A novel role for 12/15-lipoxygenase in regulating autophagy
Identifieur interne : 004491 ( Main/Merge ); précédent : 004490; suivant : 004492A novel role for 12/15-lipoxygenase in regulating autophagy
Auteurs : Alwena H. Morgan [Royaume-Uni] ; Victoria J. Hammond [Royaume-Uni] ; Machiko Sakoh-Nakatogawa [Japon] ; Yoshinori Ohsumi [Japon] ; Christopher P. Thomas [Royaume-Uni] ; Fabien Blanchet [Royaume-Uni] ; Vincent Piguet [Royaume-Uni] ; Kirill Kiselyov [États-Unis] ; Valerie B. O Onnell [Royaume-Uni]Source :
- Redox Biology [ 2213-2317 ] ; 2014.
Descripteurs français
- KwdFr :
- Acide éicosatétraénoïque-5,8,10,14 hydroxy-12 (analogues et dérivés), Acide éicosatétraénoïque-5,8,10,14 hydroxy-12 (métabolisme), Animaux, Arachidonate 12-lipoxygenase (génétique), Arachidonate 12-lipoxygenase (métabolisme), Arachidonate 15-lipoxygenase (génétique), Arachidonate 15-lipoxygenase (métabolisme), Autophagie (génétique), Famille de la protéine-8 associée à l'autophagie, Macrophages (métabolisme), Mitochondries (métabolisme), Métabolisme des lipides (génétique), Oxydoréduction, Phospholipides (métabolisme), Protéines associées aux microtubules (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae, Souris.
- MESH :
- analogues et dérivés : Acide éicosatétraénoïque-5,8,10,14 hydroxy-12.
- génétique : Arachidonate 12-lipoxygenase, Arachidonate 15-lipoxygenase, Autophagie, Métabolisme des lipides.
- métabolisme : Acide éicosatétraénoïque-5,8,10,14 hydroxy-12, Arachidonate 12-lipoxygenase, Arachidonate 15-lipoxygenase, Macrophages, Mitochondries, Phospholipides, Protéines associées aux microtubules, Protéines de Saccharomyces cerevisiae.
- Animaux, Famille de la protéine-8 associée à l'autophagie, Oxydoréduction, Saccharomyces cerevisiae, Souris.
English descriptors
- KwdEn :
- 12-Hydroxy-5,8,10,14-eicosatetraenoic Acid (analogs & derivatives), 12-Hydroxy-5,8,10,14-eicosatetraenoic Acid (metabolism), Animals, Arachidonate 12-Lipoxygenase (genetics), Arachidonate 12-Lipoxygenase (metabolism), Arachidonate 15-Lipoxygenase (genetics), Arachidonate 15-Lipoxygenase (metabolism), Autophagy (genetics), Autophagy-Related Protein 8 Family, Lipid Metabolism (genetics), Macrophages (metabolism), Mice, Microtubule-Associated Proteins (metabolism), Mitochondria (metabolism), Oxidation-Reduction, Phospholipids (metabolism), Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , analogs & derivatives : 12-Hydroxy-5,8,10,14-eicosatetraenoic Acid.
- chemical , genetics : Arachidonate 12-Lipoxygenase, Arachidonate 15-Lipoxygenase.
- chemical , metabolism : 12-Hydroxy-5,8,10,14-eicosatetraenoic Acid, Arachidonate 12-Lipoxygenase, Arachidonate 15-Lipoxygenase, Microtubule-Associated Proteins, Phospholipids, Saccharomyces cerevisiae Proteins.
- genetics : Autophagy, Lipid Metabolism.
- metabolism : Macrophages, Mitochondria.
- Animals, Autophagy-Related Protein 8 Family, Mice, Oxidation-Reduction, Saccharomyces cerevisiae.
