Caspase‐3 activation in 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP)‐treated mice
Identifieur interne : 002D20 ( Istex/Corpus ); précédent : 002D19; suivant : 002D21Caspase‐3 activation in 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP)‐treated mice
Auteurs : Hélène Turmel ; Andreas Hartmann ; Karine Parain ; Aicha Douhou ; Anu Srinivasan ; Yves Agid ; Etienne C. HirschSource :
- Movement Disorders [ 0885-3185 ] ; 2001-03.
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Abstract
In 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) models of Parkinson's disease (PD), dopaminergic (DA) neurons have been shown to die by apoptosis. Moreover, recent postmortem and in vitro results have indicated that apoptotic cell death induced by 1‐methyl‐4‐phenylpyridinium (MPP+) may be mediated by caspase‐3. To establish whether caspase‐3 activation may indeed play a role in an in vivo model of PD, we studied caspase‐3 activation in C57Bl/6 mice subchronically intoxicated with MPTP. We show that caspase‐3 activation peaks early, at days 1 and 2 after the end of MPTP intoxication. In contrast, pycnotic neurons persist until day 7 postintoxication, indicating that caspase‐3 activation is an early and transient phenomenon in apoptotic death of DA neurons. We further demonstrate that loss of tyrosine hydroxylase (TH) immunoreactivity in this model is indeed due to cell loss rather than to loss of TH protein expression. We conclude that mice subchronically intoxicated with MPTP represent a valid PD model to study and manipulate caspase activation in vivo. © 2001 Movement Disorder Society.
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DOI: 10.1002/mds.1037
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ISTEX:919388BA1F3FE05BB4D9DE7516DA1DB6A839064BLe document en format XML
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Hirsch</name><affiliation><mods:affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Movement Disorders</title><title level="j" type="sub">Official Journal of the Movement Disorder Society</title><title level="j" type="abbrev">Mov. Disord.</title><idno type="ISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-03">2001-03</date><biblScope unit="vol">16</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="185">185</biblScope><biblScope unit="page" to="189">189</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">919388BA1F3FE05BB4D9DE7516DA1DB6A839064B</idno><idno type="DOI">10.1002/mds.1037</idno><idno type="ArticleID">MDS1037</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>MPP+</term><term>MPTP</term><term>Parkinson's disease</term><term>apoptosis</term><term>caspase‐3</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) models of Parkinson's disease (PD), dopaminergic (DA) neurons have been shown to die by apoptosis. Moreover, recent postmortem and in vitro results have indicated that apoptotic cell death induced by 1‐methyl‐4‐phenylpyridinium (MPP+) may be mediated by caspase‐3. To establish whether caspase‐3 activation may indeed play a role in an in vivo model of PD, we studied caspase‐3 activation in C57Bl/6 mice subchronically intoxicated with MPTP. We show that caspase‐3 activation peaks early, at days 1 and 2 after the end of MPTP intoxication. In contrast, pycnotic neurons persist until day 7 postintoxication, indicating that caspase‐3 activation is an early and transient phenomenon in apoptotic death of DA neurons. We further demonstrate that loss of tyrosine hydroxylase (TH) immunoreactivity in this model is indeed due to cell loss rather than to loss of TH protein expression. We conclude that mice subchronically intoxicated with MPTP represent a valid PD model to study and manipulate caspase activation in vivo. © 2001 Movement Disorder Society.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Hélène Turmel MD</name><affiliations><json:string>INSERM U 289, Hópital de la Salpétrière, Paris, France</json:string></affiliations></json:item><json:item><name>Andreas Hartmann MD</name><affiliations><json:string>INSERM U 289, Hópital de la Salpétrière, Paris, France</json:string></affiliations></json:item><json:item><name>Karine Parain BsC</name><affiliations><json:string>INSERM U 289, Hópital de la Salpétrière, Paris, France</json:string></affiliations></json:item><json:item><name>Aicha Douhou BsC</name><affiliations><json:string>INSERM U 289, Hópital de la Salpétrière, Paris, France</json:string></affiliations></json:item><json:item><name>Anu Srinivasan PhD</name><affiliations><json:string>IDUN Pharmaceuticals Inc., La Jolla, California, USA</json:string></affiliations></json:item><json:item><name>Yves Agid MD, PhD</name><affiliations><json:string>INSERM U 289, Hópital de la Salpétrière, Paris, France</json:string></affiliations></json:item><json:item><name>Etienne C. 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To establish whether caspase‐3 activation may indeed play a role in an in vivo model of PD, we studied caspase‐3 activation in C57Bl/6 mice subchronically intoxicated with MPTP. We show that caspase‐3 activation peaks early, at days 1 and 2 after the end of MPTP intoxication. In contrast, pycnotic neurons persist until day 7 postintoxication, indicating that caspase‐3 activation is an early and transient phenomenon in apoptotic death of DA neurons. We further demonstrate that loss of tyrosine hydroxylase (TH) immunoreactivity in this model is indeed due to cell loss rather than to loss of TH protein expression. 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Disord.