Vesicular monoamine transporters: Structure‐function, pharmacology, and medicinal chemistry
Identifieur interne : 001389 ( Istex/Corpus ); précédent : 001388; suivant : 001390Vesicular monoamine transporters: Structure‐function, pharmacology, and medicinal chemistry
Auteurs : Kandatege WimalasenaSource :
- Medicinal Research Reviews [ 0198-6325 ] ; 2011-07.
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Abstract
Vesicular monoamine transporters (VMAT) are responsible for the uptake of cytosolic monoamines into synaptic vesicles in monoaminergic neurons. Two closely related VMATs with distinct pharmacological properties and tissue distributions have been characterized. VMAT1 is preferentially expressed in neuroendocrine cells and VMAT2 is primarily expressed in the CNS. The neurotoxicity and addictive properties of various psychostimulants have been attributed, at least partly, to their interference with VMAT2 functions. The quantitative assessment of the VMAT2 density by PET scanning has been clinically useful for early diagnosis and monitoring of the progression of Parkinson's and Alzheimer's diseases and drug addiction. The classical VMAT2 inhibitor, tetrabenazine, has long been used for the treatment of chorea associated with Huntington's disease in the United Kingdom, Canada, and Australia, and recently approved in the United States. The VMAT2 imaging may also be useful for exploiting the onset of diabetes mellitus, as VMAT2 is also expressed in the β‐cells of the pancreas. VMAT1 gene SLC18A1 is a locus with strong evidence of linkage with schizophrenia and, thus, the polymorphic forms of the VMAT1 gene may confer susceptibility to schizophrenia. This review summarizes the current understanding of the structure–function relationships of VMAT2, and the role of VMAT2 on addiction and psychostimulant‐induced neurotoxicity, and the therapeutic and diagnostic applications of specific VMAT2 ligands. The evidence for the linkage of VMAT1 gene with schizophrenia and bipolar disorder I is also discussed. © 2010 Wiley Periodicals, Inc. Med Res Rev 31: 483‐519, 2011
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DOI: 10.1002/med.20187
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Two closely related VMATs with distinct pharmacological properties and tissue distributions have been characterized. VMAT1 is preferentially expressed in neuroendocrine cells and VMAT2 is primarily expressed in the CNS. The neurotoxicity and addictive properties of various psychostimulants have been attributed, at least partly, to their interference with VMAT2 functions. The quantitative assessment of the VMAT2 density by PET scanning has been clinically useful for early diagnosis and monitoring of the progression of Parkinson's and Alzheimer's diseases and drug addiction. The classical VMAT2 inhibitor, tetrabenazine, has long been used for the treatment of chorea associated with Huntington's disease in the United Kingdom, Canada, and Australia, and recently approved in the United States. The VMAT2 imaging may also be useful for exploiting the onset of diabetes mellitus, as VMAT2 is also expressed in the β‐cells of the pancreas. 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VMAT1 gene SLC18A1 is a locus with strong evidence of linkage with schizophrenia and, thus, the polymorphic forms of the VMAT1 gene may confer susceptibility to schizophrenia. This review summarizes the current understanding of the structure–function relationships of VMAT2, and the role of VMAT2 on addiction and psychostimulant‐induced neurotoxicity, and the therapeutic and diagnostic applications of specific VMAT2 ligands. The evidence for the linkage of VMAT1 gene with schizophrenia and bipolar disorder I is also discussed. © 2010 Wiley Periodicals, Inc. 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Two closely related VMATs with distinct pharmacological properties and tissue distributions have been characterized. VMAT1 is preferentially expressed in neuroendocrine cells and VMAT2 is primarily expressed in the CNS. The neurotoxicity and addictive properties of various psychostimulants have been attributed, at least partly, to their interference with VMAT2 functions. The quantitative assessment of the VMAT2 density by PET scanning has been clinically useful for early diagnosis and monitoring of the progression of Parkinson's and Alzheimer's diseases and drug addiction. The classical VMAT2 inhibitor, tetrabenazine, has long been used for the treatment of chorea associated with Huntington's disease in the United Kingdom, Canada, and Australia, and recently approved in the United States. The