The therapeutic potential of monoamine oxidase inhibitors
Identifieur interne : 000B94 ( Main/Corpus ); précédent : 000B93; suivant : 000B95The therapeutic potential of monoamine oxidase inhibitors
Auteurs : Moussa B. H. Youdim ; Dale Edmondson ; Keith F. TiptonSource :
- Nature Reviews Neuroscience [ 1471-003X ] ; 2006-04.
Abstract
Monoamine oxidase inhibitors were among the first antidepressants to be discovered and have long been used as such. It now seems that many of these agents might have therapeutic value in several common neurodegenerative conditions, independently of their inhibition of monoamine oxidase activity. However, many claims and some counter-claims have been made about the physiological importance of these enzymes and the potential of their inhibitors. We evaluate these arguments in the light of what we know, and still have to learn, of the structure, function and genetics of the monoamine oxidases and the disparate actions of their inhibitors.
Url:
DOI: 10.1038/nrn1883
Links to Exploration step
ISTEX:D7CC3B3075538DC26D4CEA4B55124E36713D9B3FLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">The therapeutic potential of monoamine oxidase inhibitors</title><author><name sortKey="Youdim, Moussa B H" sort="Youdim, Moussa B H" uniqKey="Youdim M" first="Moussa B. H." last="Youdim">Moussa B. H. Youdim</name><affiliation><mods:affiliation>Technion-Rappaport Family Faculty of Medicine, Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Diseases, P.O. Box 9697, 31096 Haifa, Israel.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Pharmacology, P.O. Box 9697, 31096 Haifa, Israel.</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: youdim@tx.technion.ac.il</mods:affiliation></affiliation></author><author><name sortKey="Edmondson, Dale" sort="Edmondson, Dale" uniqKey="Edmondson D" first="Dale" last="Edmondson">Dale Edmondson</name><affiliation><mods:affiliation>Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, Georgia 30322, USA.</mods:affiliation></affiliation></author><author><name sortKey="Tipton, Keith F" sort="Tipton, Keith F" uniqKey="Tipton K" first="Keith F." last="Tipton">Keith F. Tipton</name><affiliation><mods:affiliation>Trinity College Dublin, Department of Biochemistry, Dublin 2, Ireland.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:D7CC3B3075538DC26D4CEA4B55124E36713D9B3F</idno><date when="2006" year="2006">2006</date><idno type="doi">10.1038/nrn1883</idno><idno type="url">https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000B94</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">The therapeutic potential of monoamine oxidase inhibitors</title><author><name sortKey="Youdim, Moussa B H" sort="Youdim, Moussa B H" uniqKey="Youdim M" first="Moussa B. H." last="Youdim">Moussa B. H. Youdim</name><affiliation><mods:affiliation>Technion-Rappaport Family Faculty of Medicine, Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Diseases, P.O. Box 9697, 31096 Haifa, Israel.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Pharmacology, P.O. Box 9697, 31096 Haifa, Israel.</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: youdim@tx.technion.ac.il</mods:affiliation></affiliation></author><author><name sortKey="Edmondson, Dale" sort="Edmondson, Dale" uniqKey="Edmondson D" first="Dale" last="Edmondson">Dale Edmondson</name><affiliation><mods:affiliation>Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, Georgia 30322, USA.</mods:affiliation></affiliation></author><author><name sortKey="Tipton, Keith F" sort="Tipton, Keith F" uniqKey="Tipton K" first="Keith F." last="Tipton">Keith F. Tipton</name><affiliation><mods:affiliation>Trinity College Dublin, Department of Biochemistry, Dublin 2, Ireland.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Nature Reviews Neuroscience</title><idno type="ISSN">1471-003X</idno><idno type="eISSN">1471-0048</idno><imprint><publisher>Nature Publishing Group</publisher><date type="published" when="2006-04">2006-04</date><biblScope unit="volume">7</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="295">295</biblScope><biblScope unit="page" to="309">309</biblScope></imprint><idno type="ISSN">1471-003X</idno></series><idno type="istex">D7CC3B3075538DC26D4CEA4B55124E36713D9B3F</idno><idno type="DOI">10.1038/nrn1883</idno><idno type="ArticleID">nrn1883</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1471-003X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="eng">Monoamine