Glial cell death induced by overexpression of α‐synuclein
Identifieur interne : 000398 ( Main/Corpus ); précédent : 000397; suivant : 000399Glial cell death induced by overexpression of α‐synuclein
Auteurs : Nadia Stefanova ; Lars Klimaschewski ; Werner Poewe ; Gregor K. Wenning ; Markus ReindlSource :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2001-09-01.
English descriptors
- KwdEn :
Abstract
α‐Synuclein is present in intracellular protein aggregates that are hallmarks of common neurodegenerative disorders including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. α‐Synuclein is localized in neurons and presynaptic terminals. Under pathological conditions, however, it is also found in glia. The role of α‐synuclein in glial cells and its relevance to the molecular pathology of neurodegenerative diseases is presently unclear. To investigate the consequence of α‐synuclein overexpression in glia, we transfected U373 astrocytoma cells with vectors encoding wild‐type human α‐synuclein or C‐terminally truncated synuclein fused to red fluorescent protein. α‐synuclein immunocytochemistry of transfected astroglial cells revealed diffuse cytoplasmic labeling associated with discrete inclusions both within cell bodies and processes. Susceptibility to oxidative stress was increased in astroglial cells overexpressing α‐synuclein, particularly in the presence of cytoplasmic inclusions. Furthermore, overexpression of α‐synuclein induced apoptotic death of astroglial cells as shown by TUNEL staining. Our in vitro model is the first to replicate salient features of the glial pathology associated with α‐synucleinopathies. It provides a simple testbed to further explore the cascade of events that leads to apoptotic glial cell death in some of these disorders; it may also be useful to assess the effects of therapeutic interventions including antioxidative and antiapoptotic strategies. J. Neurosci. Res. 65:432–438, 2001. © 2001 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jnr.1171
Links to Exploration step
ISTEX:93685E9138CCBF6824755999FAF57F488E8F92F5Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Glial cell death induced by overexpression of α‐synuclein</title><author><name sortKey="Stefanova, Nadia" sort="Stefanova, Nadia" uniqKey="Stefanova N" first="Nadia" last="Stefanova">Nadia Stefanova</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Anatomy and Histology, Medical University of Sofia, Bulgaria</mods:affiliation></affiliation></author><author><name sortKey="Klimaschewski, Lars" sort="Klimaschewski, Lars" uniqKey="Klimaschewski L" first="Lars" last="Klimaschewski">Lars Klimaschewski</name><affiliation><mods:affiliation>Department of Anatomy and Histology, University of Innsbruck, Austria</mods:affiliation></affiliation></author><author><name sortKey="Poewe, Werner" sort="Poewe, Werner" uniqKey="Poewe W" first="Werner" last="Poewe">Werner Poewe</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation></author><author><name sortKey="Wenning, Gregor K" sort="Wenning, Gregor K" uniqKey="Wenning G" first="Gregor K." last="Wenning">Gregor K. Wenning</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation></author><author><name sortKey="Reindl, Markus" sort="Reindl, Markus" uniqKey="Reindl M" first="Markus" last="Reindl">Markus Reindl</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:93685E9138CCBF6824755999FAF57F488E8F92F5</idno><date when="2001" year="2001">2001</date><idno type="doi">10.1002/jnr.1171</idno><idno type="url">https://api.istex.fr/document/93685E9138CCBF6824755999FAF57F488E8F92F5/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000398</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Glial cell death induced by overexpression of α‐synuclein</title><author><name sortKey="Stefanova, Nadia" sort="Stefanova, Nadia" uniqKey="Stefanova N" first="Nadia" last="Stefanova">Nadia Stefanova</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Anatomy and Histology, Medical University of Sofia, Bulgaria</mods:affiliation></affiliation></author><author><name sortKey="Klimaschewski, Lars" sort="Klimaschewski, Lars" uniqKey="Klimaschewski L" first="Lars" last="Klimaschewski">Lars Klimaschewski</name><affiliation><mods:affiliation>Department of Anatomy and Histology, University of Innsbruck, Austria</mods:affiliation></affiliation></author><author><name sortKey="Poewe, Werner" sort="Poewe, Werner" uniqKey="Poewe W" first="Werner" last="Poewe">Werner Poewe</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation></author><author><name sortKey="Wenning, Gregor K" sort="Wenning, Gregor K" uniqKey="Wenning G" first="Gregor K." last="Wenning">Gregor K. Wenning</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation></author><author><name sortKey="Reindl, Markus" sort="Reindl, Markus" uniqKey="Reindl M" first="Markus" last="Reindl">Markus Reindl</name><affiliation><mods:affiliation>Department of Neurology, University of Innsbruck, Austria</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. Res.