VMAT2 imaging may also be useful for exploiting the onset of diabetes mellitus, as VMAT2 is also expressed in the β‐cells of the pancreas. VMAT1 gene SLC18A1 is a locus with strong evidence of linkage with schizophrenia and, thus, the polymorphic forms of the VMAT1 gene may confer susceptibility to schizophrenia. This review summarizes the current understanding of the structure–function relationships of VMAT2, and the role of VMAT2 on addiction and psychostimulant‐induced neurotoxicity, and the therapeutic and diagnostic applications of specific VMAT2 ligands. The evidence for the linkage of VMAT1 gene with schizophrenia and bipolar disorder I is also discussed. © 2010 Wiley Periodicals, Inc. 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Rev.</title></titleGroup></publicationMeta><publicationMeta level="part" position="40"><doi origin="wiley" registered="yes">10.1002/med.v31.4</doi><numberingGroup><numbering type="journalVolume" number="31">31</numbering><numbering type="journalIssue">4</numbering></numberingGroup><coverDate startDate="2011-07">July 2011</coverDate></publicationMeta><publicationMeta level="unit" type="reviewArticle" position="1" status="forIssue"><doi origin="wiley" registered="yes">10.1002/med.20187</doi><idGroup><id type="unit" value="MED20187"></id></idGroup><countGroup><count type="pageTotal" number="37"></count></countGroup><copyright ownership="publisher">© 2010 Wiley Periodicals, Inc.</copyright><eventGroup><event type="firstOnline" date="2010-02-04"></event><event type="publishedOnlineAcceptedOrEarlyUnpaginated" date="2010-02-04"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.5.2 mode:FullText mathml2tex" date="2011-06-24"></event><event type="publishedOnlineFinalForm" date="2011-06-24"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-02"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-31"></event></eventGroup><numberingGroup><numbering type="pageFirst">483</numbering><numbering type="pageLast">519</numbering></numberingGroup><correspondenceTo>Department of Chemistry, Wichita State University, Wichita, KS 67260</correspondenceTo><objectNameGroup><objectName elementName="figure">Scheme</objectName></objectNameGroup><linkGroup><link type="toTypesetVersion" href="file:MED.MED20187.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="8"></count><count type="referenceTotal" number="168"></count></countGroup><titleGroup><title type="main" xml:lang="en">Vesicular monoamine transporters: Structure‐function, pharmacology, and medicinal chemistry</title><title type="short" xml:lang="en">VESICULAR MONOAMINE TRANSPORTERS</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Kandatege</givenNames><familyName>Wimalasena</familyName></personName><contactDetails><email>kandatege.wimalasena@wichita.edu</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>Department of Chemistry, Wichita State University, Wichita, Kansas 67260</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">vesicular monoamine transporter 1 (VMAT1)</keyword><keyword xml:id="kwd2">vesicular monoamine transporter 2 (VMAT2)</keyword><keyword xml:id="kwd3">psychostimulant abuse</keyword><keyword xml:id="kwd4">catecholamine metabolism</keyword><keyword xml:id="kwd5">synaptic vesicles</keyword><keyword xml:id="kwd6">oxidative stress</keyword><keyword xml:id="kwd7">Parkinson's disease</keyword></keywordGroup><fundingInfo><fundingAgency>National Institutes of Health</fundingAgency><fundingNumber>NS 39423</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Vesicular monoamine transporters (VMAT) are responsible for the uptake of cytosolic monoamines into synaptic vesicles in monoaminergic neurons. Two closely related VMATs with distinct pharmacological properties and tissue distributions have been characterized. VMAT1 is preferentially expressed in neuroendocrine cells and VMAT2 is primarily expressed in the CNS. The neurotoxicity and addictive properties of various psychostimulants have been attributed, at least partly, to their interference with VMAT2 functions. The quantitative assessment of the VMAT2 density by PET scanning has been clinically useful for early diagnosis and monitoring of the progression of Parkinson's and Alzheimer's diseases and drug addiction. The classical VMAT2 inhibitor, tetrabenazine, has long been used for the treatment of chorea associated with Huntington's disease in the United Kingdom, Canada, and Australia, and recently approved in the United States. The VMAT2 imaging may also be useful for exploiting the onset of diabetes mellitus, as VMAT2 is also expressed in the β‐cells of the pancreas. VMAT1 gene SLC18A1 is a locus with