oxidase inhibitors were among the first antidepressants to be discovered and have long been used as such. It now seems that many of these agents might have therapeutic value in several common neurodegenerative conditions, independently of their inhibition of monoamine oxidase activity. However, many claims and some counter-claims have been made about the physiological importance of these enzymes and the potential of their inhibitors. We evaluate these arguments in the light of what we know, and still have to learn, of the structure, function and genetics of the monoamine oxidases and the disparate actions of their inhibitors.</div></front></TEI><istex><corpusName>nature</corpusName><author><json:item><name>Moussa B. H. Youdim</name><affiliations><json:string>Technion-Rappaport Family Faculty of Medicine, Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Diseases, P.O. Box 9697, 31096 Haifa, Israel.</json:string><json:string>Department of Pharmacology, P.O. Box 9697, 31096 Haifa, Israel.</json:string><json:string>E-mail: youdim@tx.technion.ac.il</json:string></affiliations></json:item><json:item><name>Dale Edmondson</name><affiliations><json:string>Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, Georgia 30322, USA.</json:string></affiliations></json:item><json:item><name>Keith F. Tipton</name><affiliations><json:string>Trinity College Dublin, Department of Biochemistry, Dublin 2, Ireland.</json:string></affiliations></json:item></author><language><json:string>eng</json:string></language><abstract>Monoamine oxidase inhibitors were among the first antidepressants to be discovered and have long been used as such. It now seems that many of these agents might have therapeutic value in several common neurodegenerative conditions, independently of their inhibition of monoamine oxidase activity. However, many claims and some counter-claims have been made about the physiological importance of these enzymes and the potential of their inhibitors. We evaluate these arguments in the light of what we know, and still have to learn, of the structure, function and genetics of the monoamine oxidases and the disparate actions of their inhibitors.</abstract><qualityIndicators><score>6.676</score><pdfVersion>1.4</pdfVersion><pdfPageSize>595.276 x 782.362 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>643</abstractCharCount><pdfWordCount>13127</pdfWordCount><pdfCharCount>91025</pdfCharCount><pdfPageCount>15</pdfPageCount><abstractWordCount>98</abstractWordCount></qualityIndicators><title>The therapeutic potential of monoamine oxidase inhibitors</title><genre><json:string>review-article</json:string></genre><host><volume>7</volume><pages><total>15</total><last>309</last><first>295</first></pages><issn><json:string>1471-003X</json:string></issn><issue>4</issue><genre></genre><language><json:string>unknown</json:string></language><eissn><json:string>1471-0048</json:string></eissn><title>Nature Reviews Neuroscience</title></host><categories><wos><json:string>NEUROSCIENCES</json:string></wos></categories><publicationDate>2006</publicationDate><copyrightDate>2006</copyrightDate><doi><json:string>10.1038/nrn1883</json:string></doi><id>D7CC3B3075538DC26D4CEA4B55124E36713D9B3F</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">The therapeutic potential of monoamine oxidase inhibitors</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Nature Publishing Group</publisher><availability><p>NATURE</p></availability><date>2006</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">The therapeutic potential of monoamine oxidase inhibitors</title><author><persName><forename type="first">Moussa B. H.</forename><surname>Youdim</surname></persName><email>youdim@tx.technion.ac.il</email><note type="biography">Moussa B. H. Youdim is Finkelstein Professor of Life Sceinces, Professor of Pharmacology, Adjunct Professor of Biomedical Engineering, and Director of the Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Disease Research at the Technion-Rappaport Family Faculty of Medicine, Haifa, Israel. His scientific interests include the neuropharmacology and neurochemistry of monoamine oxidases and brain iron metabolism, and their roles in brain function and dysfunction; particularly emphasis in progressive neurodegenerative diseases and depression. He has served on the editorial boards of 37 international journals and is also editor of Parkinsonism and Related Disorders and Advances in Neurodegeneration Research. He has received numerous international and national prizes, and honorary degrees from Semmelweiss Medical School University, Budapest, Hungary, and elsewhere. He was a Fogarty International Scholar in Residence at the Center for Advanced Study for Human Health at the Fogarty Center, National Institutes of Health, USA, 19911999, and received their medal.