</title><idno type="ISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-09-01">2001-09-01</date><biblScope unit="volume">65</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="432">432</biblScope><biblScope unit="page" to="438">438</biblScope></imprint><idno type="ISSN">0360-4012</idno></series><idno type="istex">93685E9138CCBF6824755999FAF57F488E8F92F5</idno><idno type="DOI">10.1002/jnr.1171</idno><idno type="ArticleID">JNR1171</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0360-4012</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>cell death</term><term>glia</term><term>oxidative stress</term><term>α‐synuclein</term><term>α‐synucleinopathies</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">α‐Synuclein is present in intracellular protein aggregates that are hallmarks of common neurodegenerative disorders including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. α‐Synuclein is localized in neurons and presynaptic terminals. Under pathological conditions, however, it is also found in glia. The role of α‐synuclein in glial cells and its relevance to the molecular pathology of neurodegenerative diseases is presently unclear. To investigate the consequence of α‐synuclein overexpression in glia, we transfected U373 astrocytoma cells with vectors encoding wild‐type human α‐synuclein or C‐terminally truncated synuclein fused to red fluorescent protein. α‐synuclein immunocytochemistry of transfected astroglial cells revealed diffuse cytoplasmic labeling associated with discrete inclusions both within cell bodies and processes. Susceptibility to oxidative stress was increased in astroglial cells overexpressing α‐synuclein, particularly in the presence of cytoplasmic inclusions. Furthermore, overexpression of α‐synuclein induced apoptotic death of astroglial cells as shown by TUNEL staining. Our in vitro model is the first to replicate salient features of the glial pathology associated with α‐synucleinopathies. It provides a simple testbed to further explore the cascade of events that leads to apoptotic glial cell death in some of these disorders; it may also be useful to assess the effects of therapeutic interventions including antioxidative and antiapoptotic strategies. J. Neurosci. Res. 65:432–438, 2001. © 2001 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Nadia Stefanova</name><affiliations><json:string>Department of Neurology, University of Innsbruck, Austria</json:string><json:string>Department of Anatomy and Histology, Medical University of Sofia, Bulgaria</json:string></affiliations></json:item><json:item><name>Lars Klimaschewski</name><affiliations><json:string>Department of Anatomy and Histology, University of Innsbruck, Austria</json:string></affiliations></json:item><json:item><name>Werner Poewe</name><affiliations><json:string>Department of Neurology, University of Innsbruck, Austria</json:string></affiliations></json:item><json:item><name>Gregor K. Wenning</name><affiliations><json:string>Department of Neurology, University of Innsbruck, Austria</json:string></affiliations></json:item><json:item><name>Markus Reindl</name><affiliations><json:string>Department of Neurology, University of Innsbruck, Austria</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>α‐synuclein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glia</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>oxidative stress</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cell death</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>α‐synucleinopathies</value></json:item></subject><articleId><json:string>JNR1171</json:string></articleId><language><json:string>eng</json:string></language><abstract>α‐Synuclein is present in intracellular protein aggregates that are hallmarks of common neurodegenerative disorders including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. α‐Synuclein is localized in neurons and presynaptic terminals. Under pathological conditions, however, it is also found in glia. The role of α‐synuclein in glial cells and its relevance to the molecular pathology of neurodegenerative diseases is presently unclear. To investigate the consequence of α‐synuclein overexpression in glia, we transfected U373 astrocytoma cells with vectors encoding wild‐type human α‐synuclein or C‐terminally truncated synuclein fused to red fluorescent protein. α‐synuclein immunocytochemistry of transfected astroglial cells revealed diffuse cytoplasmic labeling associated with discrete inclusions both within cell bodies and processes. Susceptibility to oxidative stress was increased in astroglial cells overexpressing α‐synuclein, particularly in the presence of cytoplasmic inclusions. Furthermore, overexpression of α‐synuclein induced apoptotic death of astroglial cells as shown by TUNEL staining. Our in vitro model is the first to replicate salient features of the glial pathology associated with α‐synucleinopathies. It provides a simple testbed to further explore the cascade of events that leads to apoptotic glial cell death in some of these disorders; it may also be useful to assess the effects of therapeutic interventions including antioxidative and antiapoptotic strategies. J. Neurosci. Res. 65:432–438, 2001. © 2001 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>7.18</score><pdfVersion>1.2</pdfVersion><pdfPageSize>594 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>5</keywordCount><abstractCharCount>1586</abstractCharCount><pdfWordCount>4624</pdfWordCount><pdfCharCount>30736</pdfCharCount><pdfPageCount>7</pdfPageCount><abstractWordCount>213</abstractWordCount></qualityIndicators><title>Glial