>; Marina et al., <xref rid="B44" ref-type="bibr">2013</xref>; Jiménez-Bremont et al., <xref rid="B33" ref-type="bibr">2014</xref>; Tiburcio et al., <xref rid="B84" ref-type="bibr">2014</xref>; Pál et al., <xref rid="B59" ref-type="bibr">2015</xref>; Strohm et al., <xref rid="B77" ref-type="bibr">2015</xref>; Yoshimoto et al., <xref rid="B95" ref-type="bibr">2016</xref>). PAs are oxidized by a heterogeneous class of enzymes which includes copper-containing amine oxidases (CuAOs) and FAD-dependent polyamine oxidases (PAOs) (Cona et al., <xref rid="B15" ref-type="bibr">2006a</xref>; Angelini et al., <xref rid="B6" ref-type="bibr">2010</xref>; Tavladoraki et al., <xref rid="B81" ref-type="bibr">2012</xref>). CuAOs oxidize mainly Put and Cad, and less efficiently Spd and Spm at the primary amino groups, producing ammonia, H<sub>2</sub>O<sub>2</sub> and an aminoaldehyde and are thus considered involved in PA terminal catabolism. In <italic>Arabidopsis thaliana</italic> 10 <italic>CuAO</italic> genes are present, among which only eight encode for putative functional CuAOs [<italic>AtCuAO</italic>α<italic>1</italic> (<italic>At1g31670</italic>); <italic>AtCuAO</italic>α<italic>2</italic> (<italic>At1g31690</italic>); <italic>AtCuAO</italic>α<italic>3</italic> (<italic>At1g31710</italic>; previously <italic>AtCuAO2</italic>); <italic>AtCuAO</italic>β (<italic>At4g14940</italic>; prev. <italic>ATAO1</italic> or <italic>AtAO1</italic>); <italic>AtCuAO</italic>γ<italic>1</italic> (<italic>At1g62810</italic>; prev. <italic>AtCuAO1</italic>); <italic>AtCuAO</italic>γ<italic>2</italic> (<italic>At3g43670</italic>); <italic>AtCuAO</italic>δ (At4g12290, prev. <italic>AtCuAO</italic>δ<italic>2</italic>); <italic>AtCuAO</italic>ζ (<italic>At2g42490</italic>; prev. <italic>AtCuAO3</italic> or <italic>AtCuAO1</italic>)]<xref ref-type="fn" rid="fn0001"><sup>1</sup></xref> (Figure <xref ref-type="fig" rid="F1">1</xref>). The remaining two genes <italic>AtCuAO</italic>ε<italic>1</italic> (<italic>At4g12270</italic>; prev. <italic>AtCuAO</italic>ε) and <italic>AtCuAO</italic>ε<italic>2</italic> (<italic>At4g12280</italic>; prev. <italic>AtCuAO</italic>δ<italic>1</italic>) are consecutive fragments of a copy of <italic>AtCuAO</italic>δ gene. Phylogenetic analysis evidenced that plant CuAOs form three clades (I-III), clade I being composed of three subgroups (Ia-Ic) and clade II of two (IIa and IIb; Figure <xref ref-type="fig" rid="F1">1A</xref>). Furthermore, genomic sequence analysis demonstrated that the Arabidopsis CuAOs of clades I and II, but not of clade III, present a similar gene structure to each other with three introns at conserved positions (Figure <xref ref-type="fig" rid="F1">1B</xref>). This suggests that <italic>AtCuAO</italic>α<italic>1</italic> to <italic>AtCuAO</italic>δ are recent derivatives of a common ancestor.</p><fig id="F1" position="float"><label>Figure 1</label><caption><p><bold>Sequence analysis of plant CuAOs. (A)</bold> Phylogenetic analysis of CuAOs from selected spermatophytes. Plant CuAOs form three principal supported clades (I-III). Clade I consists of three groups (groups a and b consisting of CuAOs from dicots and group c from monocots), the reciprocal relationship of which is not well resolved. For simplicity reasons, for each distinct group only a representative CuAO from each plant species was considered. Amino acid sequences were aligned with ClustalW (McWilliam et al., <xref rid="B45" ref-type="bibr">2013</xref>) and phylogenetic analysis was performed using MEGA5 (Tamura et al., <xref rid="B80" ref-type="bibr">2011</xref>) software with the neighbor-joining algorithm. Bootstrap values obtained with 1000 replicates are indicated at the nodes. Accession number of proteins are indicated in Supplementary Table <xref ref-type="supplementary-material" rid="SM1">S1</xref>. <bold>(B)</bold> Genomic sequence analysis of Arabidopsis <italic>CuAOs</italic> (<italic>AtCuAOs</italic>). Black arrows show not conserved intron positions, while arrows of the same color indicate conserved intron positions. All <italic>AtCuAOs</italic> of clades I and II have three introns at conserved positions which suggests a recent common ancestor. However, based on the presence of additional introns, some of them placed at positions conserved among the members of the same group, but not among those of different groups, an independent evolution of the <italic>AtCuAOs</italic> from the different groups can be suggested. <italic>AtCuAO</italic>ζ of clade III appears evolutionarily distant from <italic>AtCuAOs</italic> of clade I and II. Amt, <italic>Amborella trichopoda</italic>; Bj, <italic>Brassica juncea</italic>; Ca, <italic>Cicer arietinum</italic>; ELAO, CuAO from latex of <italic>Euphorbia characias</italic>; Gm, <italic>Glycine max</italic>; Hv, <italic>Hordeum vulgare</italic>; LSAO, CuAO from seedlings of <italic>Lens culinaris</italic>; Md, <italic>Malus domestica</italic>; Mt, <italic>Medicago truncatula</italic>; Nt, <italic>Nicotiana tabacum</italic>; Os, <italic>Oryza sativa</italic>; PSAO, CuAO from seedlings of <italic>Pisum sativum</italic>; Psy, <italic>Pinus sylvestris</italic>; Pt, <italic>Populus trichocarpa</italic>; Rc, <italic>Ricinus communis</italic>; Sb, <italic>Sorghum bicolor</italic>; Sl, <italic>Solanum lycopersicum</italic>; Vv, <italic>Vitis vinifera</italic>; Zm, <italic>Zea mays</italic>.</p></caption><graphic xlink:href="fpls-07-00824-g0001"></graphic></fig><p>AtCuAOβ (clade Ic), AtCuAOγ1 (clade IIa) as well as <italic>Pisum sativum, Lens culinaris</italic> and <italic>Euphorbia characias</italic> CuAOs (PSAO, LSAO, and ELAO, respectively; clade Ia) are localized in the apoplast (Rossi et al., <xref rid="B71" ref-type="bibr">1992</xref>; Tipping and McPherson, <xref rid="B85" ref-type="bibr">1995</xref>; Møller and McPherson, <xref rid="B49" ref-type="bibr">1998</xref>; Padiglia et al., <xref rid="B58" ref-type="bibr">2002</xref>; Boudart et al., <xref rid="B9" ref-type="bibr">2005</xref>; Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref>), whereas AtCuAOζ, <italic>Malus domestica</italic> CuAO1 (MdAO1) and the other members of clade III in peroxisomes (Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref>; Naconsie et al., <xref rid="B56" ref-type="bibr">2014</xref>; Qu et al., <xref rid="B66" ref-type="bibr">2014</xref>; Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref>; Table <xref ref-type="table" rid="T1">1</xref>). Peroxisomal localization was also shown for AtCuAOα3 (Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref>) despite the apparent lack of canonical signal for peroxisomal localization and the fact that it is clustered together with the extracellular PSAO and LSAO. For MdAO2, which is clustered together with AtCuAOδ in clade IIb, both intracellular and apoplastic localization was shown (Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref>).</p><table-wrap id="T1" position="float"><label>Table 1</label><caption><p><bold>Characteristics and functions of plant CuAOs and PAOs</bold>.</p></caption><table frame="hsides" rules="groups"><thead><tr><th rowspan="1" colspan="1"></th><th rowspan="1" colspan="1"></th><th valign="top" align="left" rowspan="1" colspan="1"><bold>Localization</bold></th><th valign="top" align="left" rowspan="1" colspan="1"><bold>Substrate Preference</bold></th><th valign="top" align="left" rowspan="1" colspan="1"><bold>Function</bold></th><th valign="top" align="left" rowspan="1" colspan="1"><bold>References</bold></th></tr></thead><tbody><tr style="background-color:#bbbdc0"><td valign="top" align="left" colspan="6" rowspan="1"><bold>COPPER AMINE OXIDASES</bold></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade la</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">AtCuAOα1<xref ref-type="table-fn" rid="TN1"><sup>a</sup></xref></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">AtCuAOα2</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">AtCuAOα3</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Peroxisomes</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Put, Spd</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">PSAO</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Put, Spd, Spm</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Tipping and McPherson, <xref rid="B85" ref-type="bibr">1995</xref>; Moschou et al., <xref rid="B53" ref-type="bibr">2012</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">ELAO</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Put, Benzylamine, Tyramine</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Pintus et al., <xref rid="B63" ref-type="bibr">2013</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">LSAO</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Put, Spd, Spm, Tryptamine</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Rossi et al., <xref rid="B71" ref-type="bibr">1992</xref>; Medda et al., <xref rid="B47" ref-type="bibr">1997</xref>; Tavladoraki et al., <xref rid="B81" ref-type="bibr">2012</xref></td></tr><tr style="border-bottom: thin solid #000000;"><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">CaCuAO</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Put</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Wound healing, defense response</td><td valign="top" align="left" style="background-color:#d3aed2" rowspan="1" colspan="1">Rea et al., <xref rid="B68" ref-type="bibr">2002</xref></td></tr><tr style="border-bottom: thin solid #000000;"><td valign="top" align="left" rowspan="1" colspan="1">Clade Ib</td><td valign="top" align="left" style="background-color:#faf8ce" rowspan="1" colspan="1">AtCuAOβ</td><td valign="top" align="left" style="background-color:#faf8ce" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#faf8ce" rowspan="1" colspan="1">Put, Spd</td><td valign="top" align="left" style="background-color:#faf8ce" rowspan="1" colspan="1">Vascular development</td><td valign="top" align="left" style="background-color:#faf8ce" rowspan="1" colspan="1">Møller and McPherson, <xref rid="B49" ref-type="bibr">1998</xref>; Ghuge et al., <xref rid="B26" ref-type="bibr">2015a</xref></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade IIa</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">AtCuAOγ1</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">Put, Spd</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">PA- and ABA-mediated NO production</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">Wimalasekera et al., <xref rid="B92" ref-type="bibr">2011</xref>; Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref></td></tr><tr style="border-bottom: thin solid #000000;"><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">AtCuAOγ2</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d6eacd" rowspan="1" colspan="1">–</td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade IIb</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">AtCuAOδ</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">–</td></tr><tr style="border-bottom: thin solid #000000;"><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">MdAO2</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">2-Phenylethylamine, Tyramine, Ethanolamine, Ethylamine, Tryptamine</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">Fruit flavor, flower fragance</td><td valign="top" align="left" style="background-color:#fae9d9" rowspan="1" colspan="1">Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade III</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">AtCuAOζ</td><td style="background-color:#d6eef2" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Put, Spd, <italic>N</italic>-methyl-Put, Cad</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">ABA-induced stomatal closure</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref>; Naconsie et al., <xref rid="B56" ref-type="bibr">2014</xref>; Qu et al., <xref rid="B66" ref-type="bibr">2014</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">NtDAO1</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Peroxisomes</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Put, <italic>N</italic>-methyl-Put, Cad</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Naconsie et al., <xref rid="B56" ref-type="bibr">2014</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">MdAO1</td><td style="background-color:#d6eef2" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Dap, Put, Cad</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Nt-MPO1</td><td style="background-color:#d6eef2" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1"><italic>N</italic>-methyl-Put, <italic>N</italic>-methyl-Dap, Put, Dap, Cad</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Alkaloid synthesis</td><td valign="top" align="left" style="background-color:#d6eef2" rowspan="1" colspan="1">Katoh et al., <xref rid="B36" ref-type="bibr">2007</xref>; Naconsie et al., <xref rid="B56" ref-type="bibr">2014</xref></td></tr><tr style="background-color:#bbbdc0"><td valign="top" align="left" colspan="6" rowspan="1"><bold>POLYAMINE OXIDASES</bold></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade I</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">AtPAO1</td><td valign="middle" align="left" rowspan="2" style="background-color:#f498c0" colspan="1">Cytosol</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">Nor-Spm, Therm-Spm, Spm</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">Stress response</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">Tavladoraki et al., <xref rid="B82" ref-type="bibr">2006</xref>; Takahashi et al., <xref rid="B79" ref-type="bibr">2010</xref>; Sagor et al., <xref rid="B73" ref-type="bibr">2016</xref></td></tr><tr style="border-bottom: thin solid #000000;"><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">GhPAO1</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">Spm</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">Defense response, differentiation of embryogenic callus</td><td valign="top" align="left" style="background-color:#f498c0" rowspan="1" colspan="1">Cheng et al., <xref rid="B12" ref-type="bibr">2015</xref>; Mo et al., <xref rid="B48" ref-type="bibr">2015</xref></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade II</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">ZmPAO1</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Spd, Spm</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Cell wall differentiation</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Cona et al., <xref rid="B15" ref-type="bibr">2006a</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">HvPAO1</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Cervelli et al., <xref rid="B11" ref-type="bibr">2001</xref>; Cona et al., <xref rid="B15" ref-type="bibr">2006a</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">HvPAO2</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Vacuole</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Spm, Spd</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Cervelli et al., <xref rid="B11" ref-type="bibr">2001</xref>; Cona et al., <xref rid="B15" ref-type="bibr">2006a</xref></td></tr><tr style="border-bottom: thin solid #000000;"><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">OsPAO7</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Apoplast</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Spm, Spd, <italic>N</italic><sup>1</sup>-acetyl-Spm</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#daebf3" rowspan="1" colspan="1">Liu