Abstract
12/15-Lipoxygenase (LOX) enzymatically generates oxidized phospholipids in monocytes and macrophages. Herein, we show that cells deficient in 12/15-LOX contain defective mitochondria and numerous cytoplasmic vacuoles containing electron dense material, indicating defects in autophagy or membrane processing, However, both LC3 expression and lipidation were normal both basally and on chloroquine treatment. A LOX-derived oxidized phospholipid, 12-hydroxyeicosatetraenoic acid-phosphatidylethanolamine (12-HETE-PE) was found to be a preferred substrate for yeast Atg8 lipidation, versus native PE, while both native and oxidized PE were effective substrates for LC3 lipidation. Last, phospholipidomics demonstrated altered levels of several phospholipid classes. Thus, we show that oxidized phospholipids generated by 12/15-LOX can act as substrates for key proteins required for effective autophagy and that cells deficient in this enzyme show evidence of autophagic dysfunction. The data functionally link phospholipid oxidation with autophagy for the first time.
Url:
DOI: 10.1016/j.redox.2014.11.005
PubMed: 25498966
PubMed Central: 4309860
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PMC:4309860Le document en format XML
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O Onnell</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Institute of Infection and Immunity, School of Medicine, Cardiff University, Cardiff CF14 4XN, UK</nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute of Infection and Immunity, School of Medicine, Cardiff University, Cardiff CF14 4XN</wicri:regionArea><wicri:noRegion>Cardiff CF14 4XN</wicri:noRegion></affiliation></author></analytic><series><title level="j">Redox Biology</title><idno type="eISSN">2213-2317</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>12-Hydroxy-5,8,10,14-eicosatetraenoic Acid (analogs & derivatives)</term><term>12-Hydroxy-5,8,10,14-eicosatetraenoic Acid (metabolism)</term><term>Animals</term><term>Arachidonate 12-Lipoxygenase (genetics)</term><term>Arachidonate 12-Lipoxygenase (metabolism)</term><term>Arachidonate 15-Lipoxygenase (genetics)</term><term>Arachidonate 15-Lipoxygenase (metabolism)</term><term>Autophagy (genetics)</term><term>Autophagy-Related Protein 8 Family</term><term>Lipid Metabolism (genetics)</term><term>Macrophages (metabolism)</term><term>Mice</term><term>Microtubule-Associated Proteins (metabolism)</term><term>Mitochondria (metabolism)</term><term>Oxidation-Reduction</term><term>Phospholipids (metabolism)</term><term>Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide éicosatétraénoïque-5,8,10,14 hydroxy-12 (analogues et dérivés)</term><term>Acide éicosatétraénoïque-5,8,10,14 hydroxy-12 (métabolisme)</term><term>Animaux</term><term>Arachidonate 12-lipoxygenase (génétique)</term><term>Arachidonate 12-lipoxygenase (métabolisme)</term><term>Arachidonate 15-lipoxygenase (génétique)</term><term>Arachidonate 15-lipoxygenase (métabolisme)</term><term>Autophagie (génétique)</term><term>Famille de la protéine-8 associée à l'autophagie</term><term>Macrophages (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Métabolisme des lipides (génétique)</term><term>Oxydoréduction</term><term>Phospholipides (métabolisme)</term><term>Protéines associées aux microtubules (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae</term><term>Souris</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>12-Hydroxy-5,8,10,14-eicosatetraenoic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arachidonate 12-Lipoxygenase</term><term>Arachidonate 15-Lipoxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>12-Hydroxy-5,8,10,14-eicosatetraenoic Acid</term><term>Arachidonate 12-Lipoxygenase</term><term>Arachidonate 15-Lipoxygenase</term><term>Microtubule-Associated Proteins</term><term>Phospholipids</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acide éicosatétraénoïque-5,8,10,14 hydroxy-12</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Autophagy</term><term>Lipid Metabolism</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arachidonate 