cell death induced by overexpression of α‐synuclein</title><genre><json:string>article</json:string></genre><host><volume>65</volume><publisherId><json:string>JNR</json:string></publisherId><pages><total>7</total><last>438</last><first>432</first></pages><issn><json:string>0360-4012</json:string></issn><issue>5</issue><subject><json:item><value>Research Article</value></json:item></subject><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1097-4547</json:string></eissn><title>Journal of Neuroscience Research</title><doi><json:string>10.1002/(ISSN)1097-4547</json:string></doi></host><publicationDate>2001</publicationDate><copyrightDate>2001</copyrightDate><doi><json:string>10.1002/jnr.1171</json:string></doi><id>93685E9138CCBF6824755999FAF57F488E8F92F5</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/93685E9138CCBF6824755999FAF57F488E8F92F5/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/93685E9138CCBF6824755999FAF57F488E8F92F5/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/93685E9138CCBF6824755999FAF57F488E8F92F5/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Glial cell death induced by overexpression of α‐synuclein</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><availability><p>WILEY</p></availability><date>2001</date></publicationStmt><notesStmt><note>FWF - No. P14633‐PHA;</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Glial cell death induced by overexpression of α‐synuclein</title><author><persName><forename type="first">Nadia</forename><surname>Stefanova</surname></persName><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation><affiliation>Department of Anatomy and Histology, Medical University of Sofia, Bulgaria</affiliation></author><author><persName><forename type="first">Lars</forename><surname>Klimaschewski</surname></persName><affiliation>Department of Anatomy and Histology, University of Innsbruck, Austria</affiliation></author><author><persName><forename type="first">Werner</forename><surname>Poewe</surname></persName><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation></author><author><persName><forename type="first">Gregor K.</forename><surname>Wenning</surname></persName><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation></author><author><persName><forename type="first">Markus</forename><surname>Reindl</surname></persName><note type="correspondence"><p>Correspondence: Department of Neurology, University of Innsbruck, Anichstrasse 35, A‐6020 Innsbruck, Austria</p></note><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation></author></analytic><monogr><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. Res.</title><idno type="pISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><idno type="DOI">10.1002/(ISSN)1097-4547</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-09-01"></date><biblScope unit="volume">65</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="432">432</biblScope><biblScope unit="page" to="438">438</biblScope></imprint></monogr><idno type="istex">93685E9138CCBF6824755999FAF57F488E8F92F5</idno><idno type="DOI">10.1002/jnr.1171</idno><idno type="ArticleID">JNR1171</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2001</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>α‐Synuclein is present in intracellular protein aggregates that are hallmarks of common neurodegenerative disorders including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. α‐Synuclein is localized in neurons and presynaptic terminals. Under pathological conditions, however, it is also found in glia. The role of α‐synuclein in glial cells and its relevance to the molecular pathology of neurodegenerative diseases is presently unclear. To investigate the consequence of α‐synuclein overexpression in glia, we transfected U373 astrocytoma cells with vectors encoding wild‐type human α‐synuclein or C‐terminally truncated synuclein fused to red fluorescent protein. α‐synuclein immunocytochemistry of transfected astroglial cells revealed diffuse cytoplasmic labeling associated with discrete inclusions both within cell bodies and processes. Susceptibility to oxidative stress was increased in astroglial cells overexpressing α‐synuclein, particularly in the presence of cytoplasmic inclusions. Furthermore, overexpression of α‐synuclein induced apoptotic death of astroglial cells as shown by TUNEL staining. Our in vitro model is the first to replicate salient features of the glial pathology associated with α‐synucleinopathies. It provides a simple testbed to further explore the cascade of events that leads to apoptotic glial cell death in some of these disorders; it may also be useful to assess the effects of therapeutic interventions including antioxidative and antiapoptotic strategies. J. Neurosci. Res. 65:432–438, 2001. © 2001 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>α‐synuclein</term></item><item><term>glia</term></item><item><term>oxidative stress</term></item><item><term>cell death</term></item><item><term>α‐synucleinopathies</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Research Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2001-02-14">Received</change><change when="2001-04-11">Registration</change><change when="2001-09-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/93685E9138CCBF6824755999FAF57F488E8F92F5/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Inc.