et al., <xref rid="B43" ref-type="bibr">2014b</xref></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade III</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">AtPAO5</td><td style="background-color:#cee295" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Spm, Therm-Spm, Nor-Spm, <italic>N</italic><sup>1</sup>-acetyl-Spm</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Polyamine homeostasis, plant growth, stress response</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>; Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Zarza et al., <xref rid="B98" ref-type="bibr">2016</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">SelPAO5</td><td style="background-color:#cee295" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Therm-Spm, Spm, Nor-Spm, <italic>N</italic><sup>1</sup>-acetyl-Spm</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Sagor et al., <xref rid="B72" ref-type="bibr">2015</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">OsPAO1</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Cytosol</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Spm, Therm-Spm, Nor-Spm, <italic>N</italic><sup>1</sup>-acetyl-Spm</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Plant growth</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>,<xref rid="B42" ref-type="bibr">c</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">BjPAO1</td><td style="background-color:#cee295" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Shoot regeneration</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Lim et al., <xref rid="B40" ref-type="bibr">2006</xref></td></tr><tr style="border-bottom: thin solid #000000;"><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">GhPAO4</td><td style="background-color:#cee295" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Differentiation of embryogenic callus</td><td valign="top" align="left" style="background-color:#cee295" rowspan="1" colspan="1">Cheng et al., <xref rid="B12" ref-type="bibr">2015</xref></td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Clade IV</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">AtPAO2</td><td style="background-color:#8ad2d7" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Spm, Spd, Nor-Spm</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Stress response</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Moschou et al., <xref rid="B52" ref-type="bibr">2008b</xref>; Takahashi et al., <xref rid="B79" ref-type="bibr">2010</xref>; Fincato et al., <xref rid="B23" ref-type="bibr">2011</xref>; Wimalasekera et al., <xref rid="B91" ref-type="bibr">2015</xref>; Sagor et al., <xref rid="B73" ref-type="bibr">2016</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">AtPAO3</td><td valign="middle" align="left" rowspan="2" style="background-color:#8ad2d7" colspan="1">Peroxisomes</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Spd, Spm, Nor-Spm</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Pollen tip growth</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Moschou et al., <xref rid="B52" ref-type="bibr">2008b</xref>; Takahashi et al., <xref rid="B79" ref-type="bibr">2010</xref>; Fincato et al., <xref rid="B23" ref-type="bibr">2011</xref>; Wu et al., <xref rid="B93" ref-type="bibr">2010</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">AtPAO4</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Spm</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Senescence</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Moschou et al., <xref rid="B52" ref-type="bibr">2008b</xref>; Kamada-Nobusada et al., <xref rid="B34" ref-type="bibr">2008</xref>; Takahashi et al., <xref rid="B79" ref-type="bibr">2010</xref>; Fincato et al., <xref rid="B23" ref-type="bibr">2011</xref>; Sequera-Mutiozabal et al., <xref rid="B75" ref-type="bibr">2016</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">OsPAO3</td><td style="background-color:#8ad2d7" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Spd, Nor-Spm</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Ono et al., <xref rid="B57" ref-type="bibr">2012</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">OsPAO4</td><td style="background-color:#8ad2d7" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Spm, Therm-Spm, Nor-Spm</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Ono et al., <xref rid="B57" ref-type="bibr">2012</xref></td></tr><tr><td rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">OsPAO5</td><td style="background-color:#8ad2d7" rowspan="1" colspan="1"></td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Spm, Therm-Spm, Nor-Spm</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">–</td><td valign="top" align="left" style="background-color:#8ad2d7" rowspan="1" colspan="1">Ono et al., <xref rid="B57" ref-type="bibr">2012</xref></td></tr></tbody></table><table-wrap-foot><fn id="TN1"><label>a</label><p><italic>At, Arabidopsis thaliana; Bj, Brassica juncea; Ca, Cicer arietinum; Gh, Gossypium hirsutum; Hv, Hordeum vulgare; Md, Malus domestica; Nt, Nicotiana tabacum; Os, Oryza sativa; Sel, Selaginella lepidophylla; SI, Solanum lycopersicum; Zm, Zea mays. ELAO, LSAO, and PSAO: CuAO from Euphorbia characias latex. Lens culinaris seedlings and Pisum sativum seedlings, respectively</italic>.</p></fn></table-wrap-foot></table-wrap><p>Although, most of the so far characterized CuAOs, such as AtCuAOβ, AtCuAOγ1, AtCuAOα3, AtCuAOζ, PSAO, LSAO, and <italic>Nicotiana tabacum</italic> CuAO1 (NtDAO1), oxidize mainly Put, Cad, and Spd (Rossi et al., <xref rid="B71" ref-type="bibr">1992</xref>; Tipping and McPherson, <xref rid="B85" ref-type="bibr">1995</xref>; Møller and McPherson, <xref rid="B49" ref-type="bibr">1998</xref>; Planas-Portell et al., <xref rid="B64" ref-type="bibr">2013</xref>; Naconsie et al., <xref rid="B56" ref-type="bibr">2014</xref>), MdAO1 of clade III shows preference for 1,3-diaminopropane (Dap), having no activity with Spd (Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref>). Furthermore, AtCuAOζ and NtDAO1 oxidize also <italic>N</italic>-methyl-Put, though less efficiently than the non-methylated diamine. Thus, they differ from the <italic>N. tabacum N</italic>-methylputrescine oxidase (Nt-MPO1), which shows preference for <italic>N</italic>-methyl-Put and is involved in nicotine biosynthesis, although all three proteins are clustered together in clade III (Heim et al., <xref rid="B30" ref-type="bibr">2007</xref>; Katoh et al., <xref rid="B36" ref-type="bibr">2007</xref>; Dewey and Xie, <xref rid="B20" ref-type="bibr">2013</xref>; Naconsie et al., <xref rid="B56" ref-type="bibr">2014</xref>). This indicates that clade III consists of a heterogeneous group of CuAOs. Another remarkable finding is the higher catalytic activity of MdAO2 with monoamines, such as 2-phenylethylamine, tyramine and tryptamine, than with Put and Spd (Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref>). Interestingly, tyramine is also a substrate of ELAO whereas tryptamine and other indoleamines are both substrates and inhibitors of LSAO (Medda et al., <xref rid="B47" ref-type="bibr">1997</xref>; Pintus et al., <xref rid="B63" ref-type="bibr">2013</xref>). It was speculated that 2-phenylacetaldehyde produced by MdAO2-mediated oxidation of 2-phenylethylamine may be converted in fruits to 2-phenylethanol, a volatile compound that is a major contributor to fruit flavor and flower fragrance. It is also possible that 4-hydroxyphenylacetaldehyde produced by tyramine oxidation is involved in benzylisoquinoline alkaloid biosynthesis in plants (Zarei et al., <xref rid="B96" ref-type="bibr">2015a</xref>).</p><p>PAOs oxidize the secondary amino groups of a series of PAs and reaction products depend on the catalytic mechanism and substrate specificity. The apoplastic PAOs oxidize the carbon at the <italic>endo</italic>-side of the <italic>N</italic><sup>4</sup> atom of Spd and Spm producing Dap, H<sub>2</sub>O<sub>2</sub>, and an aminoaldehyde (Tavladoraki et al., <xref rid="B83" ref-type="bibr">1998</xref>; Cervelli et al., <xref rid="B11" ref-type="bibr">2001</xref>; Liu et al., <xref rid="B43" ref-type="bibr">2014b</xref>), whereas all the intracellular PAOs oxidize the carbon at the <italic>exo</italic>-side of the <italic>N</italic><sup>4</sup> atom of Spd or Spm, to produce Put or Spd, respectively, together with H<sub>2</sub>O<sub>2</sub> and 3-aminopropanal (Tavladoraki et al., <xref rid="B82" ref-type="bibr">2006</xref>; Kamada-Nobusada et al., <xref rid="B34" ref-type="bibr">2008</xref>; Moschou et al., <xref rid="B52" ref-type="bibr">2008b</xref>; Fincato et al., <xref rid="B23" ref-type="bibr">2011</xref>; Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>; Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>; Mo et al., <xref rid="B48" ref-type="bibr">2015</xref>). Some of the intracellular PAOs are also able to oxidize Therm-Spm and norspermine (Nor-Spm) with the production of Spd and norspermidine (Nor-Spd), respectively (Tavladoraki et al., <xref rid="B82" ref-type="bibr">2006</xref>; Fincato et al., <xref rid="B23" ref-type="bibr">2011</xref>; Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>). Recently, a <italic>Selaginella lepidophylla</italic> PAO (SelPAO5) was shown to produce Nor-Spd from Therm-Spm (Sagor et al., <xref rid="B72" ref-type="bibr">2015</xref>). These differences in reaction products reflect differences in position and orientation of the substrate inside the catalytic site. Both the <italic>exo</italic>- and <italic>endo</italic>-mode of PA oxidation produce a biologically active diamine or triamine which can be converted to higher PAs. Indeed, even Dap, which has a role in the control of stomata movement through its acetylated form (Jammes et al., <xref rid="B32" ref-type="bibr">2014</xref>), can be converted by aminopropyltransferases to Nor-Spd and subsequently to Nor-Spm, two PAs correlated to stress tolerance (Kuehn et al., <xref rid="B39" ref-type="bibr">1990</xref>; Fuell et al., <xref rid="B24" ref-type="bibr">2010</xref>; Sagor et al., <xref rid="B72" ref-type="bibr">2015</xref>). In this way, all PAOs can be considered involved in PA back-conversion. This view changes the prevailing idea that the PAOs with an <italic>endo</italic>-mode of substrate cleavage are involved in PA terminal catabolism, thus attributing to CuAOs the role of PA terminal catabolism which permits nitrogen and carbon re-assimilation to various biochemical reactions (Moschou et al., <xref rid="B53" ref-type="bibr">2012</xref>).</p><p>In Arabidopsis five PAOs are present (AtPAO1-AtPAO5), which are localized intracellularly and show an <italic>exo</italic>-mode of substrate oxidation. AtPAO1 and AtPAO5 present cytosolic localization and a preference for Spm, Therm-Spm, and Nor-Spm, as substrates (Tavladoraki et al., <xref rid="B82" ref-type="bibr">2006</xref>; Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>; Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>). AtPAO5 accepts also <italic>N</italic><sup>1</sup>-acetyl-Spm as a substrate and appears to be a peculiar PAO, having a better activity as a dehydrogenase rather than as an oxidase (Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>). AtPAO2, AtPAO3, and AtPAO4 are localized in the peroxisomes and oxidize both Spd and Spm (Kamada-Nobusada et al., <xref rid="B34" ref-type="bibr">2008</xref>; Moschou et al., <xref rid="B52" ref-type="bibr">2008b</xref>; Takahashi et al., <xref rid="B79" ref-type="bibr">2010</xref>; Fincato et al., <xref rid="B23" ref-type="bibr">2011</xref>; Sequera-Mutiozabal et al., <xref rid="B75" ref-type="bibr">2016</xref>). Furthermore, AtPAO2, AtPAO3, and AtPAO4 present similar gene structures and tissue-specific expression patterns (root tips, guard cells and pollen grains; Takahashi et al., <xref rid="B79" ref-type="bibr">2010</xref>; Fincato et al., <xref rid="B22" ref-type="bibr">2012</xref>). Phylogenetic studies showed that PAOs are divided into four major clades (Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>; Wang and Liu, <xref rid="B90" ref-type="bibr">2015</xref>). Worth noticing is the fact that the PAOs of the same clade present some common characteristics (Table <xref ref-type="table" rid="T1">1</xref>). In particular, clade I PAOs have cytosolic localization and oxidize specifically Spm but not Spd, while clade IV PAOs present peroxisomal localization and specificity for either Spm or Spd or both. The apoplastic PAOs of clade II show preference for both Spm and Spd and are characterized by a <italic>k</italic><sub><italic>cat</italic></sub> value at least 10-fold higher than that of the PAOs of the other clades. Clade III PAOs are cytosolic enzymes which recognize Spm, Therm-Spm, Nor-Spm, and <italic>N</italic><sup>1</sup>-acetyl Spm as substrates and are regulated by PAs (Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>; Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>; Wang and Liu, <xref rid="B90" ref-type="bibr">2015</xref>). Furthermore, they present very low <italic>k</italic><sub><italic>cat</italic></sub> values as oxidases, which indicate that not only AtPAO5 but all AtPAO5 orthologs may have activity mainly as dehydrogenases (Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>).