</note><affiliation>Moussa B. H. Youdim is Finkelstein Professor of Life Sceinces, Professor of Pharmacology, Adjunct Professor of Biomedical Engineering, and Director of the Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Disease Research at the Technion-Rappaport Family Faculty of Medicine, Haifa, Israel. His scientific interests include the neuropharmacology and neurochemistry of monoamine oxidases and brain iron metabolism, and their roles in brain function and dysfunction; particularly emphasis in progressive neurodegenerative diseases and depression. He has served on the editorial boards of 37 international journals and is also editor of Parkinsonism and Related Disorders and Advances in Neurodegeneration Research. He has received numerous international and national prizes, and honorary degrees from Semmelweiss Medical School University, Budapest, Hungary, and elsewhere. He was a Fogarty International Scholar in Residence at the Center for Advanced Study for Human Health at the Fogarty Center, National Institutes of Health, USA, 19911999, and received their medal.</affiliation><affiliation>Technion-Rappaport Family Faculty of Medicine, Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Diseases, P.O. Box 9697, 31096 Haifa, Israel.</affiliation><affiliation>Department of Pharmacology, P.O. Box 9697, 31096 Haifa, Israel.</affiliation></author><author><persName><forename type="first">Dale</forename><surname>Edmondson</surname></persName><note type="biography">Dale E. Edmondson is Professor of Biochemistry and Adjunct Professor of Chemistry at Emory University, Atlanta, Georgia, USA. His research career has focused on the structures and mechanisms of flavo-enzymes and metallo-enzymes, with more than 150 publications in this area. His work on the structures and mechanisms of MAOA and MAOB have been ongoing since 1982. He received his Ph.D. in Chemistry in 1970 at the University of Arizona, Tucson, USA, and carried out postdoctoral research at the University of Michigan, USA, and at the University of California, San Francisco, USA. He joined the Emory faculty as an Associate Professor in 1980, and was promoted to Professor in 1986.</note><affiliation>Dale E. Edmondson is Professor of Biochemistry and Adjunct Professor of Chemistry at Emory University, Atlanta, Georgia, USA. His research career has focused on the structures and mechanisms of flavo-enzymes and metallo-enzymes, with more than 150 publications in this area. His work on the structures and mechanisms of MAOA and MAOB have been ongoing since 1982. He received his Ph.D. in Chemistry in 1970 at the University of Arizona, Tucson, USA, and carried out postdoctoral research at the University of Michigan, USA, and at the University of California, San Francisco, USA. He joined the Emory faculty as an Associate Professor in 1980, and was promoted to Professor in 1986.</affiliation><affiliation>Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, Georgia 30322, USA.</affiliation></author><author><persName><forename type="first">Keith F.</forename><surname>Tipton</surname></persName><note type="biography">Keith F. Tipton is Professor of Biochemistry at Trinity College Dublin (TCD), Ireland. He received his Ph.D. in biochemistry in 1966 at Cambridge University, UK, and was a Lecturer and Fellow of Kings College there until accepting the Chair at TCD in 1997. He was elected Fellow of TCD in 1979 and Member of the Royal Irish Academy (MRIA) in 1989. His research interests include enzymology and neurochemistry. He has published a lot in these areas and believes that enzyme kinetics are fun. He has been an editor of several journals, including the The Biochemical Journal, Biochimica et Biophysica Acta and Journal of Neurochemistry, and is co-author and editor of several books.