</publisherName><publisherLoc>New York</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4547</doi><issn type="print">0360-4012</issn><issn type="electronic">1097-4547</issn><idGroup><id type="product" value="JNR"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF NEUROSCIENCE RESEARCH">Journal of Neuroscience Research</title><title type="short">J. Neurosci. Res.</title></titleGroup></publicationMeta><publicationMeta level="part" position="50"><doi origin="wiley" registered="yes">10.1002/jnr.v65:5</doi><numberingGroup><numbering type="journalVolume" number="65">65</numbering><numbering type="journalIssue">5</numbering></numberingGroup><coverDate startDate="2001-09-01">1 September 2001</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="100" status="forIssue"><doi origin="wiley" registered="yes">10.1002/jnr.1171</doi><idGroup><id type="unit" value="JNR1171"></id></idGroup><countGroup><count type="pageTotal" number="7"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title><title type="tocHeading1">Research Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2001 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2001-02-14"></event><event type="manuscriptRevised" date="2001-04-09"></event><event type="manuscriptAccepted" date="2001-04-11"></event><event type="firstOnline" date="2001-08-28"></event><event type="publishedOnlineFinalForm" date="2001-08-28"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.6 mode:FullText source:FullText result:FullText" date="2010-04-20"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-31"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-30"></event></eventGroup><numberingGroup><numbering type="pageFirst">432</numbering><numbering type="pageLast">438</numbering></numberingGroup><correspondenceTo>Department of Neurology, University of Innsbruck, Anichstrasse 35, A‐6020 Innsbruck, Austria</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JNR.JNR1171.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="3"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="27"></count><count type="wordTotal" number="5227"></count></countGroup><titleGroup><title type="main" xml:lang="en">Glial cell death induced by overexpression of α‐synuclein</title><title type="short" xml:lang="en">Overexpression of α‐Synuclein in Glia</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1 #af3"><personName><givenNames>Nadia</givenNames><familyName>Stefanova</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Lars</givenNames><familyName>Klimaschewski</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Werner</givenNames><familyName>Poewe</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Gregor K.</givenNames><familyName>Wenning</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Markus</givenNames><familyName>Reindl</familyName></personName><contactDetails><email>Markus.Reindl@uibk.ac.at</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="AT" type="organization"><unparsedAffiliation>Department of Neurology, University of Innsbruck, Austria</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="AT" type="organization"><unparsedAffiliation>Department of Anatomy and Histology, University of Innsbruck, Austria</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="BG" type="organization"><unparsedAffiliation>Department of Anatomy and Histology, Medical University of Sofia, Bulgaria</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">α‐synuclein</keyword><keyword xml:id="kwd2">glia</keyword><keyword xml:id="kwd3">oxidative stress</keyword><keyword xml:id="kwd4">cell death</keyword><keyword xml:id="kwd5">α‐synucleinopathies</keyword></keywordGroup><fundingInfo><fundingAgency>FWF</fundingAgency><fundingNumber>P14633‐PHA</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>α‐Synuclein is present in intracellular protein aggregates that are hallmarks of common neurodegenerative disorders including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. α‐Synuclein is localized in neurons and presynaptic terminals. Under pathological conditions, however, it is also found in glia. The role of α‐synuclein in glial cells and its relevance to the molecular pathology of neurodegenerative diseases is presently unclear. To investigate the consequence of α‐synuclein overexpression in glia, we transfected U373 astrocytoma cells with vectors encoding wild‐type human α‐synuclein or C‐terminally truncated synuclein fused to red fluorescent protein. α‐synuclein immunocytochemistry of transfected astroglial cells revealed diffuse cytoplasmic labeling associated with discrete inclusions both within cell bodies and processes. Susceptibility to oxidative stress was increased in astroglial cells overexpressing α‐synuclein, particularly in the presence of cytoplasmic inclusions. Furthermore, overexpression of α‐synuclein induced apoptotic death of astroglial cells as shown by TUNEL staining. Our in vitro model is the first to replicate salient features of the glial pathology associated with α‐synucleinopathies. It provides