</p></sec><sec id="s2"><title>Cell-wall amine oxidases: driving ROS production in the apoplastic “hub”</title><p>Compelling evidence supports a key role for reactive oxygen species (ROS; superoxide anion, <inline-formula><mml:math id="M1"><mml:msubsup><mml:mrow><mml:mtext>O</mml:mtext></mml:mrow><mml:mrow><mml:mn>2</mml:mn></mml:mrow><mml:mrow><mml:mo>•</mml:mo><mml:mo>-</mml:mo></mml:mrow></mml:msubsup></mml:math></inline-formula>; H<sub>2</sub>O<sub>2</sub>; hydroxyl radical, <sup>•</sup>OH; singlet oxygen, <sup>1</sup>O<sub>2</sub>) and nitric oxide (NO) in orchestrating developmental processes, as well as in being involved in signaling of both local and systemic defense responses in plants. The apoplast is a major “hub” for these chemical species. Their accumulation in large amounts and the complexity of the regulatory mechanisms involved in their biosynthesis reflect the peculiar role of this compartment in physiological events that depend on temporarily regulated and spatially restricted ROS and NO signatures (Kärkönen and Kuchitsu, <xref rid="B35" ref-type="bibr">2015</xref>). Indeed, ROS are key players in cell-wall loosening and stiffening, as well as in developmental cell death, and stress-related events, such as the two-phase oxidative burst, wound-healing and the hypersensitive response (De Pinto et al., <xref rid="B19" ref-type="bibr">2012</xref>; Kärkönen and Kuchitsu, <xref rid="B35" ref-type="bibr">2015</xref>). Furthermore, ROS generated in the apoplast may well influence Ca<sup>2+</sup> transport across plasma membrane thus inducing a multiplicity of Ca<sup>2+</sup>-mediated responses (Gilroy et al., <xref rid="B29" ref-type="bibr">2014</xref>; Pottosin et al., <xref rid="B65" ref-type="bibr">2014</xref>). Systems involved in ROS biosynthesis in the apoplast include plasma membrane NADPH oxidases and quinone reductases, cell-wall peroxidases (PODs), oxalate oxidases, amine oxidases (Kärkönen and Kuchitsu, <xref rid="B35" ref-type="bibr">2015</xref>). Non enzymatic <sup>•</sup>OH production can be also driven by Fenton-type reaction dependent on a reducing agent (for example ascorbate), transition metal ions and H<sub>2</sub>O<sub>2</sub> (Schopfer et al., <xref rid="B74" ref-type="bibr">2002</xref>; Müller et al., <xref rid="B54" ref-type="bibr">2009</xref>). Although, a very significative amount of data suggests NADPH oxidases and/or PODs to have a prevalent role in ROS production in response to microbial pathogens, wounding, as well as in development-related events, the contribution of other systems has been largely underestimated (Cona et al., <xref rid="B15" ref-type="bibr">2006a</xref>,<xref rid="B16" ref-type="bibr">b</xref>; Monshausen et al., <xref rid="B50" ref-type="bibr">2007</xref>; Angelini et al., <xref rid="B7" ref-type="bibr">2008</xref>; Kärkönen and Kuchitsu, <xref rid="B35" ref-type="bibr">2015</xref>; Roach et al., <xref rid="B69" ref-type="bibr">2015</xref>). This consideration derives mainly from the analysis of literature data based on extensive use of diphenyleneiodonium (DPI), sodium azide or potassium cyanide and diethyldithiocarbamate (DDC) as diagnostic tools for the involvement of NADPH oxidase, POD or superoxide dismutase activity, respectively, in ROS production. However, these compounds are inhibitors of CuAOs (DDC, azide, cyanide) and PAOs (DPI) as well (Cona et al., <xref rid="B16" ref-type="bibr">2006b</xref>; Medda et al., <xref rid="B46" ref-type="bibr">2009</xref>). Noteworthy, a cross-talk has been recently suggested between AtPAO3 and NADPH oxidase activity, affecting ROS homeostasis and respiration rate in Arabidopsis (Andronis et al., <xref rid="B5" ref-type="bibr">2014</xref>). On the other hand, several evidences support a role of PAs not only in ROS production, but also in that of NO (Tun et al., <xref rid="B89" ref-type="bibr">2006</xref>; Pál et al., <xref rid="B59" ref-type="bibr">2015</xref>). Indeed, loss-of-function <italic>atcuao</italic>γ<italic>1</italic> and <italic>atpao2</italic> mutants are impaired in PA- and/or abscisic acid (ABA)-mediated NO production (Wimalasekera et al., <xref rid="B92" ref-type="bibr">2011</xref>, <xref rid="B91" ref-type="bibr">2015</xref>).</p></sec><sec id="s3"><title>Polyamine oxidation in the apoplast: cell-wall modifications and growth regulation</title><p>Early studies in legumes, as well as in maize and tobacco plants evidenced a close correlation between tissue distribution of cell-wall associated CuAO, PAO, and POD activities (Federico and Angelini, <xref rid="B21" ref-type="bibr">1991</xref>; Rea et al., <xref rid="B68" ref-type="bibr">2002</xref>; Paschalidis and Roubelakis-Angelakis, <xref rid="B60" ref-type="bibr">2005</xref>). These studies, also supported by the use of mechanism-based specific inhibitors, suggested a role of PA oxidation in providing H<sub>2</sub>O<sub>2</sub> for POD activity during cell-wall cross-linking, lignification and/or suberization processes taking place in the course of organ development, de-etiolation, or wound-healing (Cona et al., <xref rid="B14" ref-type="bibr">2003</xref>, <xref rid="B15" ref-type="bibr">2006a</xref>, <xref rid="B17" ref-type="bibr">2014</xref>; Angelini et al., <xref rid="B7" ref-type="bibr">2008</xref>). A role for lignin synthesis in anther cell-walls has been also hypothesized for an <italic>Oryza sativa</italic> PAO (OsPAO7; Liu et al., <xref rid="B43" ref-type="bibr">2014b</xref>). The major concern raised by these studies comes from the low levels or even absence of PAs in the apoplast under physiological growth conditions (Rea et al., <xref rid="B67" ref-type="bibr">2004</xref>). However, this issue was overcome by the observation that PAs are secreted in the apoplastic milieu during specific developmental phases or under biotic and abiotic stress conditions (Yoda et al., <xref rid="B94" ref-type="bibr">2003</xref>; Moschou et al., <xref rid="B51" ref-type="bibr">2008a</xref>; Rodríguez et al., <xref rid="B70" ref-type="bibr">2009</xref>). On the other hand, in <italic>Zea mays</italic>, PAO-mediated H<sub>2</sub>O<sub>2</sub> production in the apoplast significantly contributes to leaf blade elongation, possibly through Fenton and/or Haber-Weiss type reactions driving <sup>•</sup>OH synthesis (Rodríguez et al., <xref rid="B70" ref-type="bibr">2009</xref>). A similar role has been suggested in <italic>Glycine max</italic> hypocotyls for the putative apoplastic GmCuAO1 (Delis et al., <xref rid="B18" ref-type="bibr">2006</xref>). This contribution is particularly important under salt stress conditions which inhibit both NADPH oxidases and apoplastic POD activities and induce secretion of PAs in the apoplast (Rodríguez et al., <xref rid="B70" ref-type="bibr">2009</xref>; Campestre et al., <xref rid="B10" ref-type="bibr">2011</xref>; Shoresh et al., <xref rid="B76" ref-type="bibr">2011</xref>).</p></sec><sec id="s4"><title>Apoplastic CuAOs and PAOs: developmental PCD and root xylem differentiation</title><p>It is well established that ROS have a key role in programmed cell death (PCD) in plants (De Pinto et al., <xref rid="B19" ref-type="bibr">2012</xref>). Although, cell-wall maturation and lignification is intimately connected to the cell-death phase of xylem tissue differentiation, it is difficult to distinguish specific ROS contribution to each specific event (Bollhöner et al., <xref rid="B8" ref-type="bibr">2012</xref>). Notably, transition between cell proliferation and tissue differentiation in the root is regulated independently by either hormonal balance (auxin and citokinin) or ROS (<inline-formula><mml:math id="M2"><mml:msubsup><mml:mrow><mml:mtext>O</mml:mtext></mml:mrow><mml:mrow><mml:mn>2</mml:mn></mml:mrow><mml:mrow><mml:mo>•</mml:mo><mml:mo>-</mml:mo></mml:mrow></mml:msubsup></mml:math></inline-formula> and H<sub>2</sub>O<sub>2</sub>) distribution (Tsukagoshi et al., <xref rid="B88" ref-type="bibr">2010</xref>). Several lines of evidence links PA oxidation in the apoplast and concomitant ROS production with cell-wall maturation and developmental PCD in particular during xylem tissue differentiation. Møller and McPherson (<xref rid="B49" ref-type="bibr">1998</xref>) demonstrated that <italic>AtCuAO</italic>β expression in root xylem tissues precedes and overlaps with lignin synthesis in Arabidopsis. Furthermore, although the roots of loss-of-function <italic>atcuao</italic>β mutants did not display evident changes as compared to wild-type plants during normal growth, methyl jasmonate induced early protoxylem differentiation in roots of wild-type plants, concomitantly with increased <italic>AtCuAO</italic>β expression levels, decreased Put levels and H<sub>2</sub>O<sub>2</sub> accumulation. As these events do not occur in <italic>atcuao</italic>β roots, a role of <italic>AtCuAO</italic>β in protoxylem differentiation under stress condition can be suggested (Ghuge et al., <xref rid="B26" ref-type="bibr">2015a</xref>,<xref rid="B28" ref-type="bibr">c</xref>). On the other hand, tobacco plants over-expressing a fungal endopolygalacturonase, releasing cell-wall derived oligogalacturonides and mediating both developmental events and defense responses, showed higher CuAO activity, lower Put level, H<sub>2</sub>O<sub>2</sub> accumulation and an earlier root xylem differentiation. These events were reverted by 2-bromoethylamine, a mechanism-based CuAO inhibitor (Cona et al., <xref rid="B17" ref-type="bibr">2014</xref>). Furthermore, it has been observed that active ZmPAO and H<sub>2</sub>O<sub>2</sub> accumulate in root xylem and xylem parenchyma tissues early during their differentiation (Tisi et al., <xref rid="B86" ref-type="bibr">2011</xref>). <italic>N</italic>-prenylagmatine, a specific PAO inhibitor, inhibited secondary cell-wall deposition, while exogenous Spd induced DNA fragmentation and nuclei condensation, thus suggesting a role for PAO in providing H<sub>2</sub>O<sub>2</sub> during secondary wall deposition and developmental PCD in xylem tissue (Tisi et al., <xref rid="B86" ref-type="bibr">2011</xref>). Moreover, over-expression of <italic>ZmPAO1</italic>, as well as down-regulation of the gene encoding S-adenosyl-L-methionine decarboxylase via RNAi in tobacco plants promoted vascular cell differentiation and induced PCD in root cap cells suggesting that the balance between intracellular PA anabolism and apoplastic catabolism is an integrated signaling system coordinating PCD or stress tolerance (Moschou et al., <xref rid="B51" ref-type="bibr">2008a</xref>; Tisi et al., <xref rid="B86" ref-type="bibr">2011</xref>).</p></sec><sec id="s5"><title>Peroxisomal PAOs: involvement in pollen tube and root growth</title><p>PAs and ROS deriving from their oxidation regulate ion channels both in animals and plants during different physiological and stress-response processes directly influencing plasma membrane ion transport and/or acting as second messengers (Pegg, <xref rid="B62" ref-type="bibr">2014</xref>; Pottosin et al., <xref rid="B65" ref-type="bibr">2014</xref>). In particular, H<sub>2</sub>O<sub>2</sub> produced through Spd oxidation by the peroxisomal AtPAO3, which is highly expressed in pollen grains also during pollen tube growth (Fincato et al., <xref rid="B22" ref-type="bibr">2012</xref>), was shown to trigger the opening of hyperpolarization activated Ca<sup>2+</sup>-permeable channels in pollen tubes, thus altering the tip-specific cytosolic Ca<sup>2+</sup> gradient which plays a pivotal role in controlling pollen tube elongation (Wu et al., <xref rid="B93" ref-type="bibr">2010</xref>). Indeed, two loss-of-function Arabidopsis <italic>atpao3</italic> mutants presented reduced pollen tube growth rate and seed production. Peroxisomal OsPAO3, OsPAO4, and OsPAO5 (Ono et al., <xref rid="B57" ref-type="bibr">2012</xref>) are coherently expressed in anthers (Liu et al., <xref rid="B43" ref-type="bibr">2014b</xref>). More studies are necessary to determine in detail the effect of PAs on pollen maturation, since the effect seems to be complex involving PA conjugation, ROS formation/scavenging, and cell-death events (Aloisi et al., <xref rid="B3" ref-type="bibr">2015</xref>). Furthermore, based on the vigorous root growth of <italic>AtPAO2</italic> over-expressor plants and the hypersensitivity of <italic>atpao2</italic> loss-of-function mutant plants to ABA, it has been recently hypothesized a positive function of <italic>AtPAO2</italic> in Arabidopsis root growth (Wimalasekera et al., <xref rid="B91" ref-type="bibr">2015</xref>).</p></sec><sec id="s6"><title>CuAOs and PAOs in stomata movement and fruit ripening</title><p>ROS and calcium signatures in guard cells, as well as ion transport from the apoplast into the cytosol and from the cytosol for storage in the vacuole are important components of the regulatory network controlling stomata movements (Kollist et al., <xref rid="B38" ref-type="bibr">2014</xref>; Murata et al., <xref rid="B55" ref-type="bibr">2015</xref>). In <italic>Vicia faba</italic>, it has been shown that ABA-mediated stomata closure involves induction of an apoplastic CuAO activity as a source of H<sub>2</sub>O<sub>2</sub>, and that this activity is necessary to increase cytosolic Ca<sup>2+</sup> levels in response to ABA (An et al., <xref rid="B4" ref-type="bibr">2008</xref>). Consistently with these observations, the apoplastic AtCuAOβ was shown to be expressed in guard cells (Ghuge et al., <xref rid="B27" ref-type="bibr">2015b</xref>). In addition, the peroxisomal AtCuAOζ which is expressed in guard cells is also involved in the ABA-mediated control of stomata opening (Qu et al., <xref rid="B66" ref-type="bibr">2014</xref>). PAOs were also shown to contribute to the control of stomata movement in <italic>Vitis vinifera</italic> and <italic>Arabidopsis</italic> (Paschalidis et al., <xref rid="B61" ref-type="bibr">2010</xref>; Hou et al., <xref rid="B31" ref-type="bibr">2013</xref>).</p><p>PA catabolism has been also associated with grape and tomato fruit ripening (Agudelo-Romero et al., <xref rid="B1" ref-type="bibr">2013</xref>; Tsaniklidis et al., <xref rid="B87" ref-type="bibr">2016</xref>). Despite the increase of arginine decarboxylase expression levels during grape fruit ripening, the level of free and conjugated PAs was strongly decreased. This decrease was accompanied by up-regulation of two <italic>CuAOs</italic> and three <italic>PAO</italic> genes, one <italic>CuAO</italic> and two <italic>PAOs</italic> of them encoding for proteins with putative peroxisomal localization (Agudelo-Romero et al., <xref rid="B1" ref-type="bibr">2013</xref>). Increase of CuAO and PAO activity, as well of H<sub>2</sub>O<sub>2</sub> production during fruit maturation, was also observed. Furthermore, the relatively high expression levels of <italic>Solanum lycopersicum</italic> CuAO (SlCuAO1), which is clustered together with AtCuAOδ in clade IIb, was attributed to the implication of PA metabolism in physiological processes taking place during fruit ripening (Tsaniklidis et al., <xref rid="B87" ref-type="bibr">2016</xref>). The up-regulation of CuAOs/PAOs during ripening may constitute a source of ROS for signaling events leading to the acceleration of the ripening process. It is also possible that PA catabolism interferes with plant hormonal pathways, such as ethylene and ABA (Agudelo-Romero et al., <xref rid="B1" ref-type="bibr">2013</xref>). Alternatively, 4-aminobutanal produced through PA catabolism can be metabolized to γ-aminobutyric acid by an aminoaldehyde dehydrogenase (Zarei et al., <xref rid="B97" ref-type="bibr">2015b</xref>) and enter into the Krebs cycle, thus constituting a link between nitrogen and carbon metabolism (Moschou et al., <xref rid="B53" ref-type="bibr">2012</xref>).</p></sec><sec id="s7"><title>Cytosolic PAOs in the control of Therm-Spm levels</title><p>Loss-of-function Arabidopsis mutants for <italic>AtPAO5</italic> present increased levels of Therm-Spm, <italic>N</italic><sup>1</sup>-acetyl-Spm and Spm which are the substrates of the enzyme (Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>; Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Sagor et al., <xref rid="B73" ref-type="bibr">2016</xref>; Zarza et al., <xref rid="B98" ref-type="bibr">2016</xref>). Interestingly, the expression levels of <italic>AtPAO5</italic>, as well as of its functional orthologue in rice (<italic>OsPAO1</italic>), are controlled by Therm-Spm and Spm (Ahou et al., <xref rid="B2" ref-type="bibr">2014</xref>; Liu et al., <xref rid="B41" ref-type="bibr">2014a</xref>,<xref rid="B42" ref-type="bibr">c</xref>). This indicates the necessity for a fine tune regulation of PA levels for proper growth and stress response, since levels above an upper limit or below a threshold may be detrimental for the plants. Indeed, the <italic>atpao5</italic> mutants present altered growth parameters at late developmental stages mainly due to the increased Therm-Spm levels (Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>), as have been also observed in mutants for <italic>Therm-Spm synthase</italic> and <italic>S-adenosylmethionine decarboxylase</italic> with reduced Therm-Spm levels (Clay and Nelson, <xref rid="B13" ref-type="bibr">2005</xref>; Ge et al., <xref rid="B25" ref-type="bibr">2006</xref>; Yoshimoto et al., <xref rid="B95" ref-type="bibr">2016</xref>). Furthermore, the <italic>atpao5</italic> mutants were hypersensitive to low doses of exogenous Therm-Spm (Kim et al., <xref rid="B37" ref-type="bibr">2014</xref>; Liu et al., <xref rid="B42" ref-type="bibr">2014c</xref>).