</note><affiliation>Keith F. Tipton is Professor of Biochemistry at Trinity College Dublin (TCD), Ireland. He received his Ph.D. in biochemistry in 1966 at Cambridge University, UK, and was a Lecturer and Fellow of Kings College there until accepting the Chair at TCD in 1997. He was elected Fellow of TCD in 1979 and Member of the Royal Irish Academy (MRIA) in 1989. His research interests include enzymology and neurochemistry. He has published a lot in these areas and believes that enzyme kinetics are fun. He has been an editor of several journals, including the The Biochemical Journal, Biochimica et Biophysica Acta and Journal of Neurochemistry, and is co-author and editor of several books.</affiliation><affiliation>Trinity College Dublin, Department of Biochemistry, Dublin 2, Ireland.</affiliation></author></analytic><monogr><title level="j">Nature Reviews Neuroscience</title><idno type="pISSN">1471-003X</idno><idno type="eISSN">1471-0048</idno><imprint><publisher>Nature Publishing Group</publisher><date type="published" when="2006-04"></date><biblScope unit="volume">7</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="295">295</biblScope><biblScope unit="page" to="309">309</biblScope></imprint></monogr><idno type="istex">D7CC3B3075538DC26D4CEA4B55124E36713D9B3F</idno><idno type="DOI">10.1038/nrn1883</idno><idno type="ArticleID">nrn1883</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2006</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Monoamine oxidase inhibitors were among the first antidepressants to be discovered and have long been used as such. It now seems that many of these agents might have therapeutic value in several common neurodegenerative conditions, independently of their inhibition of monoamine oxidase activity. However, many claims and some counter-claims have been made about the physiological importance of these enzymes and the potential of their inhibitors. We evaluate these arguments in the light of what we know, and still have to learn, of the structure, function and genetics of the monoamine oxidases and the disparate actions of their inhibitors.</p></abstract></profileDesc><revisionDesc><change when="2006-04">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus nature" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0"</istex:xmlDeclaration><istex:docType PUBLIC="-//NPG//DTD XML Article//EN" URI="NPG_XML_Article.dtd" name="istex:docType"><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f1//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f1" NDATA="ITEM" name="figf1"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f2//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f2" NDATA="ITEM" name="figf2"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f3//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f3" NDATA="ITEM" name="figf3"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f4//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f4" NDATA="ITEM" name="figf4"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f5//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f5" NDATA="ITEM" name="figf5"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f6//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f6" NDATA="ITEM" name="figf6"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-f7//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-f7" NDATA="ITEM" name="figf7"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-t1//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-t1" NDATA="ITEM" name="tbl1"></istex:entity><istex:entity PUBLIC="-//NatureAmerica//FICI nrn1883-t2//EN" URL="//snapple/web_d/web/npg/nrn/journal/vaop/ncurrent/images/nrn1883-t2" NDATA="ITEM" name="tbl2"></istex:entity></istex:docType><istex:document><article id="nrn1883" language="eng" publish="issue" relation="no" origsrc="yes"><!--nrn1883--><pubfm><jtl>Nature Reviews Neuroscience</jtl><vol>7</vol><iss>4</iss><idt>200604</idt><categ id="rv"></categ><pp><spn>295</spn><epn>309</epn><cnt>15</cnt></pp><issn type="print">1471-003X</issn><issn type="electronic">1471-0048</issn><cpg><cpy>2006</cpy><cpn>Nature Publishing Group</cpn></cpg><doi>10.1038/nrn1883</doi></pubfm><fm><atl>The therapeutic potential of monoamine oxidase inhibitors</atl><aug><cau><fnm>Moussa B. H.