a simple testbed to further explore the cascade of events that leads to apoptotic glial cell death in some of these disorders; it may also be useful to assess the effects of therapeutic interventions including antioxidative and antiapoptotic strategies. J. Neurosci. Res. 65:432–438, 2001. © 2001 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Glial cell death induced by overexpression of α‐synuclein</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Overexpression of α‐Synuclein in Glia</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Glial cell death induced by overexpression of α‐synuclein</title></titleInfo><name type="personal"><namePart type="given">Nadia</namePart><namePart type="family">Stefanova</namePart><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation><affiliation>Department of Anatomy and Histology, Medical University of Sofia, Bulgaria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lars</namePart><namePart type="family">Klimaschewski</namePart><affiliation>Department of Anatomy and Histology, University of Innsbruck, Austria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Werner</namePart><namePart type="family">Poewe</namePart><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Gregor K.</namePart><namePart type="family">Wenning</namePart><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Markus</namePart><namePart type="family">Reindl</namePart><affiliation>Department of Neurology, University of Innsbruck, Austria</affiliation><description>Correspondence: Department of Neurology, University of Innsbruck, Anichstrasse 35, A‐6020 Innsbruck, Austria</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>John Wiley & Sons, Inc.</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2001-09-01</dateIssued><dateCaptured encoding="w3cdtf">2001-02-14</dateCaptured><dateValid encoding="w3cdtf">2001-04-11</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">3</extent><extent unit="references">27</extent><extent unit="words">5227</extent></physicalDescription><abstract lang="en">α‐Synuclein is present in intracellular protein aggregates that are hallmarks of common neurodegenerative disorders including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. α‐Synuclein is localized in neurons and presynaptic terminals. Under pathological conditions, however, it is also found in glia. The role of α‐synuclein in glial cells and its relevance to the molecular pathology of neurodegenerative diseases is presently unclear. To investigate the consequence of α‐synuclein overexpression in glia, we transfected U373 astrocytoma cells with vectors encoding wild‐type human α‐synuclein or C‐terminally truncated synuclein fused to red fluorescent protein. α‐synuclein immunocytochemistry of transfected astroglial cells revealed diffuse cytoplasmic labeling associated with discrete inclusions both within cell bodies and processes. Susceptibility to oxidative stress was increased in astroglial cells overexpressing α‐synuclein, particularly in the presence of cytoplasmic inclusions. Furthermore, overexpression of α‐synuclein induced apoptotic death of astroglial cells as shown by TUNEL staining. Our in vitro model is the first to replicate salient features of the glial pathology associated with α‐synucleinopathies. It provides a simple testbed to further explore the cascade of events that leads to apoptotic glial cell death in some of these disorders; it may also be useful to assess the effects of therapeutic interventions including antioxidative and antiapoptotic strategies. J. Neurosci. Res. 65:432–438, 2001. © 2001 Wiley‐Liss, Inc.</abstract><note type="funding">FWF - No. P14633‐PHA; </note><subject lang="en"><genre>Keywords</genre><topic>α‐synuclein</topic><topic>glia</topic><topic>oxidative stress</topic><topic>cell death</topic><topic>α‐synucleinopathies</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Neuroscience Research</title></titleInfo><titleInfo type="abbreviated"><title>J. Neurosci. Res.</title></titleInfo><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Research Article</topic></subject><identifier type="ISSN">0360-4012</identifier><identifier type="eISSN">1097-4547</identifier><identifier type="DOI">10.1002/(ISSN)1097-4547</identifier><identifier type="PublisherID">JNR</identifier><part><date>2001</date><detail type="volume"><caption>vol.</caption><number>65</number></detail><detail type="issue"><caption>no.</caption><number>5</number></detail><extent unit="pages"><start>432</start><end>438</end><total>7</total></extent></part></relatedItem><identifier type="istex">93685E9138CCBF6824755999FAF57F488E8F92F5</identifier><identifier type="DOI">10.1002/jnr.1171</identifier><identifier type="ArticleID">JNR1171</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2001 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>John Wiley & Sons, Inc.</recordOrigin></recordInfo></mods></metadata><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 000398 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000398 | 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:93685E9138CCBF6824755999FAF57F488E8F92F5
|texte= Glial cell death induced by overexpression of α‐synuclein
}}
| This area was generated with Dilib version V0.6.23. |  |