</p></sec><sec id="s8"><title>Intracellular PAOs and somatic embryogenesis</title><p>Some studies suggest that in <italic>Gossypium hirsutum</italic> an AtPAO1-like (GhPAO1) and an AtPAO5-like (GhPAO4) PAO may play a crucial role in the generation and differentiation of embryogenic callus during somatic embryogenesis (Cheng et al., <xref rid="B12" ref-type="bibr">2015</xref>). Indeed, PAO activity levels significantly increased during conversion of embryogenic callus into somatic embryos, and inhibition of PAO activity by 1,8-diaminooctane resulted in brown and necrotic cultures, and a significant decrease in both fresh weight and somatic embryo number. Importantly, the negative effects of 1,8-diaminooctane were reversed by application of exogenous H<sub>2</sub>O<sub>2</sub>. Furthermore, in Arabidopsis, <italic>AtPAO5</italic> and its <italic>B. juncea</italic> ortholog (<italic>BjPAO</italic>) have a role in shoot regeneration from root cultures (Lim et al., <xref rid="B40" ref-type="bibr">2006</xref>).</p></sec><sec id="s9"><title>Concluding remarks</title><p>Numerous recent studies have evidenced an extraordinary complexity in <italic>CuAO</italic> and <italic>PAO</italic> gene families regarding catalytic activity, subcellular localization, expression pattern and physiological roles of the encoded proteins. Indeed, important links to developmental and stress-related events are emerging for CuAOs and PAOs through ROS/NO production and regulation of specific PA levels.</p></sec><sec id="s10"><title>Author contributions</title><p>All authors listed, have made substantial, direct and intellectual contribution to the work, and approved it for publication.</p><sec><title>Conflict of interest statement</title><p>The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.</p></sec></sec></body><back><ack><p>We apologize to authors whose papers could not be cited owing to space limitations. This work was supported by University “Roma Tre.” We are grateful to Dr. Daniele Salvi (CIBIO-InBio, Portugal) for useful discussions regarding phylogenetic analysis. Moreover, we deeply thank Dr. Ilaria Fraudentali, Dr. Andrea Carucci, and Dr. Stefano Franchi (Department of Science, University “Roma Tre,” Italy) for technical assistance in figure and table preparation.</p></ack><fn-group><fn id="fn0001"><p><sup>1</sup>Due to heterogeneity of <italic>CuAO</italic> gene classification in literature, we have renumbered them according to Qu et al. (<xref rid="B66" ref-type="bibr">2014</xref>) with some modifications taking into consideration the phylogenetic analysis (Figure <xref ref-type="fig" rid="F1">1</xref>). We trust that this will help for future use.</p></fn></fn-group><sec sec-type="supplementary-material" id="s11"><title>Supplementary material</title><p>The Supplementary Material for this article can be found online at: <ext-link ext-link-type="uri" xlink:href="http://journal.frontiersin.org/article/10.3389/fpls.2016.00824">http://journal.frontiersin.org/article/10.3389/fpls.2016.00824</ext-link></p><supplementary-material content-type="local-data" id="SM1"><media xlink:href="Table1.PDF"><caption><p>Click here for additional data file.</p></caption></media></supplementary-material></sec><ref-list><title>References</title><ref id="B1"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Agudelo-Romero</surname><given-names>P.</given-names></name><name><surname>Bortolloti</surname><given-names>C.</given-names></name><name><surname>Pais</surname><given-names>M. S.</given-names></name><name><surname>Tiburcio</surname><given-names>A. F.</given-names></name><name><surname>Fortes</surname><given-names>A. M.</given-names></name></person-group> (<year>2013</year>). <article-title>Study of polyamines during grape ripening indicate an important role of polyamine catabolism</article-title>. <source>Plant Physiol. Biochem.</source><volume>67</volume>, <fpage>105</fpage>–<lpage>119</lpage>. <pub-id pub-id-type="doi">10.1016/j.plaphy.2013.02.024</pub-id><pub-id pub-id-type="pmid">23562795</pub-id></mixed-citation></ref><ref id="B2"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ahou</surname><given-names>A.</given-names></name><name><surname>Martignago</surname><given-names>D.</given-names></name><name><surname>Alabdallah</surname><given-names>O.</given-names></name><name><surname>Tavazza</surname><given-names>R.</given-names></name><name><surname>Stano</surname><given-names>P.</given-names></name><name><surname>Macone</surname><given-names>A.</given-names></name><etal></etal></person-group>. (<year>2014</year>). <article-title>A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines</article-title>. <source>J. Exp. Bot.</source><volume>65</volume>, <fpage>1585</fpage>–<lpage>1603</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/eru016</pub-id><pub-id pub-id-type="pmid">24550437</pub-id></mixed-citation></ref><ref id="B3"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Aloisi</surname><given-names>I.</given-names></name><name><surname>Cai</surname><given-names>G.</given-names></name><name><surname>Tumiatti</surname><given-names>V.</given-names></name><name><surname>Minarini</surname><given-names>A.</given-names></name><name><surname>Del Duca</surname><given-names>S.</given-names></name></person-group> (<year>2015</year>). <article-title>Natural polyamines and synthetic analogs modify the growth and the morphology of <italic>Pyrus communis</italic> pollen tubes affecting ROS levels and causing cell death</article-title>. <source>Plant Sci.</source><volume>239</volume>, <fpage>92</fpage>–<lpage>105</lpage>. <pub-id pub-id-type="doi">10.1016/j.plantsci.2015.07.008</pub-id><pub-id pub-id-type="pmid">26398794</pub-id></mixed-citation></ref><ref id="B4"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>An</surname><given-names>Z.</given-names></name><name><surname>Jing</surname><given-names>W.</given-names></name><name><surname>Liu</surname><given-names>Y.</given-names></name><name><surname>Zhang</surname><given-names>W.</given-names></name></person-group> (<year>2008</year>). <article-title>Hydrogen peroxide generated by copper amine oxidase is involved in abscisic acid-induced stomatal closure in <italic>Vicia faba</italic></article-title>. <source>J. Exp. Bot.</source><volume>59</volume>, <fpage>815</fpage>–<lpage>825</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/erm370</pub-id><pub-id pub-id-type="pmid">18272918</pub-id></mixed-citation></ref><ref id="B5"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Andronis</surname><given-names>E. A.</given-names></name><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Toumi</surname><given-names>I.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name></person-group> (<year>2014</year>). <article-title>Peroxisomal polyamine oxidase and NADPH-oxidase cross-talk for ROS homeostasis which affects respiration rate in <italic>Arabidopsis thaliana</italic></article-title>. <source>Front. Plant Sci.</source><volume>5</volume>:<issue>132</issue>. <pub-id pub-id-type="doi">10.3389/fpls.2014.00132</pub-id><pub-id pub-id-type="pmid">24765099</pub-id></mixed-citation></ref><ref id="B6"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Fincato</surname><given-names>P.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><name><surname>Tisi</surname><given-names>A.</given-names></name></person-group> (<year>2010</year>). <article-title>Plant amine oxidases “on the move”: an update</article-title>. <source>Plant Physiol. Biochem.</source><volume>48</volume>, <fpage>560</fpage>–<lpage>564</lpage>. <pub-id pub-id-type="doi">10.1016/j.plaphy.2010.02.001</pub-id><pub-id pub-id-type="pmid">20219383</pub-id></mixed-citation></ref><ref id="B7"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Tisi</surname><given-names>A.</given-names></name><name><surname>Rea</surname><given-names>G.</given-names></name><name><surname>Chen</surname><given-names>M. M.</given-names></name><name><surname>Botta</surname><given-names>M.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><etal></etal></person-group>. (<year>2008</year>). <article-title>Involvement of polyamine oxidase in wound healing</article-title>. <source>Plant Physiol.</source><volume>146</volume>, <fpage>162</fpage>–<lpage>177</lpage>. <pub-id pub-id-type="doi">10.1104/pp.107.108902</pub-id><pub-id pub-id-type="pmid">17993545</pub-id></mixed-citation></ref><ref id="B8"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Bollhöner</surname><given-names>B.</given-names></name><name><surname>Prestele</surname><given-names>J.</given-names></name><name><surname>Tuominen</surname><given-names>H.</given-names></name></person-group> (<year>2012</year>). <article-title>Xylem cell death: emerging understanding of regulation and function</article-title>. <source>J. Exp. Bot.</source><volume>63</volume>, <fpage>1081</fpage>–<lpage>1094</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/err438</pub-id><pub-id pub-id-type="pmid">22213814</pub-id></mixed-citation></ref><ref id="B9"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Boudart</surname><given-names>G.</given-names></name><name><surname>Jamet</surname><given-names>E.</given-names></name><name><surname>Rossignol</surname><given-names>M.</given-names></name><name><surname>Lafitte</surname><given-names>C.</given-names></name><name><surname>Borderies</surname><given-names>G.</given-names></name><name><surname>Jauneau</surname><given-names>A.</given-names></name><etal></etal></person-group>. (<year>2005</year>). <article-title>Cell wall proteins in apoplastic fluids of <italic>Arabidopsis thaliana</italic> rosettes: identification by mass spectrometry and bioinformatics</article-title>. <source>Proteomics</source><volume>5</volume>, <fpage>212</fpage>–<lpage>221</lpage>. <pub-id pub-id-type="doi">10.1002/pmic.200400882</pub-id><pub-id pub-id-type="pmid">15593128</pub-id></mixed-citation></ref><ref id="B10"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Campestre</surname><given-names>M. P.</given-names></name><name><surname>Bordenave</surname><given-names>C. D.</given-names></name><name><surname>Origone</surname><given-names>A. C.</given-names></name><name><surname>Menéndez</surname><given-names>A. B.</given-names></name><name><surname>Ruiz</surname><given-names>O. A.</given-names></name><name><surname>Rodríguez</surname><given-names>A. A.</given-names></name><etal></etal></person-group>. (<year>2011</year>). <article-title>Polyamine catabolism is involved in response to salt stress in soybean hypocotyls</article-title>. <source>J. Plant Physiol.</source><volume>168</volume>, <fpage>1234</fpage>–<lpage>1240</lpage>. <pub-id pub-id-type="doi">10.1016/j.jplph.2011.01.007</pub-id><pub-id pub-id-type="pmid">21324548</pub-id></mixed-citation></ref><ref id="B11"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cervelli</surname><given-names>M.</given-names></name><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Polticelli</surname><given-names>F.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Mariottini</surname><given-names>P.</given-names></name></person-group> (<year>2001</year>). <article-title>A barley polyamine oxidase isoform with distinct structural features and subcellular localization</article-title>. <source>Eur. J. Biochem.</source><volume>268</volume>, <fpage>3816</fpage>–<lpage>3830</lpage>. <pub-id pub-id-type="doi">10.1046/j.1432-1327.2001.02296.x</pub-id><pub-id pub-id-type="pmid">11432750</pub-id></mixed-citation></ref><ref id="B12"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cheng</surname><given-names>W. H.</given-names></name><name><surname>Wang</surname><given-names>F. L.</given-names></name><name><surname>Cheng</surname><given-names>X. Q.</given-names></name><name><surname>Zhu</surname><given-names>Q. H.</given-names></name><name><surname>Sun</surname><given-names>Y. Q.</given-names></name><name><surname>Zhu</surname><given-names>H. G.</given-names></name><etal></etal></person-group>. (<year>2015</year>). <article-title>Polyamine and its metabolite H<sub>2</sub>O<sub>2</sub> play a key role in the conversion of embryogenic callus into somatic embryos in upland cotton (<italic>Gossypium hirsutum</italic> L)</article-title>. <source>Front. Plant Sci.</source><volume>6</volume>:<issue>1063</issue>. <pub-id pub-id-type="doi">10.3389/fpls.2015.01063</pub-id><pub-id pub-id-type="pmid">26697030</pub-id></mixed-citation></ref><ref id="B13"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Clay</surname><given-names>N. K.</given-names></name><name><surname>Nelson</surname><given-names>T.</given-names></name></person-group> (<year>2005</year>). <article-title>Arabidopsis thickvein mutation affects vein thickness and organ vascularization, and resides in a provascular cell-specific spermine synthase involved in vein definition and in polar auxin transport</article-title>. <source>Plant Physiol.</source><volume>138</volume>, <fpage>767</fpage>–<lpage>777</lpage>. <pub-id pub-id-type="doi">10.1104/pp.104.055756</pub-id><pub-id pub-id-type="pmid">15894745</pub-id></mixed-citation></ref><ref id="B14"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Cenci</surname><given-names>F.</given-names></name><name><surname>Cervelli</surname><given-names>M.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Mariottini</surname><given-names>P.</given-names></name><name><surname>Moreno</surname><given-names>S.</given-names></name><etal></etal></person-group>. (<year>2003</year>). <article-title>Polyamine oxidase, a hydrogen peroxide-producing enzyme, is up-regulated by light and down-regulated by auxin in the outer tissues of the maize mesocotyl</article-title>. <source>Plant Physiol.</source><volume>131</volume>, <fpage>803</fpage>–<lpage>813</lpage>. <pub-id pub-id-type="doi">10.1104/pp.011379</pub-id><pub-id pub-id-type="pmid">12586904</pub-id></mixed-citation></ref><ref id="B15"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Rea</surname><given-names>G.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name></person-group> (<year>2006a</year>). <article-title>Functions of amine oxidases in plant development and defence</article-title>. <source>Trends Plant Sci.</source><volume>11</volume>, <fpage>80</fpage>–<lpage>88</lpage>. <pub-id pub-id-type="doi">10.1016/j.tplants.2005.12.009</pub-id><pub-id pub-id-type="pmid">16406305</pub-id></mixed-citation></ref><ref id="B16"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Rea</surname><given-names>G.</given-names></name><name><surname>Botta</surname><given-names>M.</given-names></name><name><surname>Corelli</surname><given-names>F.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name></person-group> (<year>2006b</year>). <article-title>Flavin-containing polyamine oxidase is a hydrogen peroxide source in the oxidative response to the protein phosphatase inhibitor cantharidin in <italic>Zea mays</italic> L</article-title>. <source>J. Exp. Bot.</source><volume>57</volume>, <fpage>2277</fpage>–<lpage>2289</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/erj195</pub-id><pub-id pub-id-type="pmid">16831849</pub-id></mixed-citation></ref><ref id="B17"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Tisi</surname><given-names>A.</given-names></name><name><surname>Ghuge</surname><given-names>S. A.</given-names></name><name><surname>Franchi</surname><given-names>S.</given-names></name><name><surname>De Lorenzo</surname><given-names>G.