</fnm><snm>Youdim</snm><inits>M B H</inits><orf rid="a1"></orf><orf rid="a2"></orf><corf rid="c1"></corf><bio><p>Moussa B. H. Youdim is Finkelstein Professor of Life Sceinces, Professor of Pharmacology, Adjunct Professor of Biomedical Engineering, and Director of the Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Disease Research at the Technion-Rappaport Family Faculty of Medicine, Haifa, Israel. His scientific interests include the neuropharmacology and neurochemistry of monoamine oxidases and brain iron metabolism, and their roles in brain function and dysfunction; particularly emphasis in progressive neurodegenerative diseases and depression. He has served on the editorial boards of 37 international journals and is also editor of <i>Parkinsonism and Related Disorders</i> and <i>Advances in Neurodegeneration Research</i>. He has received numerous international and national prizes, and honorary degrees from Semmelweiss Medical School University, Budapest, Hungary, and elsewhere. He was a Fogarty International Scholar in Residence at the Center for Advanced Study for Human Health at the Fogarty Center, National Institutes of Health, USA, 1991–1999, and received their medal.</p></bio></cau><au><fnm>Dale</fnm><snm>Edmondson</snm><inits>D</inits><orf rid="a3"></orf><bio><p>Dale E. Edmondson is Professor of Biochemistry and Adjunct Professor of Chemistry at Emory University, Atlanta, Georgia, USA. His research career has focused on the structures and mechanisms of flavo-enzymes and metallo-enzymes, with more than 150 publications in this area. His work on the structures and mechanisms of MAOA and MAOB have been ongoing since 1982. He received his Ph.D. in Chemistry in 1970 at the University of Arizona, Tucson, USA, and carried out postdoctoral research at the University of Michigan, USA, and at the University of California, San Francisco, USA. He joined the Emory faculty as an Associate Professor in 1980, and was promoted to Professor in 1986.</p></bio></au><au><fnm>Keith F.</fnm><snm>Tipton</snm><inits>K F</inits><orf rid="a4"></orf><bio><p>Keith F. Tipton is Professor of Biochemistry at Trinity College Dublin (TCD), Ireland. He received his Ph.D. in biochemistry in 1966 at Cambridge University, UK, and was a Lecturer and Fellow of Kings College there until accepting the Chair at TCD in 1997. He was elected Fellow of TCD in 1979 and Member of the Royal Irish Academy (MRIA) in 1989. His research interests include enzymology and neurochemistry. He has published a lot in these areas and believes that enzyme kinetics are fun. He has been an editor of several journals, including the <i>The Biochemical Journal</i>, <i>Biochimica et Biophysica Acta</i> and <i>Journal of Neurochemistry</i>, and is co-author and editor of several books.</p></bio></au><aff><oid id="a1"></oid><org>Technion-Rappaport Family Faculty of Medicine, Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Diseases, P.O. Box 9697</org>, <zip>31096</zip> <cty>Haifa</cty>, <cny>Israel</cny>.</aff><aff><oid id="a2"></oid><org>Department of Pharmacology, P.O. Box 9697</org>, <zip>31096</zip> <cty>Haifa</cty>, <cny>Israel</cny>.</aff><aff><oid id="a3"></oid><org>Emory University School of Medicine, Department of Biochemistry</org>, <street>1510 Clifton Road</street>, <cty>Atlanta</cty>, <st>Georgia</st> <zip>30322</zip>, <cny>USA</cny>.</aff><aff><oid id="a4"></oid><org>Trinity College Dublin, Department of Biochemistry</org>, <cty>Dublin</cty> <zip>2</zip>, <cny>Ireland</cny>.</aff><caff><coid id="c1"></coid><email>youdim@tx.technion.ac.il</email></caff></aug><execsumm><p><list id="l1" type="bullet"><li>Monoamine oxidase (MAO) inhibitors were among the first antidepressants to be discovered and introduced into the clinic. Early forms have almost disappeared from use as a consequence of their side effects, which include the 'cheese reaction' — that is, stimulation of cardiovascular sympathetic nervous system activity due to a build-up of dietary amines.</li><li>The identification of two forms of MAO, known as MAOA and MAOB, and their respective selective inhibitors has contributed to a better understanding of their physiological roles, regulation of neurotransmitter metabolism and the mechanism of the 'cheese reaction', and has led to the development of selective inhibitors that avoid this side effect.</li><li>The two enzymes differ structurally in their substrate–inhibitor recognition sites, but not in their active sites, which contain a covalently bound flavin moiety. Knowledge of the three-dimensional structures of MAOA and MAOB has provided new insights into the way in which MAO interacts with substrates and inhibitors, and has revealed intriguing species differences for MAOA.