strong evidence of linkage with schizophrenia and, thus, the polymorphic forms of the VMAT1 gene may confer susceptibility to schizophrenia. This review summarizes the current understanding of the structure–function relationships of VMAT2, and the role of VMAT2 on addiction and psychostimulant‐induced neurotoxicity, and the therapeutic and diagnostic applications of specific VMAT2 ligands. The evidence for the linkage of VMAT1 gene with schizophrenia and bipolar disorder I is also discussed. © 2010 Wiley Periodicals, Inc. Med Res Rev 31: 483‐519, 2011</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Vesicular monoamine transporters: Structure‐function, pharmacology, and medicinal chemistry</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>VESICULAR MONOAMINE TRANSPORTERS</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Vesicular monoamine transporters: Structure‐function, pharmacology, and medicinal chemistry</title></titleInfo><name type="personal"><namePart type="given">Kandatege</namePart><namePart type="family">Wimalasena</namePart><affiliation>Department of Chemistry, Wichita State University, Wichita, Kansas 67260</affiliation><affiliation>Department of Chemistry, Wichita State University, Wichita, KS 67260</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2011-07</dateIssued><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">5</extent><extent unit="tables">8</extent><extent unit="references">168</extent></physicalDescription><abstract lang="en">Vesicular monoamine transporters (VMAT) are responsible for the uptake of cytosolic monoamines into synaptic vesicles in monoaminergic neurons. Two closely related VMATs with distinct pharmacological properties and tissue distributions have been characterized. VMAT1 is preferentially expressed in neuroendocrine cells and VMAT2 is primarily expressed in the CNS. The neurotoxicity and addictive properties of various psychostimulants have been attributed, at least partly, to their interference with VMAT2 functions. The quantitative assessment of the VMAT2 density by PET scanning has been clinically useful for early diagnosis and monitoring of the progression of Parkinson's and Alzheimer's diseases and drug addiction. The classical VMAT2 inhibitor, tetrabenazine, has long been used for the treatment of chorea associated with Huntington's disease in the United Kingdom, Canada, and Australia, and recently approved in the United States. The VMAT2 imaging may also be useful for exploiting the onset of diabetes mellitus, as VMAT2 is also expressed in the β‐cells of the pancreas. VMAT1 gene SLC18A1 is a locus with strong evidence of linkage with schizophrenia and, thus, the polymorphic forms of the VMAT1 gene may confer susceptibility to schizophrenia. This review summarizes the current understanding of the structure–function relationships of VMAT2, and the role of VMAT2 on addiction and psychostimulant‐induced neurotoxicity, and the therapeutic and diagnostic applications of specific VMAT2 ligands. The evidence for the linkage of VMAT1 gene with schizophrenia and bipolar disorder I is also discussed. © 2010 Wiley Periodicals, Inc. Med Res Rev 31: 483‐519, 2011</abstract><note type="funding">National Institutes of Health - No. NS 39423; </note><subject lang="en"><genre>keywords</genre><topic>vesicular monoamine transporter 1 (VMAT1)</topic><topic>vesicular monoamine transporter 2 (VMAT2)</topic><topic>psychostimulant abuse</topic><topic>catecholamine metabolism</topic><topic>synaptic vesicles</topic><topic>oxidative stress</topic><topic>Parkinson's disease</topic></subject><relatedItem type="host"><titleInfo><title>Medicinal Research Reviews</title></titleInfo><titleInfo type="abbreviated"><title>Med. Res. Rev.</title></titleInfo><genre type="journal">journal</genre><identifier type="ISSN">0198-6325</identifier><identifier type="eISSN">1098-1128</identifier><identifier type="DOI">10.1002/(ISSN)1098-1128</identifier><identifier type="PublisherID">MED</identifier><part><date>2011</date><detail type="volume"><caption>vol.</caption><number>31</number></detail><detail type="issue"><caption>no.</caption><number>4</number></detail><extent unit="pages"><start>483</start><end>519</end><total>37</total></extent></part></relatedItem><identifier type="istex">A174C413E6726EA8D185183D9624D28B4359702A</identifier><identifier type="DOI">10.1002/med.20187</identifier><identifier type="ArticleID">MED20187</identifier><accessCondition type="use and reproduction" contentType="copyright">© 2010 Wiley Periodicals, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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