12-lipoxygenase</term><term>Arachidonate 15-lipoxygenase</term><term>Autophagie</term><term>Métabolisme des lipides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Macrophages</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide éicosatétraénoïque-5,8,10,14 hydroxy-12</term><term>Arachidonate 12-lipoxygenase</term><term>Arachidonate 15-lipoxygenase</term><term>Macrophages</term><term>Mitochondries</term><term>Phospholipides</term><term>Protéines associées aux microtubules</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Autophagy-Related Protein 8 Family</term><term>Mice</term><term>Oxidation-Reduction</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Famille de la protéine-8 associée à l'autophagie</term><term>Oxydoréduction</term><term>Saccharomyces cerevisiae</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>12/15-Lipoxygenase (LOX) enzymatically generates oxidized phospholipids in monocytes and macrophages. Herein, we show that cells deficient in 12/15-LOX contain defective mitochondria and numerous cytoplasmic vacuoles containing electron dense material, indicating defects in autophagy or membrane processing, However, both LC3 expression and lipidation were normal both basally and on chloroquine treatment. A LOX-derived oxidized phospholipid, 12-hydroxyeicosatetraenoic acid-phosphatidylethanolamine (12-HETE-PE) was found to be a preferred substrate for yeast Atg8 lipidation, versus native PE, while both native and oxidized PE were effective substrates for LC3 lipidation. Last, phospholipidomics demonstrated altered levels of several phospholipid classes. Thus, we show that oxidized phospholipids generated by 12/15-LOX can act as substrates for key proteins required for effective autophagy and that cells deficient in this enzyme show evidence of autophagic dysfunction. The data functionally link phospholipid oxidation with autophagy for the first time.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Maskrey, B H" uniqKey="Maskrey B">B.H. Maskrey</name></author><author><name sortKey="Bermudez Fajardo, A" uniqKey="Bermudez Fajardo A">A. Bermúdez-Fajardo</name></author><author><name sortKey="Morgan, A H" uniqKey="Morgan A">A.H. Morgan</name></author><author><name sortKey="Stewart Jones, E" uniqKey="Stewart Jones E">E. Stewart-Jones</name></author><author><name sortKey="Dioszeghy, V" uniqKey="Dioszeghy V">V. Dioszeghy</name></author><author><name sortKey="Taylor, G W" uniqKey="Taylor G">G.W. Taylor</name></author><author><name sortKey="Baker, P R" uniqKey="Baker P">P.R. Baker</name></author><author><name sortKey="Coles, B" uniqKey="Coles B">B. Coles</name></author><author><name sortKey="Coffey, M J" uniqKey="Coffey M">M.J. Coffey</name></author><author><name sortKey="Kuhn, H" uniqKey="Kuhn H">H. 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Kurihara</name></author><author><name sortKey="Levkovitz, H" uniqKey="Levkovitz H">H. Levkovitz</name></author><author><name sortKey="Sigal, E" uniqKey="Sigal E">E. Sigal</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sanjuan, M A" uniqKey="Sanjuan M">M.A. Sanjuan</name></author><author><name sortKey="Dillon, C P" uniqKey="Dillon C">C.P. Dillon</name></author><author><name sortKey="Tait, S W" uniqKey="Tait S">S.W. Tait</name></author><author><name sortKey="Moshiach, S" uniqKey="Moshiach S">S. Moshiach</name></author><author><name sortKey="Dorsey, F" uniqKey="Dorsey F">F. Dorsey</name></author><author><name sortKey="Connell, S" uniqKey="Connell S">S. Connell</name></author><author><name sortKey="Komatsu, M" uniqKey="Komatsu M">M. Komatsu</name></author><author><name sortKey="Tanaka, K" uniqKey="Tanaka K">K. Tanaka</name></author><author><name sortKey="Cleveland, J L" uniqKey="Cleveland J">J.L. Cleveland</name></author><author><name sortKey="Withoff, S" uniqKey="Withoff S">S. Withoff</name></author><author><name sortKey="Green, D R" uniqKey="Green D">D.R. Green</name></author></analytic></biblStruct></listBibl></div1></back></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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