</li><li>The discovery that the synthetic compound MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) is a substrate of MAOB, which converts this compound to the neurotoxin MPP<super>+</super> (1-methyl-4-phenylpyridinium), causing a parkinsonism syndrome in some mouse strains and primates including humans, provided a basis for our understanding of the participation of MAO in dopaminergic neurodegeneration, and MAOB inhibitors as neuroprotective drugs with disease-modifying activity.</li><li>The propargylamine irreversible MAOB inhibitors, including <i>l</i>-deprenyl (Selegiline) and rasagiline, have shown efficacy in the treatment of Parkinson's disease. These drugs exert a neuroprotective activity not related to MAO inhibition, as shown in cultured neurons and <i>in vivo</i> models of neurodegeneration. The molecular mechanism of this neuroprotective activity involves regulation of B-cell lymphoma/leukaemia 2 (BCL2) family proteins and protein kinase-dependent signalling pathways as well as interactions with glyceraldehyde-3-phosphate dehydrogenase and induction of some antioxidant enzymes.</li><li>Although considerable advances have been made in our understanding of the structure of MAO, its neurobiology and the mechanisms of action of its selective inhibitors in neuropsychiatric disorders, much remains to be learnt about MAO and its interactions with both substrates and inhibitors.</li></list></p></execsumm><websumm>Youdim and colleagues describe how the recent solving of the crystal structures of monoamine oxidase enzymes has increased our understanding of the action of their inhibitors, some of which are now showing therapeutic value in the treatment of neurodegenerative conditions.</websumm><abs><p>Monoamine oxidase inhibitors were among the first antidepressants to be discovered and have long been used as such. It now seems that many of these agents might have therapeutic value in several common neurodegenerative conditions, independently of their inhibition of monoamine oxidase activity. However, many claims and some counter-claims have been made about the physiological importance of these enzymes and the potential of their inhibitors. We evaluate these arguments in the light of what we know, and still have to learn, of the structure, function and genetics of the monoamine oxidases and the disparate actions of their inhibitors.</p></abs></fm></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="eng"><title>The therapeutic potential of monoamine oxidase inhibitors</title></titleInfo><titleInfo type="alternative" lang="eng" contentType="CDATA"><title>The therapeutic potential of monoamine oxidase inhibitors</title></titleInfo><name type="personal"><namePart type="given">Moussa B. H.</namePart><namePart type="family">Youdim</namePart><affiliation>Technion-Rappaport Family Faculty of Medicine, Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Diseases, P.O. Box 9697, 31096 Haifa, Israel.</affiliation><affiliation>Department of Pharmacology, P.O. Box 9697, 31096 Haifa, Israel.</affiliation><affiliation>E-mail: youdim@tx.technion.ac.il</affiliation><role><roleTerm type="text">author</roleTerm></role><description>Moussa B. H. Youdim is Finkelstein Professor of Life Sceinces, Professor of Pharmacology, Adjunct Professor of Biomedical Engineering, and Director of the Eve Topf and US National Parkinson Foundation Centers of Excellence for Neurodegenerative Disease Research at the Technion-Rappaport Family Faculty of Medicine, Haifa, Israel. His scientific interests include the neuropharmacology and neurochemistry of monoamine oxidases and brain iron metabolism, and their roles in brain function and dysfunction; particularly emphasis in progressive neurodegenerative diseases and depression. He has served on the editorial boards of 37 international journals and is also editor of Parkinsonism and Related Disorders and Advances in Neurodegeneration Research. He has received numerous international and national prizes, and honorary degrees from Semmelweiss Medical School University, Budapest, Hungary, and elsewhere. He was a Fogarty International Scholar in Residence at the Center for Advanced Study for Human Health at the Fogarty Center, National Institutes of Health, USA, 19911999, and received their medal.