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name></person-group> (<year>2014</year>). <article-title>Wound healing response and xylem differentiation in tobacco plants over-expressing a fungal endopolygalacturonase is mediated by copper amine oxidase activity</article-title>. <source>Plant Physiol. Biochem.</source><volume>82</volume>, <fpage>54</fpage>–<lpage>65</lpage>. <pub-id pub-id-type="doi">10.1016/j.plaphy.2014.05.004</pub-id><pub-id pub-id-type="pmid">24907525</pub-id></mixed-citation></ref><ref id="B18"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Delis</surname><given-names>C.</given-names></name><name><surname>Dimou</surname><given-names>M.</given-names></name><name><surname>Flemetakis</surname><given-names>E.</given-names></name><name><surname>Aivalakis</surname><given-names>G.</given-names></name><name><surname>Katinakis</surname><given-names>P.</given-names></name></person-group> (<year>2006</year>). <article-title>A root- and hypocotyl-specific gene coding for copper-containing amine oxidase is related to cell expansion in soybean seedlings</article-title>. <source>J. Exp. Bot.</source><volume>57</volume>, <fpage>101</fpage>–<lpage>111</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/erj009</pub-id><pub-id pub-id-type="pmid">16291800</pub-id></mixed-citation></ref><ref id="B19"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>De Pinto</surname><given-names>M. C.</given-names></name><name><surname>Locato</surname><given-names>V.</given-names></name><name><surname>De Gara</surname><given-names>L.</given-names></name></person-group> (<year>2012</year>). <article-title>Redox regulation in plant programmed cell death</article-title>. <source>Plant Cell Environ.</source><volume>35</volume>, <fpage>234</fpage>–<lpage>244</lpage>. <pub-id pub-id-type="doi">10.1111/j.1365-3040.2011.02387.x</pub-id><pub-id pub-id-type="pmid">21711357</pub-id></mixed-citation></ref><ref id="B20"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Dewey</surname><given-names>R. E.</given-names></name><name><surname>Xie</surname><given-names>J.</given-names></name></person-group> (<year>2013</year>). <article-title>Molecular genetics of alkaloid biosynthesis in <italic>Nicotiana tabacum</italic></article-title>. <source>Phytochemistry</source><volume>94</volume>, <fpage>10</fpage>–<lpage>27</lpage>. <pub-id pub-id-type="doi">10.1016/j.phytochem.2013.06.002</pub-id><pub-id pub-id-type="pmid">23953973</pub-id></mixed-citation></ref><ref id="B21"><mixed-citation publication-type="book"><person-group person-group-type="author"><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name></person-group> (<year>1991</year>). <article-title>Polyamine catabolism in plants</article-title>, in <source>Biochemistry and Physiology of Polyamines in Plants</source>, eds <person-group person-group-type="editor"><name><surname>Slocum</surname><given-names>R. D.</given-names></name><name><surname>Flores</surname><given-names>H. E.</given-names></name></person-group> (<publisher-loc>Boca Raton, FL</publisher-loc>: <publisher-name>CRC Press</publisher-name>), <fpage>41</fpage>–<lpage>56</lpage>.</mixed-citation></ref><ref id="B22"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fincato</surname><given-names>P.</given-names></name><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Ahou</surname><given-names>A.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name></person-group> (<year>2012</year>). <article-title>The members of <italic>Arabidopsis thaliana</italic> PAO gene family exhibit distinct tissue- and organ-specific expression pattern during seedling growth and flower development</article-title>. <source>Amino Acids</source><volume>42</volume>, <fpage>831</fpage>–<lpage>841</lpage>. <pub-id pub-id-type="doi">10.1007/s00726-011-0999-7</pub-id><pub-id pub-id-type="pmid">21814784</pub-id></mixed-citation></ref><ref id="B23"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fincato</surname><given-names>P.</given-names></name><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Spedaletti</surname><given-names>V.</given-names></name><name><surname>Tavazza</surname><given-names>R.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name></person-group> (<year>2011</year>). <article-title>Functional diversity inside the Arabidopsis polyamine oxidase gene family</article-title>. <source>J. Exp. Bot.</source><volume>62</volume>, <fpage>1155</fpage>–<lpage>1168</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/erq341</pub-id><pub-id pub-id-type="pmid">21081665</pub-id></mixed-citation></ref><ref id="B24"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fuell</surname><given-names>C.</given-names></name><name><surname>Elliot</surname><given-names>K. A.</given-names></name><name><surname>Hanfrey</surname><given-names>C. C.</given-names></name><name><surname>Franceschetti</surname><given-names>M.</given-names></name><name><surname>Michael</surname><given-names>A. J.</given-names></name></person-group> (<year>2010</year>). <article-title>Polyamine biosynthetic diversity in plants and algae</article-title>. <source>Plant Physiol. Biochem.</source><volume>48</volume>, <fpage>513</fpage>–<lpage>520</lpage>. <pub-id pub-id-type="doi">10.1016/j.plaphy.2010.02.008</pub-id><pub-id pub-id-type="pmid">20227886</pub-id></mixed-citation></ref><ref id="B25"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ge</surname><given-names>C.</given-names></name><name><surname>Cui</surname><given-names>X.</given-names></name><name><surname>Wang</surname><given-names>Y.</given-names></name><name><surname>Hu</surname><given-names>Y.</given-names></name><name><surname>Fu</surname><given-names>Z.</given-names></name><name><surname>Zhang</surname><given-names>D.</given-names></name><etal></etal></person-group>. (<year>2006</year>). <article-title><italic>BUD2</italic>, encoding an S-adenosylmethionine decarboxylase, is required for Arabidopsis growth and development</article-title>. <source>Cell Res.</source><volume>16</volume>, <fpage>446</fpage>–<lpage>456</lpage>. <pub-id pub-id-type="doi">10.1038/sj.cr.7310056</pub-id><pub-id pub-id-type="pmid">16699540</pub-id></mixed-citation></ref><ref id="B26"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ghuge</surname><given-names>S. A.</given-names></name><name><surname>Carucci</surname><given-names>A.</given-names></name><name><surname>Rodrigues-Pousada</surname><given-names>R. A.</given-names></name><name><surname>Tisi</surname><given-names>A.</given-names></name><name><surname>Franchi</surname><given-names>S.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><etal></etal></person-group>. (<year>2015a</year>). <article-title>The apoplastic copper AMINE OXIDASE1 mediates jasmonic acid-induced protoxylem differentiation in Arabidopsis roots</article-title>. <source>Plant Physiol.</source><volume>168</volume>, <fpage>690</fpage>–<lpage>707</lpage>. <pub-id pub-id-type="doi">10.1104/pp.15.00121</pub-id><pub-id pub-id-type="pmid">25883242</pub-id></mixed-citation></ref><ref id="B27"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ghuge</surname><given-names>S. A.</given-names></name><name><surname>Carucci</surname><given-names>A.</given-names></name><name><surname>Rodrigues-Pousada</surname><given-names>R. A.</given-names></name><name><surname>Tisi</surname><given-names>A.</given-names></name><name><surname>Franchi</surname><given-names>S.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><etal></etal></person-group>. (<year>2015b</year>). <article-title>The MeJA-inducible copper amine oxidase <italic>AtAO1</italic> is expressed in xylem tissue and guard cells</article-title>. <source>Plant Signal Behav.</source><volume>10</volume>:<fpage>e1073872</fpage>. <pub-id pub-id-type="doi">10.1080/15592324.2015.1073872</pub-id><pub-id pub-id-type="pmid">26241131</pub-id></mixed-citation></ref><ref id="B28"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ghuge</surname><given-names>S. A.</given-names></name><name><surname>Tisi</surname><given-names>A.</given-names></name><name><surname>Carucci</surname><given-names>A.</given-names></name><name><surname>Rodrigues-Pousada</surname><given-names>R. A.</given-names></name><name><surname>Franchi</surname><given-names>S.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><etal></etal></person-group>. (<year>2015c</year>). <article-title>Cell wall amine oxidases: new players in root xylem differentiation under stress conditions</article-title>. <source>Plants.</source><volume>4</volume>, <fpage>489</fpage>–<lpage>504</lpage>. <pub-id pub-id-type="doi">10.3390/plants4030489</pub-id><pub-id pub-id-type="pmid">27135338</pub-id></mixed-citation></ref><ref id="B29"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Gilroy</surname><given-names>S.</given-names></name><name><surname>Suzuki</surname><given-names>N.</given-names></name><name><surname>Miller</surname><given-names>G.</given-names></name><name><surname>Choi</surname><given-names>W. G.</given-names></name><name><surname>Toyota</surname><given-names>M.</given-names></name><name><surname>Devireddy</surname><given-names>A. R.</given-names></name><etal></etal></person-group>. (<year>2014</year>). <article-title>A tidal wave of signals: calcium and ROS at the forefront of rapid systemic signaling</article-title>. <source>Trends Plant Sci.</source><volume>19</volume>, <fpage>623</fpage>–<lpage>630</lpage>. <pub-id pub-id-type="doi">10.1016/j.tplants.2014.06.013</pub-id><pub-id pub-id-type="pmid">25088679</pub-id></mixed-citation></ref><ref id="B30"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Heim</surname><given-names>W. G.</given-names></name><name><surname>Sykes</surname><given-names>K. A.</given-names></name><name><surname>Hildreth</surname><given-names>S. B.</given-names></name><name><surname>Sun</surname><given-names>J.</given-names></name><name><surname>Lu</surname><given-names>R.-H.</given-names></name><name><surname>Jelesko</surname><given-names>J. G.</given-names></name></person-group> (<year>2007</year>). <article-title>Cloning and characterization of a <italic>Nicotiana tabacum</italic> methylputrescine oxidase transcript</article-title>. <source>Phytochemistry</source><volume>68</volume>, <fpage>454</fpage>–<lpage>463</lpage>. <pub-id pub-id-type="doi">10.1016/j.phytochem.2006.11.003</pub-id><pub-id pub-id-type="pmid">17174363</pub-id></mixed-citation></ref><ref id="B31"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hou</surname><given-names>Z.-H.</given-names></name><name><surname>Liu</surname><given-names>G.-H.</given-names></name><name><surname>Wang</surname><given-names>L.-X.</given-names></name><name><surname>Liu</surname><given-names>X.</given-names></name></person-group> (<year>2013</year>). <article-title>Regulatory function of polyamine oxidase-generated hydrogen peroxide in ethylene-induced stomatal closure in <italic>Arabidopsis thaliana</italic></article-title>. <source>J. Integr. Agricult.</source><volume>12</volume>, <fpage>251</fpage>–<lpage>262</lpage>. <pub-id pub-id-type="doi">10.1016/S2095-3119(13)60224-5</pub-id></mixed-citation></ref><ref id="B32"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Jammes</surname><given-names>F.</given-names></name><name><surname>Leonhardt</surname><given-names>N.</given-names></name><name><surname>Tran</surname><given-names>D.</given-names></name><name><surname>Bousserouel</surname><given-names>H.</given-names></name><name><surname>Véry</surname><given-names>A. A.</given-names></name><name><surname>Renou</surname><given-names>J. P.</given-names></name><etal></etal></person-group>. (<year>2014</year>). <article-title>Acetylated 1,3-diaminopropane antagonizes abscisic acid-mediated stomatal closing in Arabidopsis</article-title>. <source>Plant J.</source><volume>79</volume>, <fpage>322</fpage>–<lpage>333</lpage>. <pub-id pub-id-type="doi">10.1111/tpj.12564</pub-id><pub-id pub-id-type="pmid">24891222</pub-id></mixed-citation></ref><ref id="B33"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Jiménez-Bremont</surname><given-names>J. F.</given-names></name><name><surname>Marina</surname><given-names>M.</given-names></name><name><surname>Guerrero-González</surname><given-names>M.</given-names></name><name><surname>de</surname><given-names>L.</given-names></name><name><surname>Rossi</surname><given-names>F. R.</given-names></name><name><surname>Sánchez-Rangel</surname><given-names>D.</given-names></name><name><surname>Rodríguez-Kessler</surname><given-names>M.</given-names></name><etal></etal></person-group>. (<year>2014</year>). <article-title>Physiological and molecular implications of plant polyamine metabolism during biotic interactions</article-title>. <source>Front Plant Sci.</source><volume>5</volume>:<issue>95</issue>. <pub-id pub-id-type="doi">10.3389/fpls.2014.00095</pub-id><pub-id pub-id-type="pmid">24672533</pub-id></mixed-citation></ref><ref id="B34"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kamada-Nobusada</surname><given-names>T.</given-names></name><name><surname>Hayashi</surname><given-names>M.</given-names></name><name><surname>Fukazawa</surname><given-names>M.</given-names></name><name><surname>Sakakibara</surname><given-names>H.</given-names></name><name><surname>Nishimura</surname><given-names>M.</given-names></name></person-group> (<year>2008</year>). <article-title>A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in <italic>Arabidopsis thaliana</italic></article-title>. <source>Plant Cell Physiol.</source><volume>49</volume>, <fpage>1272</fpage>–<lpage>1282</lpage>. <pub-id pub-id-type="doi">10.1093/pcp/pcn114</pub-id><pub-id pub-id-type="pmid">18703589</pub-id></mixed-citation></ref><ref id="B35"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kärkönen</surname><given-names>A.</given-names></name><name><surname>Kuchitsu</surname><given-names>K.</given-names></name></person-group> (<year>2015</year>). <article-title>Reactive oxygen species in cell wall metabolism and development in plants</article-title>. <source>Phytochemistry.</source><volume>112</volume>, <fpage>22</fpage>–<lpage>32</lpage>. <pub-id pub-id-type="doi">10.1016/j.phytochem.2014.09.016</pub-id><pub-id pub-id-type="pmid">25446232</pub-id></mixed-citation></ref><ref id="B36"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Katoh</surname><given-names>A.</given-names></name><name><surname>Shoji</surname><given-names>T.</given-names></name><name><surname>Hashimoto</surname><given-names>T.</given-names></name></person-group> (<year>2007</year>). <article-title>Molecular cloning of N-methylputrescine oxidase from tobacco</article-title>. <source>Plant Cell Physiol.</source><volume>48</volume>, <fpage>550</fpage>–<lpage>554</lpage>. <pub-id pub-id-type="doi">10.1093/pcp/pcm018</pub-id><pub-id pub-id-type="pmid">17283012</pub-id></mixed-citation></ref><ref id="B37"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kim</surname><given-names>D. W.</given-names></name><name><surname>Watanabe</surname><given-names>K.</given-names></name><name><surname>Murayama</surname><given-names>C.</given-names></name><name><surname>Izawa</surname><given-names>S.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Michael</surname><given-names>A. J.</given-names></name><etal></etal></person-group>. (<year>2014</year>). <article-title>Polyamine oxidase 5 regulates Arabidopsis growth through thermospermine oxidase activity</article-title>. <source>Plant Physiol.