</title><idno type="pISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><idno type="DOI">10.1002/(ISSN)1531-8257</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-03"></date><biblScope unit="vol">16</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="185">185</biblScope><biblScope unit="page" to="189">189</biblScope></imprint></monogr><idno type="istex">919388BA1F3FE05BB4D9DE7516DA1DB6A839064B</idno><idno type="DOI">10.1002/mds.1037</idno><idno type="ArticleID">MDS1037</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2001</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>In 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) models of Parkinson's disease (PD), dopaminergic (DA) neurons have been shown to die by apoptosis. Moreover, recent postmortem and in vitro results have indicated that apoptotic cell death induced by 1‐methyl‐4‐phenylpyridinium (MPP+) may be mediated by caspase‐3. To establish whether caspase‐3 activation may indeed play a role in an in vivo model of PD, we studied caspase‐3 activation in C57Bl/6 mice subchronically intoxicated with MPTP. We show that caspase‐3 activation peaks early, at days 1 and 2 after the end of MPTP intoxication. In contrast, pycnotic neurons persist until day 7 postintoxication, indicating that caspase‐3 activation is an early and transient phenomenon in apoptotic death of DA neurons. We further demonstrate that loss of tyrosine hydroxylase (TH) immunoreactivity in this model is indeed due to cell loss rather than to loss of TH protein expression. 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Disord.</title></titleGroup></publicationMeta><publicationMeta level="part" position="20"><doi origin="wiley" registered="yes">10.1002/mds.v16:2</doi><numberingGroup><numbering type="journalVolume" number="16">16</numbering><numbering type="journalIssue">2</numbering></numberingGroup><coverDate startDate="2001-03">March 2001</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="2" status="forIssue"><doi origin="wiley" registered="yes">10.1002/mds.1037</doi><idGroup><id type="unit" value="MDS1037"></id></idGroup><countGroup><count type="pageTotal" number="5"></count></countGroup><titleGroup><title type="articleCategory">Article</title><title type="tocHeading1">Articles</title></titleGroup><copyright ownership="thirdParty">Copyright © 2001 Movement Disorder Society</copyright><eventGroup><event type="manuscriptReceived" date="2000-06-24"></event><event type="manuscriptRevised" date="2000-08-04"></event><event type="manuscriptAccepted" date="2000-08-15"></event><event type="publishedOnlineEarlyUnpaginated" date="2001-03-01"></event><event type="firstOnline" date="2001-03-07"></event><event type="publishedOnlineFinalForm" date="2001-03-28"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText" date="2010-03-09"></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">185</numbering><numbering type="pageLast">189</numbering></numberingGroup><correspondenceTo>INSERM U 289, Hópital de la Salpétrière, 47 Boulevard de l'Hópital, 75013 Paris, France.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:MDS.MDS1037.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="4"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="17"></count><count type="wordTotal" number="2338"></count></countGroup><titleGroup><title type="main" xml:lang="en">Caspase‐3 activation in 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP)‐treated mice</title><title type="short" xml:lang="en">Caspase‐3 and MPTP</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" noteRef="#fn1"><personName><givenNames>Hélène</givenNames><familyName>Turmel</familyName><degrees>MD</degrees></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1" noteRef="#fn2"><personName><givenNames>Andreas</givenNames><familyName>Hartmann</familyName><degrees>MD</degrees></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Karine</givenNames><familyName>Parain</familyName><degrees>BsC</degrees></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Aicha</givenNames><familyName>Douhou</familyName><degrees>BsC</degrees></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Anu</givenNames><familyName>Srinivasan</familyName><degrees>PhD</degrees></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Yves</givenNames><familyName>Agid</familyName><degrees>MD, PhD</degrees></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Etienne C.</givenNames><familyName>Hirsch</familyName><degrees>PhD</degrees></personName><contactDetails><email>hirsch@ccr.jussieu.fr</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="FR" type="organization"><unparsedAffiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="US" type="organization"><unparsedAffiliation>IDUN Pharmaceuticals Inc., La Jolla, California, USA</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">Parkinson's disease</keyword><keyword xml:id="kwd2">MPTP</keyword><keyword xml:id="kwd3">MPP<sup>+</sup></keyword><keyword xml:id="kwd4">apoptosis</keyword><keyword xml:id="kwd5">caspase‐3</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>In 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) models of Parkinson's disease (PD), dopaminergic (DA) neurons have been shown to die by apoptosis. Moreover, recent postmortem and in vitro results have indicated that apoptotic cell death induced by 1‐methyl‐4‐phenylpyridinium (MPP<sup>+</sup>) may be mediated by caspase‐3. To establish whether caspase‐3 activation may indeed play a role in an in vivo model of PD, we studied caspase‐3 activation in C57Bl/6 mice subchronically intoxicated with MPTP. We show that caspase‐3 activation peaks early, at days 1 and 2 after the end of MPTP intoxication. In contrast, pycnotic neurons persist until day 7 postintoxication, indicating that caspase‐3 activation is an early and transient phenomenon in apoptotic death of DA neurons. We further demonstrate that loss of tyrosine hydroxylase (TH) immunoreactivity in this model is indeed due to cell loss rather than to loss of TH protein expression. We conclude that mice subchronically intoxicated with MPTP represent a valid PD model to study and manipulate caspase activation in vivo. © 2001 Movement Disorder Society.