</description></name><name type="personal"><namePart type="given">Dale</namePart><namePart type="family">Edmondson</namePart><affiliation>Emory University School of Medicine, Department of Biochemistry, 1510 Clifton Road, Atlanta, Georgia 30322, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role><description>Dale E. Edmondson is Professor of Biochemistry and Adjunct Professor of Chemistry at Emory University, Atlanta, Georgia, USA. His research career has focused on the structures and mechanisms of flavo-enzymes and metallo-enzymes, with more than 150 publications in this area. His work on the structures and mechanisms of MAOA and MAOB have been ongoing since 1982. He received his Ph.D. in Chemistry in 1970 at the University of Arizona, Tucson, USA, and carried out postdoctoral research at the University of Michigan, USA, and at the University of California, San Francisco, USA. He joined the Emory faculty as an Associate Professor in 1980, and was promoted to Professor in 1986.</description></name><name type="personal"><namePart type="given">Keith F.</namePart><namePart type="family">Tipton</namePart><affiliation>Trinity College Dublin, Department of Biochemistry, Dublin 2, Ireland.</affiliation><role><roleTerm type="text">author</roleTerm></role><description>Keith F. Tipton is Professor of Biochemistry at Trinity College Dublin (TCD), Ireland. He received his Ph.D. in biochemistry in 1966 at Cambridge University, UK, and was a Lecturer and Fellow of Kings College there until accepting the Chair at TCD in 1997. He was elected Fellow of TCD in 1979 and Member of the Royal Irish Academy (MRIA) in 1989. His research interests include enzymology and neurochemistry. He has published a lot in these areas and believes that enzyme kinetics are fun. He has been an editor of several journals, including the The Biochemical Journal, Biochimica et Biophysica Acta and Journal of Neurochemistry, and is co-author and editor of several books.</description></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="Review"></genre><originInfo><publisher>Nature Publishing Group</publisher><dateIssued encoding="w3cdtf">2006-04</dateIssued><copyrightDate encoding="w3cdtf">2006</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="eng">Monoamine oxidase inhibitors were among the first antidepressants to be discovered and have long been used as such. It now seems that many of these agents might have therapeutic value in several common neurodegenerative conditions, independently of their inhibition of monoamine oxidase activity. However, many claims and some counter-claims have been made about the physiological importance of these enzymes and the potential of their inhibitors. We evaluate these arguments in the light of what we know, and still have to learn, of the structure, function and genetics of the monoamine oxidases and the disparate actions of their inhibitors.</abstract><relatedItem type="host"><titleInfo><title>Nature Reviews Neuroscience</title></titleInfo><identifier type="ISSN">1471-003X</identifier><identifier type="eISSN">1471-0048</identifier><part><date>2006</date><detail type="volume"><caption>vol.</caption><number>7</number></detail><detail type="issue"><caption>no.</caption><number>4</number></detail><extent unit="pages"><start>295</start><end>309</end><total>15</total></extent></part></relatedItem><identifier type="istex">D7CC3B3075538DC26D4CEA4B55124E36713D9B3F</identifier><identifier type="DOI">10.1038/nrn1883</identifier><identifier type="ArticleID">nrn1883</identifier><accessCondition type="use and reproduction" contentType="copyright">©2006 Nature Publishing Group</accessCondition><recordInfo><recordContentSource>NATURE</recordContentSource></recordInfo></mods></metadata><annexes><json:item><original>true</original><mimetype>image/jpeg</mimetype><extension>jpeg</extension><uri>https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/annexes/jpeg</uri></json:item></annexes><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/D7CC3B3075538DC26D4CEA4B55124E36713D9B3F/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">NEUROSCIENCES</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000B94 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000B94 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= ISTEX:D7CC3B3075538DC26D4CEA4B55124E36713D9B3F
|texte= The therapeutic potential of monoamine oxidase inhibitors
}}
| This area was generated with Dilib version V0.6.23. |  |