</source><volume>165</volume>, <fpage>1575</fpage>–<lpage>1590</lpage>. <pub-id pub-id-type="doi">10.1104/pp.114.242610</pub-id><pub-id pub-id-type="pmid">24906355</pub-id></mixed-citation></ref><ref id="B38"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kollist</surname><given-names>H.</given-names></name><name><surname>Nuhkat</surname><given-names>M.</given-names></name><name><surname>Roelfsema</surname><given-names>M. R.</given-names></name></person-group> (<year>2014</year>). <article-title>Closing gaps: linking elements that control stomatal movement</article-title>. <source>New Phytol.</source><volume>203</volume>, <fpage>44</fpage>–<lpage>62</lpage>. <pub-id pub-id-type="doi">10.1111/nph.12832</pub-id><pub-id pub-id-type="pmid">24800691</pub-id></mixed-citation></ref><ref id="B39"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kuehn</surname><given-names>G. D.</given-names></name><name><surname>Rodriguez-Garay</surname><given-names>B.</given-names></name><name><surname>Bagga</surname><given-names>S.</given-names></name><name><surname>Phillips</surname><given-names>G. C.</given-names></name></person-group> (<year>1990</year>). <article-title>Novel occurrence of uncommon polyamines in higher plants</article-title>. <source>Plant Physiol.</source><volume>94</volume>, <fpage>855</fpage>–<lpage>857</lpage>. <pub-id pub-id-type="doi">10.1104/pp.94.3.855</pub-id><pub-id pub-id-type="pmid">16667862</pub-id></mixed-citation></ref><ref id="B40"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lim</surname><given-names>T. S.</given-names></name><name><surname>Chitra</surname><given-names>T. R.</given-names></name><name><surname>Han</surname><given-names>P.</given-names></name><name><surname>Pua</surname><given-names>E. C.</given-names></name><name><surname>Yu</surname><given-names>H.</given-names></name></person-group> (<year>2006</year>). <article-title>Cloning and characterization of Arabidopsis and <italic>Brassica juncea</italic> flavin containing amine oxidases</article-title>. <source>J. Exp. Bot.</source><volume>57</volume>, <fpage>4155</fpage>–<lpage>4169</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/erl193</pub-id><pub-id pub-id-type="pmid">17122409</pub-id></mixed-citation></ref><ref id="B41"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Liu</surname><given-names>T.</given-names></name><name><surname>Kim</surname><given-names>D. W.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Berberich</surname><given-names>T.</given-names></name><name><surname>Kusano</surname><given-names>T.</given-names></name></person-group> (<year>2014a</year>). <article-title><italic>Oryza sativa</italic> polyamine oxidase 1 back-converts tetraamines, spermine and thermospermine, to spermidine</article-title>. <source>Plant Cell Rep.</source><volume>33</volume>, <fpage>143</fpage>–<lpage>151</lpage>. <pub-id pub-id-type="doi">10.1007/s00299-013-1518-y</pub-id><pub-id pub-id-type="pmid">24105034</pub-id></mixed-citation></ref><ref id="B42"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Liu</surname><given-names>T.</given-names></name><name><surname>Kim</surname><given-names>D. W.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Berberich</surname><given-names>T.</given-names></name><name><surname>Kusano</surname><given-names>T.</given-names></name></person-group> (<year>2014c</year>). <article-title>POLYAMINE OXIDASE 1 from rice (<italic>Oryza sativa</italic>) is a functional ortholog of Arabidopsis POLYAMINE OXIDASE 5</article-title>. <source>Plant Signal Behav.</source><volume>9</volume>:<fpage>e29773</fpage>. <pub-id pub-id-type="doi">10.4161/psb.29773</pub-id><pub-id pub-id-type="pmid">25763711</pub-id></mixed-citation></ref><ref id="B43"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Liu</surname><given-names>T.</given-names></name><name><surname>Kim</surname><given-names>D. W.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Maeda</surname><given-names>S.</given-names></name><name><surname>Watanabe</surname><given-names>S.</given-names></name><name><surname>Kamio</surname><given-names>Y.</given-names></name><etal></etal></person-group>. (<year>2014b</year>). <article-title>Polyamine oxidase 7 is a terminal catabolism-type enzyme in <italic>Oryza sativa</italic> and is specifically expressed in anthers</article-title>. <source>Plant Cell Physiol.</source><volume>55</volume>, <fpage>1110</fpage>–<lpage>1122</lpage>. <pub-id pub-id-type="doi">10.1093/pcp/pcu047</pub-id><pub-id pub-id-type="pmid">24634478</pub-id></mixed-citation></ref><ref id="B44"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Marina</surname><given-names>M.</given-names></name><name><surname>Sirera</surname><given-names>F. V.</given-names></name><name><surname>Rambla</surname><given-names>J. L.</given-names></name><name><surname>Gonzalez</surname><given-names>M. E.</given-names></name><name><surname>Blázquez</surname><given-names>M. A.</given-names></name><name><surname>Carbonell</surname><given-names>J.</given-names></name><etal></etal></person-group>. (<year>2013</year>). <article-title>Thermospermine catabolism increases <italic>Arabidopsis thaliana</italic> resistance to <italic>Pseudomonas viridiflava</italic></article-title>. <source>J. Exp. Bot.</source><volume>64</volume>, <fpage>1393</fpage>–<lpage>13402</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/ert012</pub-id><pub-id pub-id-type="pmid">23382552</pub-id></mixed-citation></ref><ref id="B45"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>McWilliam</surname><given-names>H.</given-names></name><name><surname>Li</surname><given-names>W.</given-names></name><name><surname>Uludag</surname><given-names>M.</given-names></name><name><surname>Squizzato</surname><given-names>S.</given-names></name><name><surname>Park</surname><given-names>Y. M.</given-names></name><name><surname>Buso</surname><given-names>N.</given-names></name><etal></etal></person-group>. (<year>2013</year>). <article-title>Analysis Tool Web Services from the EMBL-EBI</article-title>. <source>Nucleic Acids Res</source>. <volume>41</volume>, <fpage>W597</fpage>–<lpage>W600</lpage>. <pub-id pub-id-type="doi">10.1093/nar/gkt376</pub-id><pub-id pub-id-type="pmid">23671338</pub-id></mixed-citation></ref><ref id="B46"><mixed-citation publication-type="book"><person-group person-group-type="author"><name><surname>Medda</surname><given-names>R.</given-names></name><name><surname>Bellelli</surname><given-names>A.</given-names></name><name><surname>Peč</surname><given-names>P.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Floris</surname><given-names>G.</given-names></name></person-group> (<year>2009</year>). <article-title>Copper Amine oxidases from plants</article-title>, in <source>Copper Amine Oxidases: Structure, Catalytic Mechanism and Role in Pathophysiology</source>, eds <person-group person-group-type="editor"><name><surname>Floris</surname><given-names>G.</given-names></name><name><surname>Mondovì</surname><given-names>B.</given-names></name></person-group> (<publisher-loc>Boca Raton, FL</publisher-loc>: <publisher-name>Taylor and Francis Group, C.R.C. Press</publisher-name>), <fpage>39</fpage>–<lpage>50</lpage>.</mixed-citation></ref><ref id="B47"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Medda</surname><given-names>R.</given-names></name><name><surname>Padiglia</surname><given-names>A.</given-names></name><name><surname>Finazzi Agrò</surname><given-names>A.</given-names></name><name><surname>Pedersen</surname><given-names>J. Z.</given-names></name><name><surname>Lorrai</surname><given-names>A.</given-names></name><name><surname>Floris</surname><given-names>G.</given-names></name></person-group> (<year>1997</year>). <article-title>Tryptamine as substrate and inhibitor of lentil seedling copper amine oxidase</article-title>. <source>Eur. J. Biochem.</source><volume>250</volume>, <fpage>377</fpage>–<lpage>382</lpage>. <pub-id pub-id-type="pmid">9428687</pub-id></mixed-citation></ref><ref id="B48"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Mo</surname><given-names>H.</given-names></name><name><surname>Wang</surname><given-names>X.</given-names></name><name><surname>Zhang</surname><given-names>Y.</given-names></name><name><surname>Zhang</surname><given-names>G.</given-names></name><name><surname>Zhang</surname><given-names>J. F.</given-names></name><name><surname>Ma</surname><given-names>Z. Y.</given-names></name></person-group> (<year>2015</year>). <article-title>Cotton polyamine oxidase is required for spermine and camalexin signalling in the defence response to <italic>Verticillium dahliae</italic></article-title>. <source>Plant J.</source><volume>83</volume>, <fpage>962</fpage>–<lpage>975</lpage>. <pub-id pub-id-type="doi">10.1111/tpj.12941</pub-id><pub-id pub-id-type="pmid">26221980</pub-id></mixed-citation></ref><ref id="B49"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Møller</surname><given-names>S. G.</given-names></name><name><surname>McPherson</surname><given-names>M. J.</given-names></name></person-group> (<year>1998</year>). <article-title>Developmental expression and biochemical analysis of the <italic>Arabidopsis atao1</italic> gene encoding an H<sub>2</sub>O<sub>2</sub>-generating diamine oxidase</article-title>. <source>Plant J.</source><volume>13</volume>, <fpage>781</fpage>–<lpage>791</lpage>. <pub-id pub-id-type="doi">10.1046/j.1365-313X.1998.00080.x</pub-id><pub-id pub-id-type="pmid">9681017</pub-id></mixed-citation></ref><ref id="B50"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Monshausen</surname><given-names>G. B.</given-names></name><name><surname>Bibikova</surname><given-names>T. N.</given-names></name><name><surname>Messerli</surname><given-names>M. A.</given-names></name><name><surname>Shi</surname><given-names>C.</given-names></name><name><surname>Gilroy</surname><given-names>S.</given-names></name></person-group> (<year>2007</year>). <article-title>Oscillations in extracellular pH and reactive oxygen species modulate tip growth of Arabidopsis root hairs</article-title>. <source>Proc. Natl. Acad. Sci. U.S.A.</source><volume>104</volume>, <fpage>20996</fpage>–<lpage>21001</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.0708586104</pub-id><pub-id pub-id-type="pmid">18079291</pub-id></mixed-citation></ref><ref id="B51"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Paschalidis</surname><given-names>K. A.</given-names></name><name><surname>Delis</surname><given-names>I. D.</given-names></name><name><surname>Andriopoulou</surname><given-names>A. H.</given-names></name><name><surname>Lagiotis</surname><given-names>G. D.</given-names></name><name><surname>Yakoumakis</surname><given-names>D. I.</given-names></name><etal></etal></person-group>. (<year>2008a</year>). <article-title>Spermidine exodus and oxidation in the apoplast induced by abiotic stress is responsible for H<sub>2</sub>O<sub>2</sub> signatures that direct tolerance responses in tobacco</article-title>. <source>Plant Cell</source><volume>20</volume>, <fpage>1708</fpage>–<lpage>1724</lpage>. <pub-id pub-id-type="doi">10.1105/tpc.108.059733</pub-id><pub-id pub-id-type="pmid">18577660</pub-id></mixed-citation></ref><ref id="B52"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Sanmartin</surname><given-names>M.</given-names></name><name><surname>Andriopoulou</surname><given-names>A. H.</given-names></name><name><surname>Rojo</surname><given-names>E.</given-names></name><name><surname>Sanchez-Serrano</surname><given-names>J. J.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name></person-group> (<year>2008b</year>). <article-title>Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis</article-title>. <source>Plant Physiol.</source><volume>47</volume>, <fpage>1845</fpage>–<lpage>1857</lpage>. <pub-id pub-id-type="doi">10.1104/pp.108.123802</pub-id><pub-id pub-id-type="pmid">18583528</pub-id></mixed-citation></ref><ref id="B53"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Wu</surname><given-names>J.</given-names></name><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name></person-group> (<year>2012</year>). <article-title>The polyamines and their catabolic products are significant players in the turnover of nitrogenous molecules in plants</article-title>. <source>J. Exp. Bot.</source><volume>63</volume>, <fpage>5003</fpage>–<lpage>5015</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/ers202</pub-id><pub-id pub-id-type="pmid">22936828</pub-id></mixed-citation></ref><ref id="B54"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Müller</surname><given-names>K.</given-names></name><name><surname>Linkies</surname><given-names>A.</given-names></name><name><surname>Vreeburg</surname><given-names>R. A.</given-names></name><name><surname>Fry</surname><given-names>S. C.</given-names></name><name><surname>Krieger-Liszkay</surname><given-names>A.</given-names></name><name><surname>Leubner-Metzger</surname><given-names>G.</given-names></name></person-group> (<year>2009</year>). <article-title><italic>In vivo</italic> cell wall loosening by hydroxyl radicals during cress seed germination and elongation growth</article-title>. <source>Plant Physiol.</source><volume>150</volume>, <fpage>1855</fpage>–<lpage>1865</lpage>. <pub-id pub-id-type="doi">10.1104/pp.109.139204</pub-id><pub-id pub-id-type="pmid">19493972</pub-id></mixed-citation></ref><ref id="B55"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Murata</surname><given-names>Y.</given-names></name><name><surname>Mori</surname><given-names>I. C.</given-names></name><name><surname>Munemasa</surname><given-names>S.</given-names></name></person-group> (<year>2015</year>). <article-title>Diverse stomatal signaling and the signal integration mechanism</article-title>. <source>Annu. Rev. Plant Biol.</source><volume>66</volume>, <fpage>369</fpage>–<lpage>392</lpage>. <pub-id pub-id-type="doi">10.1146/annurev-arplant-043014-114707</pub-id><pub-id pub-id-type="pmid">25665132</pub-id></mixed-citation></ref><ref id="B56"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Naconsie</surname><given-names>M.</given-names></name><name><surname>Kato</surname><given-names>K.</given-names></name><name><surname>Shoji</surname><given-names>T.</given-names></name><name><surname>Hashimoto</surname><given-names>T.</given-names></name></person-group> (<year>2014</year>). <article-title>Molecular evolution of N-methylputrescine oxidase in tobacco</article-title>. <source>Plant Cell Physiol.</source><volume>55</volume>, <fpage>436</fpage>–<lpage>444</lpage>. <pub-id pub-id-type="doi">10.1093/pcp/pct179</pub-id><pub-id pub-id-type="pmid">24287136</pub-id></mixed-citation></ref><ref id="B57"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ono</surname><given-names>Y.</given-names></name><name><surname>Kim</surname><given-names>D. W.</given-names></name><name><surname>Watanabe</surname><given-names>K.</given-names></name><name><surname>Sasaki</surname><given-names>A.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Berberich</surname><given-names>T.</given-names></name><etal></etal></person-group>. (<year>2012</year>). <article-title>Constitutively and highly expressed <italic>Oryza sativa</italic> polyamine oxidases localize in peroxisomes and catalyze polyamine back conversion</article-title>. <source>Amino Acids</source><volume>42</volume>, <fpage>867</fpage>–<lpage>876</lpage>. <pub-id pub-id-type="doi">10.1007/s00726-011-1002-3</pub-id><pub-id pub-id-type="pmid">21796433</pub-id></mixed-citation></ref><ref id="B58"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Padiglia</surname><given-names>A.