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>Hélène Turmel and Andreas Hartmann contributed equally to this work.</p></note><note xml:id="fn2"><p>Hélène Turmel and Andreas Hartmann contributed equally to this work.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><!--Version 0.6 générée le 3-12-2015--><mods version="3.6"><titleInfo lang="en"><title>Caspase‐3 activation in 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP)‐treated mice</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Caspase‐3 and MPTP</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Caspase‐3 activation in 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP)‐treated mice</title></titleInfo><name type="personal"><namePart type="given">Hélène</namePart><namePart type="family">Turmel</namePart><namePart type="termsOfAddress">MD</namePart><affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</affiliation><description>Hélène Turmel and Andreas Hartmann contributed equally to this work.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Andreas</namePart><namePart type="family">Hartmann</namePart><namePart type="termsOfAddress">MD</namePart><affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</affiliation><description>Hélène Turmel and Andreas Hartmann contributed equally to this work.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Karine</namePart><namePart type="family">Parain</namePart><namePart type="termsOfAddress">BsC</namePart><affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Aicha</namePart><namePart type="family">Douhou</namePart><namePart type="termsOfAddress">BsC</namePart><affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Anu</namePart><namePart type="family">Srinivasan</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>IDUN Pharmaceuticals Inc., La Jolla, California, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yves</namePart><namePart type="family">Agid</namePart><namePart type="termsOfAddress">MD, PhD</namePart><affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Etienne C.</namePart><namePart type="family">Hirsch</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>INSERM U 289, Hópital de la Salpétrière, Paris, France</affiliation><description>Correspondence: INSERM U 289, Hópital de la Salpétrière, 47 Boulevard de l'Hópital, 75013 Paris, France.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre authority="originalCategForm">article</genre><originInfo><publisher>John Wiley & Sons, Inc.</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2001-03</dateIssued><dateCaptured encoding="w3cdtf">2000-06-24</dateCaptured><dateValid encoding="w3cdtf">2000-08-15</dateValid><copyrightDate encoding="w3cdtf">2001</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">4</extent><extent unit="references">17</extent><extent unit="words">2338</extent></physicalDescription><abstract lang="en">In 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) models of Parkinson's disease (PD), dopaminergic (DA) neurons have been shown to die by apoptosis. Moreover, recent postmortem and in vitro results have indicated that apoptotic cell death induced by 1‐methyl‐4‐phenylpyridinium (MPP+) may be mediated by caspase‐3. To establish whether caspase‐3 activation may indeed play a role in an in vivo model of PD, we studied caspase‐3 activation in C57Bl/6 mice subchronically intoxicated with MPTP. We show that caspase‐3 activation peaks early, at days 1 and 2 after the end of MPTP intoxication. In contrast, pycnotic neurons persist until day 7 postintoxication, indicating that caspase‐3 activation is an early and transient phenomenon in apoptotic death of DA neurons. We further demonstrate that loss of tyrosine hydroxylase (TH) immunoreactivity in this model is indeed due to cell loss rather than to loss of TH protein expression. We conclude that mice subchronically intoxicated with MPTP represent a valid PD model to study and manipulate caspase activation in vivo. © 2001 Movement Disorder Society.</abstract><subject lang="en"><genre>Keywords</genre><topic>Parkinson's disease</topic><topic>MPTP</topic><topic>MPP+</topic><topic>apoptosis</topic><topic>caspase‐3</topic></subject><relatedItem type="host"><titleInfo><title>Movement Disorders</title><subTitle>Official Journal of the Movement Disorder Society</subTitle></titleInfo><titleInfo type="abbreviated"><title>Mov. Disord.</title></titleInfo><subject><genre>article category</genre><topic>Article</topic></subject><identifier type="ISSN">0885-3185</identifier><identifier type="eISSN">1531-8257</identifier><identifier type="DOI">10.1002/(ISSN)1531-8257</identifier><identifier type="PublisherID">MDS</identifier><part><date>2001</date><detail type="volume"><caption>vol.</caption><number>16</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>185</start><end>189</end><total>5</total></extent></part></relatedItem><identifier type="istex">919388BA1F3FE05BB4D9DE7516DA1DB6A839064B</identifier><identifier type="DOI">10.1002/mds.1037</identifier><identifier type="ArticleID">MDS1037</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2001 Movement Disorder Society</accessCondition><recordInfo><recordOrigin>John Wiley & Sons, Inc.</recordOrigin><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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