</given-names></name><name><surname>Medda</surname><given-names>R.</given-names></name><name><surname>Scanu</surname><given-names>T.</given-names></name><name><surname>Longu</surname><given-names>S.</given-names></name><name><surname>Rossi</surname><given-names>A.</given-names></name><name><surname>Floris</surname><given-names>G.</given-names></name></person-group> (<year>2002</year>). <article-title>Structure and nucleotide sequence of <italic>Euphorbia characias</italic> copper/TPQ-containing amine oxidase gene</article-title>. <source>J. Protein Chem</source>. <volume>21</volume>, <fpage>435</fpage>–<lpage>441</lpage>. <pub-id pub-id-type="doi">10.1023/A:1021337302116</pub-id><pub-id pub-id-type="pmid">12523646</pub-id></mixed-citation></ref><ref id="B59"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pál</surname><given-names>M.</given-names></name><name><surname>Szalai</surname><given-names>G.</given-names></name><name><surname>Janda</surname><given-names>T.</given-names></name></person-group> (<year>2015</year>). <article-title>Speculation: polyamines are important in abiotic stress signaling</article-title>. <source>Plant Sci.</source><volume>237</volume>, <fpage>16</fpage>–<lpage>23</lpage>. <pub-id pub-id-type="doi">10.1016/j.plantsci.2015.05.003</pub-id><pub-id pub-id-type="pmid">26089148</pub-id></mixed-citation></ref><ref id="B60"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Paschalidis</surname><given-names>K. A.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name></person-group> (<year>2005</year>). <article-title>Sites and regulation of polyamine catabolism in the tobacco plant. Correlations with cell division/expansion, cell cycle progression, and vascular development</article-title>. <source>Plant Physiol.</source><volume>138</volume>, <fpage>2174</fpage>–<lpage>2184</lpage>. <pub-id pub-id-type="doi">10.1104/pp.105.063941</pub-id><pub-id pub-id-type="pmid">16040649</pub-id></mixed-citation></ref><ref id="B61"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Paschalidis</surname><given-names>K. A.</given-names></name><name><surname>Toumi</surname><given-names>I.</given-names></name><name><surname>Moschou</surname><given-names>N. P.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name></person-group> (<year>2010</year>). <article-title>ABA-dependent amine oxidases-derived H<sub>2</sub>O<sub>2</sub> affects stomata conductance</article-title>. <source>Plant Signal Behav.</source><volume>5</volume>, <fpage>1153</fpage>–<lpage>1156</lpage>. <pub-id pub-id-type="doi">10.4161/psb.5.9.12679</pub-id><pub-id pub-id-type="pmid">21490422</pub-id></mixed-citation></ref><ref id="B62"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pegg</surname><given-names>A. E.</given-names></name></person-group> (<year>2014</year>). <article-title>The function of spermine</article-title>. <source>IUBMB Life</source><volume>66</volume>, <fpage>8</fpage>–<lpage>18</lpage>. <pub-id pub-id-type="doi">10.1002/iub.1237</pub-id><pub-id pub-id-type="pmid">24395705</pub-id></mixed-citation></ref><ref id="B63"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pintus</surname><given-names>F.</given-names></name><name><surname>Spanò</surname><given-names>D.</given-names></name><name><surname>Floris</surname><given-names>G.</given-names></name><name><surname>Medda</surname><given-names>R.</given-names></name></person-group> (<year>2013</year>). <article-title><italic>Euphorbia characias</italic> latex amine oxidase and peroxidase: interacting enzymes?</article-title><source>Protein J.</source><volume>32</volume>, <fpage>435</fpage>–<lpage>441</lpage>. <pub-id pub-id-type="doi">10.1007/s10930-013-9501-6</pub-id><pub-id pub-id-type="pmid">23839010</pub-id></mixed-citation></ref><ref id="B64"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Planas-Portell</surname><given-names>J.</given-names></name><name><surname>Gallart</surname><given-names>M.</given-names></name><name><surname>Tiburcio</surname><given-names>A. F.</given-names></name><name><surname>Altabella</surname><given-names>T.</given-names></name></person-group> (<year>2013</year>). <article-title>Copper containing amine oxidases contribute to terminal polyamine oxidation in peroxisomes and apoplast of <italic>Arabidopsis thaliana</italic></article-title>. <source>BMC Plant Biol.</source><volume>13</volume>:<fpage>109</fpage>. <pub-id pub-id-type="doi">10.1186/1471-2229-13-109</pub-id><pub-id pub-id-type="pmid">23915037</pub-id></mixed-citation></ref><ref id="B65"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pottosin</surname><given-names>I.</given-names></name><name><surname>Velarde-Buendía</surname><given-names>A. M.</given-names></name><name><surname>Bose</surname><given-names>J.</given-names></name><name><surname>Zepeda-Jazo</surname><given-names>I.</given-names></name><name><surname>Shabala</surname><given-names>S.</given-names></name><name><surname>Dobrovinskaya</surname><given-names>O.</given-names></name></person-group> (<year>2014</year>). <article-title>Cross-talk between reactive oxygen species and polyamines in regulation of ion transport across the plasma membrane: implications for plant adaptive responses</article-title>. <source>J. Exp. Bot.</source><volume>65</volume>, <fpage>1271</fpage>–<lpage>1283</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/ert423</pub-id><pub-id pub-id-type="pmid">24465010</pub-id></mixed-citation></ref><ref id="B66"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Qu</surname><given-names>Y.</given-names></name><name><surname>An</surname><given-names>Z.</given-names></name><name><surname>Zhuang</surname><given-names>B.</given-names></name><name><surname>Jing</surname><given-names>W.</given-names></name><name><surname>Zhang</surname><given-names>Q.</given-names></name><name><surname>Zhang</surname><given-names>W.</given-names></name></person-group> (<year>2014</year>). <article-title>Copper amine oxidase and phospholipase D act independently in abscisic acid (ABA)-induced stomatal closure in <italic>Vicia faba</italic> and Arabidopsis</article-title>. <source>J. Plant Res.</source><volume>127</volume>, <fpage>533</fpage>–<lpage>544</lpage>. <pub-id pub-id-type="doi">10.1007/s10265-014-0633-3</pub-id><pub-id pub-id-type="pmid">24817219</pub-id></mixed-citation></ref><ref id="B67"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rea</surname><given-names>G.</given-names></name><name><surname>de Pinto</surname><given-names>M. C.</given-names></name><name><surname>Tavazza</surname><given-names>R.</given-names></name><name><surname>Biondi</surname><given-names>S.</given-names></name><name><surname>Gobbi</surname><given-names>V.</given-names></name><name><surname>Ferrante</surname><given-names>P.</given-names></name><etal></etal></person-group>. (<year>2004</year>). <article-title>Ectopic expression of maize polyamine oxidase and pea copper amine oxidase in the cell wall of tobacco plants</article-title>. <source>Plant Physiol.</source><volume>134</volume>, <fpage>1414</fpage>–<lpage>1426</lpage>. <pub-id pub-id-type="doi">10.1104/pp.103.036764</pub-id><pub-id pub-id-type="pmid">15064377</pub-id></mixed-citation></ref><ref id="B68"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rea</surname><given-names>G.</given-names></name><name><surname>Metoui</surname><given-names>O.</given-names></name><name><surname>Infantino</surname><given-names>A.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name></person-group> (<year>2002</year>). <article-title>Copper amine oxidase expression in defense responses to wounding and <italic>Ascochyta rabiei</italic> invasion</article-title>. <source>Plant Physiol.</source><volume>128</volume>, <fpage>865</fpage>–<lpage>875</lpage>. <pub-id pub-id-type="doi">10.1104/pp.010646</pub-id><pub-id pub-id-type="pmid">11891243</pub-id></mixed-citation></ref><ref id="B69"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Roach</surname><given-names>T.</given-names></name><name><surname>Colville</surname><given-names>L.</given-names></name><name><surname>Beckett</surname><given-names>R. P.</given-names></name><name><surname>Minibayeva</surname><given-names>F. V.</given-names></name><name><surname>Havaux</surname><given-names>M.</given-names></name><name><surname>Kranner</surname><given-names>I.</given-names></name></person-group> (<year>2015</year>). <article-title>A proposed interplay between peroxidase, amine oxidase and lipoxygenase in the wounding-induced oxidative burst in <italic>Pisum sativum</italic> seedlings</article-title>. <source>Phytochemistry</source><volume>112</volume>, <fpage>130</fpage>–<lpage>1388</lpage>. <pub-id pub-id-type="doi">10.1016/j.phytochem.2014.06.003</pub-id><pub-id pub-id-type="pmid">24996671</pub-id></mixed-citation></ref><ref id="B70"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rodríguez</surname><given-names>A. A.</given-names></name><name><surname>Maiale</surname><given-names>S. J.</given-names></name><name><surname>Menéndez</surname><given-names>A. B.</given-names></name><name><surname>Ruiz</surname><given-names>O. A.</given-names></name></person-group> (<year>2009</year>). <article-title>Polyamine oxidase activity contributes to sustain maize leaf elongation under saline stress</article-title>. <source>J. Exp. Bot.</source><volume>60</volume>, <fpage>4249</fpage>–<lpage>4262</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/erp256</pub-id><pub-id pub-id-type="pmid">19717530</pub-id></mixed-citation></ref><ref id="B71"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rossi</surname><given-names>A.</given-names></name><name><surname>Petruzzelli</surname><given-names>R.</given-names></name><name><surname>Agrò</surname><given-names>A. F.</given-names></name></person-group> (<year>1992</year>). <article-title>cDNA-derived amino-acid sequence of lentil seedlings' amine oxidase</article-title>. <source>FEBS Lett.</source><volume>301</volume>, <fpage>253</fpage>–<lpage>257</lpage>. <pub-id pub-id-type="doi">10.1016/0014-5793(92)80251-B</pub-id><pub-id pub-id-type="pmid">1577161</pub-id></mixed-citation></ref><ref id="B72"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sagor</surname><given-names>G. H.</given-names></name><name><surname>Inoue</surname><given-names>M.</given-names></name><name><surname>Kim</surname><given-names>D. W.</given-names></name><name><surname>Kojima</surname><given-names>S.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Berberich</surname><given-names>T.</given-names></name><etal></etal></person-group>. (<year>2015</year>). <article-title>The polyamine oxidase from lycophyte <italic>Selaginella lepidophylla</italic> (SelPAO5), unlike that of angiosperms, back-converts thermospermine to norspermidine</article-title>. <source>FEBS Lett.</source><volume>589</volume>, <fpage>3071</fpage>–<lpage>3078</lpage>. <pub-id pub-id-type="doi">10.1016/j.febslet.2015.08.045</pub-id><pub-id pub-id-type="pmid">26348400</pub-id></mixed-citation></ref><ref id="B73"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sagor</surname><given-names>G. H. M.</given-names></name><name><surname>Zhang</surname><given-names>S.</given-names></name><name><surname>Kojima</surname><given-names>S.</given-names></name><name><surname>Simm</surname><given-names>S.</given-names></name><name><surname>Berberich</surname><given-names>T.</given-names></name><name><surname>Kusano</surname><given-names>T.</given-names></name></person-group> (<year>2016</year>). <article-title>Reducing cytoplasmic polyamine oxidase activity in Arabidopsis increases salt and drought tolerance by reducing reactive oxygen species production and increasing defense gene expression</article-title>. <source>Front. Plant Sci.</source><volume>7</volume>:<issue>214</issue>. <pub-id pub-id-type="doi">10.3389/fpls.2016.00214</pub-id><pub-id pub-id-type="pmid">26973665</pub-id></mixed-citation></ref><ref id="B74"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Schopfer</surname><given-names>P.</given-names></name><name><surname>Liszkay</surname><given-names>A.</given-names></name><name><surname>Bechtold</surname><given-names>M.</given-names></name><name><surname>Frahry</surname><given-names>G.</given-names></name><name><surname>Wagner</surname><given-names>A.</given-names></name></person-group> (<year>2002</year>). <article-title>Evidence that hydroxyl radicals mediate auxin-induced extension growth</article-title>. <source>Planta.</source><volume>214</volume>, <fpage>821</fpage>–<lpage>828</lpage>. <pub-id pub-id-type="doi">10.1007/s00425-001-0699-8</pub-id><pub-id pub-id-type="pmid">11941457</pub-id></mixed-citation></ref><ref id="B75"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sequera-Mutiozabal</surname><given-names>M. I.</given-names></name><name><surname>Erban</surname><given-names>A.</given-names></name><name><surname>Kopka J</surname><given-names>Atanasov, K. E.</given-names></name><name><surname>Bastida</surname><given-names>J.</given-names></name><name><surname>Fotopoulos</surname><given-names>V.</given-names></name><etal></etal></person-group>. (<year>2016</year>). <article-title>Global metabolic profiling of Arabidopsis polyamine oxidase 4 (AtPAO4) loss-of-function mutants exhibiting delayed dark-induced senescence</article-title>. <source>Front. Plant Sci.</source><volume>7</volume>:<issue>173</issue>. <pub-id pub-id-type="doi">10.3389/fpls.2016.00173</pub-id><pub-id pub-id-type="pmid">26925084</pub-id></mixed-citation></ref><ref id="B76"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Shoresh</surname><given-names>M.</given-names></name><name><surname>Spivak</surname><given-names>M.</given-names></name><name><surname>Bernstein</surname><given-names>N.</given-names></name></person-group> (<year>2011</year>). <article-title>Involvement of calcium-mediated effects on ROS metabolism in the regulation of growth improvement under salinity</article-title>. <source>Free Radic Biol Med.</source><volume>51</volume>, <fpage>1221</fpage>–<lpage>1234</lpage>. <pub-id pub-id-type="doi">10.1016/j.freeradbiomed.2011.03.036</pub-id><pub-id pub-id-type="pmid">21466848</pub-id></mixed-citation></ref><ref id="B77"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Strohm</surname><given-names>A. K.</given-names></name><name><surname>Vaughn</surname><given-names>L. M.</given-names></name><name><surname>Masson</surname><given-names>P. H.</given-names></name></person-group> (<year>2015</year>). <article-title>Natural variation in the expression of ORGANIC CATION TRANSPORTER 1 affects root length responses to cadaverine in Arabidopsis</article-title>. <source>J. Exp. Bot.</source><volume>66</volume>, <fpage>853</fpage>–<lpage>862</lpage>. <pub-id pub-id-type="doi">10.1093/jxb/eru444</pub-id><pub-id pub-id-type="pmid">25403917</pub-id></mixed-citation></ref><ref id="B78"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Takahashi</surname><given-names>T.</given-names></name><name><surname>Kakehi</surname><given-names>J.</given-names></name></person-group> (<year>2010</year>). <article-title>Polyamines: ubiquitous polycations with unique roles in growth and stress responses</article-title>. <source>Ann. Bot.</source><volume>105</volume>, <fpage>1</fpage>–<lpage>6</lpage>. <pub-id pub-id-type="doi">10.1093/aob/mcp259</pub-id><pub-id pub-id-type="pmid">19828463</pub-id></mixed-citation></ref><ref id="B79"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Takahashi</surname><given-names>Y.</given-names></name><name><surname>Cong</surname><given-names>R.</given-names></name><name><surname>Sagor</surname><given-names>G. H.</given-names></name><name><surname>Niitsu</surname><given-names>M.</given-names></name><name><surname>Berberich</surname><given-names>T.</given-names></name><name><surname>Kusano</surname><given-names>T.</given-names></name></person-group> (<year>2010</year>). <article-title>Characterization of five polyamine oxidase isoforms in <italic>Arabidopsis thaliana</italic></article-title>. <source>Plant Cell Rep.</source><volume>29</volume>, <fpage>955</fpage>–<lpage>965</lpage>. <pub-id pub-id-type="doi">10.1007/s00299-010-0881-1</pub-id><pub-id pub-id-type="pmid">20532512</pub-id></mixed-citation></ref><ref id="B80"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tamura</surname><given-names>K.</given-names></name><name><surname>Peterson</surname><given-names>D.</given-names></name><name><surname>Peterson</surname><given-names>N.</given-names></name><name><surname>Stecher</surname><given-names>G.</given-names></name><name><surname>Nei</surname><given-names>M.</given-names></name><name><surname>Kumar</surname><given-names>S.</given-names></name></person-group> (<year>2011</year>). <article-title>MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods</article-title>. <source>Mol. Biol. Evol.</source><volume>28</volume>, <fpage>2731</fpage>–<lpage>2739</lpage>. <pub-id pub-id-type="doi">10.1093/molbev/msr121</pub-id><pub-id pub-id-type="pmid">21546353</pub-id></mixed-citation></ref><ref id="B81"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Tempera</surname><given-names>G.</given-names></name><name><surname>Viceconte</surname><given-names>N.</given-names></name><name><surname>Saccoccio</surname><given-names>S.</given-names></name><etal></etal></person-group>. (<year>2012</year>). <article-title>Polyamine catabolism: target for antiproliferative therapies in animals and stress tolerance strategies in plants</article-title>. <source>Amino Acids</source><volume>42</volume>, <fpage>411</fpage>–<lpage>426</lpage>. <pub-id pub-id-type="doi">10.1007/s00726-011-1012-1</pub-id><pub-id pub-id-type="pmid">21874532</pub-id></mixed-citation></ref><ref id="B82"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><name><surname>Rossi</surname><given-names>M. N.</given-names></name><name><surname>Saccuti</surname><given-names>G.</given-names></name><name><surname>Perez-Amador</surname><given-names>M. A.</given-names></name><name><surname>Polticelli</surname><given-names>F.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><etal></etal></person-group>. (<year>2006</year>). <article-title>Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion</article-title>. <source>Plant Physiol.</source><volume>141</volume>, <fpage>1519</fpage>–<lpage>1532</lpage>. <pub-id pub-id-type="doi">10.1104/pp.106.080911</pub-id><pub-id pub-id-type="pmid">16778015</pub-id></mixed-citation></ref><ref id="B83"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><name><surname>Schininà</surname><given-names>M. E.</given-names></name><name><surname>Cecconi</surname><given-names>F.</given-names></name><name><surname>Di Agostino</surname><given-names>S.</given-names></name><name><surname>Manera</surname><given-names>F.</given-names></name><name><surname>Rea</surname><given-names>G.</given-names></name><etal></etal></person-group>. (<year>1998</year>). <article-title>Maize polyamine oxidase: primary structure from protein and cDNA sequencing</article-title>. <source>FEBS Lett.</source><volume>426</volume>, <fpage>62</fpage>–<lpage>66</lpage>. <pub-id pub-id-type="doi">10.1016/S0014-5793(98)00311-1</pub-id><pub-id pub-id-type="pmid">9598979</pub-id></mixed-citation></ref><ref id="B84"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tiburcio</surname><given-names>A. F.</given-names></name><name><surname>Altabella</surname><given-names>T.</given-names></name><name><surname>Bitrián</surname><given-names>M.</given-names></name><name><surname>Alcázar</surname><given-names>R.</given-names></name></person-group> (<year>2014</year>). <article-title>The roles of polyamines during the lifespan of plants: from development to stress</article-title>. <source>Planta</source><volume>240</volume>, <fpage>1</fpage>–<lpage>18</lpage>. <pub-id pub-id-type="doi">10.1007/s00425-014-2055-9</pub-id><pub-id pub-id-type="pmid">24659098</pub-id></mixed-citation></ref><ref id="B85"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tipping</surname><given-names>A. J.</given-names></name><name><surname>McPherson</surname><given-names>M. J.</given-names></name></person-group> (<year>1995</year>). <article-title>Cloning and molecular analysis of the pea seedling copper amine oxidase</article-title>. <source>J. Biol. Chem.</source><volume>270</volume>, <fpage>16939</fpage>–<lpage>16946</lpage>. <pub-id pub-id-type="pmid">7622512</pub-id></mixed-citation></ref><ref id="B86"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tisi</surname><given-names>A.</given-names></name><name><surname>Federico</surname><given-names>R.</given-names></name><name><surname>Moreno</surname><given-names>S.</given-names></name><name><surname>Lucretti</surname><given-names>S.</given-names></name><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Roubelakis-Angelakis</surname><given-names>K. A.</given-names></name><etal></etal></person-group>. (<year>2011</year>). <article-title>Perturbation of polyamine catabolism can strongly affect root development and xylem differentiation</article-title>. <source>Plant Physiol.</source><volume>157</volume>, <fpage>200</fpage>–<lpage>215</lpage>. <pub-id pub-id-type="doi">10.1104/pp.111.173153</pub-id><pub-id pub-id-type="pmid">21746808</pub-id></mixed-citation></ref><ref id="B87"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tsaniklidis</surname><given-names>G.</given-names></name><name><surname>Kotsiras</surname><given-names>A.</given-names></name><name><surname>Tsafouros</surname><given-names>A.</given-names></name><name><surname>Roussos</surname><given-names>P. A.</given-names></name><name><surname>Aivalakis</surname><given-names>G.</given-names></name><name><surname>Katinakis</surname><given-names>P.</given-names></name><etal></etal></person-group>. (<year>2016</year>). <article-title>Spatial and temporal distribution of genes involved in polyamine metabolism during tomato fruit development</article-title>. <source>Plant Physiol. Biochem.</source><volume>100</volume>, <fpage>27</fpage>–<lpage>36</lpage>. <pub-id pub-id-type="doi">10.1016/j.plaphy.2016.01.001</pub-id><pub-id pub-id-type="pmid">26773542</pub-id></mixed-citation></ref><ref id="B88"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tsukagoshi</surname><given-names>H.</given-names></name><name><surname>Busch</surname><given-names>W.</given-names></name><name><surname>Benfey</surname><given-names>P. N.</given-names></name></person-group> (<year>2010</year>). <article-title>Transcriptional regulation of ROS controls transition from proliferation to differentiation in the root</article-title>. <source>Cell</source><volume>143</volume>, <fpage>606</fpage>–<lpage>616</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2010.10.020</pub-id><pub-id pub-id-type="pmid">21074051</pub-id></mixed-citation></ref><ref id="B89"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tun</surname><given-names>N. N.</given-names></name><name><surname>Santa-Catarina</surname><given-names>C.</given-names></name><name><surname>Begum</surname><given-names>T.</given-names></name><name><surname>Silveira</surname><given-names>V.</given-names></name><name><surname>Handro</surname><given-names>W.</given-names></name><name><surname>Floh</surname><given-names>E. I.</given-names></name><etal></etal></person-group>. (<year>2006</year>). <article-title>Polyamines induce rapid biosynthesis of nitric oxide (NO) in <italic>Arabidopsis thaliana</italic> seedlings</article-title>. <source>Plant Cell Physiol.</source><volume>47</volume>, <fpage>346</fpage>–<lpage>354</lpage>. <pub-id pub-id-type="doi">10.1093/pcp/pci252</pub-id><pub-id pub-id-type="pmid">16415068</pub-id></mixed-citation></ref><ref id="B90"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wang</surname><given-names>W.</given-names></name><name><surname>Liu</surname><given-names>J. H.</given-names></name></person-group> (<year>2015</year>). <article-title>Genome-wide identification and expression analysis of the polyamine oxidase gene family in sweet orange (<italic>Citrus sinensis</italic>)</article-title>. <source>Gene</source><volume>555</volume>, <fpage>421</fpage>–<lpage>429</lpage>. <pub-id pub-id-type="doi">10.1016/j.gene.2014.11.042</pub-id><pub-id pub-id-type="pmid">25445392</pub-id></mixed-citation></ref><ref id="B91"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wimalasekera</surname><given-names>R.</given-names></name><name><surname>Schaarschmidt</surname><given-names>F.</given-names></name><name><surname>Angelini</surname><given-names>R.</given-names></name><name><surname>Cona</surname><given-names>A.</given-names></name><name><surname>Tavladoraki</surname><given-names>P.</given-names></name><name><surname>Scherer</surname><given-names>G. F.</given-names></name></person-group> (<year>2015</year>). <article-title>POLYAMINE OXIDASE2 of Arabidopsis contributes to ABA mediated plant developmental processes</article-title>. <source>Plant Physiol. Biochem.</source><volume>96</volume>, <fpage>231</fpage>–<lpage>240</lpage>. <pub-id pub-id-type="doi">10.1016/j.plaphy.2015.08.003</pub-id><pub-id pub-id-type="pmid">26310141</pub-id></mixed-citation></ref><ref id="B92"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wimalasekera</surname><given-names>R.</given-names></name><name><surname>Villar</surname><given-names>C.</given-names></name><name><surname>Begum</surname><given-names>T.</given-names></name><name><surname>Scherer</surname><given-names>G. F.</given-names></name></person-group> (<year>2011</year>). <article-title>COPPER AMINE OXIDASE1 (CuAO1) of <italic>Arabidopsis thaliana</italic> contributes to abscisic acid- and polyamine-induced nitric oxide biosynthesis and abscisic acid signal transduction</article-title>. <source>Mol. Plant.</source><volume>4</volume>, <fpage>663</fpage>–<lpage>678</lpage>. <pub-id pub-id-type="doi">10.1093/mp/ssr023</pub-id><pub-id pub-id-type="pmid">21471330</pub-id></mixed-citation></ref><ref id="B93"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wu</surname><given-names>J.</given-names></name><name><surname>Shang</surname><given-names>Z.</given-names></name><name><surname>Wu</surname><given-names>J.</given-names></name><name><surname>Jiang</surname><given-names>X.</given-names></name><name><surname>Moschou</surname><given-names>P. N.</given-names></name><name><surname>Sun</surname><given-names>W.</given-names></name><etal></etal></person-group>. (<year>2010</year>). <article-title>Spermidine oxidase-derived H<sub>2</sub>O<sub>2</sub> regulates pollen plasma membrane hyperpolarization-activated Ca<sup>2+</sup>-permeable channels and pollen tube growth</article-title>. <source>Plant J.</source><volume>63</volume>, <fpage>1042</fpage>–<lpage>1053</lpage>. <pub-id pub-id-type="doi">10.1111/j.1365-313X.2010.04301.x</pub-id><pub-id pub-id-type="pmid">20626657</pub-id></mixed-citation></ref><ref id="B94"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yoda</surname><given-names>H.</given-names></name><name><surname>Yamaguchi</surname><given-names>Y.</given-names></name><name><surname>Sano</surname><given-names>H.</given-names></name></person-group> (<year>2003</year>). <article-title>Induction of hypersensitive cell death by hydrogen peroxide produced through polyamine degradation in tobacco plants</article-title>. <source>Plant Physiol.</source><volume>132</volume>, <fpage>1973</fpage>–<lpage>1981</lpage>. <pub-id pub-id-type="doi">10.1104/pp.103.024737</pub-id><pub-id pub-id-type="pmid">12913153</pub-id></mixed-citation></ref><ref id="B95"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yoshimoto</surname><given-names>K.</given-names></name><name><surname>Takamura</surname><given-names>H.</given-names></name><name><surname>Kadota</surname><given-names>I.</given-names></name><name><surname>Motose</surname><given-names>H.</given-names></name><name><surname>Takahashi</surname><given-names>T.</given-names></name></person-group> (<year>2016</year>). <article-title>Chemical control of xylem differentiation by thermospermine, xylemin, and auxin</article-title>. <source>Sci. Rep.</source><volume>6</volume>, <fpage>21487</fpage>. <pub-id pub-id-type="doi">10.1038/srep21487</pub-id><pub-id pub-id-type="pmid">26879262</pub-id></mixed-citation></ref><ref id="B96"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Zarei</surname><given-names>A.</given-names></name><name><surname>Trobacher</surname><given-names>C. P.</given-names></name><name><surname>Cooke</surname><given-names>A. R.</given-names></name><name><surname>Meyers</surname><given-names>A. J.</given-names></name><name><surname>Hall</surname><given-names>J. C.</given-names></name><name><surname>Shelp</surname><given-names>B. J.</given-names></name></person-group> (<year>2015a</year>). <article-title>Apple fruit copper amine oxidase isoforms: peroxisomal MdAO1 prefers diamines as substrates, whereas extracellular MdAO2 exclusively utilizes monoamines</article-title>. <source>Plant Cell Physiol.</source><volume>56</volume>, <fpage>137</fpage>–<lpage>147</lpage>. <pub-id pub-id-type="doi">10.1093/pcp/pcu155</pub-id><pub-id pub-id-type="pmid">25378687</pub-id></mixed-citation></ref><ref id="B97"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Zarei</surname><given-names>A.</given-names></name><name><surname>Trobacher</surname><given-names>C. P.</given-names></name><name><surname>Shelp</surname><given-names>B. J.</given-names></name></person-group> (<year>2015b</year>). <article-title>NAD<sup>+</sup>-aminoaldehyde dehydrogenase candidates for 4-aminobutyrate (GABA) and β-alanine production during terminal oxidation of polyamines in apple fruit</article-title>. <source>FEBS Lett.</source><volume>589</volume>, <fpage>2695</fpage>–<lpage>2700</lpage>. <pub-id pub-id-type="doi">10.1016/j.febslet.2015.08.005</pub-id><pub-id pub-id-type="pmid">26296314</pub-id></mixed-citation></ref><ref id="B98"><mixed-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Zarza</surname><given-names>X.</given-names></name><name><surname>Atanasov</surname><given-names>K. E.</given-names></name><name><surname>Marco</surname><given-names>F.</given-names></name><name><surname>Arbona</surname><given-names>V.</given-names></name><name><surname>Carrasco</surname><given-names>P.</given-names></name><name><surname>Kopka</surname><given-names>J.</given-names></name><etal></etal></person-group>. (<year>2016</year>). <article-title>Polyamine oxidase 5 loss-of-function mutations in Arabidopsis thaliana trigger metabolic and transcriptional reprogramming and promote salt stress tolerance</article-title>. <source>Plant Cell Environ.</source> [Epub ahead of print]. <pub-id pub-id-type="doi">10.1111/pce.12714.</pub-id><pub-id pub-id-type="pmid">26791972</pub-id></mixed-citation></ref></ref-list></back></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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