Disrupted mitochondrial electron transport function increases expression of anti‐apoptotic Bcl‐2 and Bcl‐XL proteins in SH‐SY5Y neuroblastoma and in Parkinson disease cybrid cells through oxidative stress
Identifieur interne : 000180 ( Main/Corpus ); précédent : 000179; suivant : 000181Disrupted mitochondrial electron transport function increases expression of anti‐apoptotic Bcl‐2 and Bcl‐XL proteins in SH‐SY5Y neuroblastoma and in Parkinson disease cybrid cells through oxidative stress
Auteurs : George A. Veech ; Jameel Dennis ; Paula M. Keeney ; Christopher P. Fall ; Russell H. Swerdlow ; W. Davis Parker Jr. ; James P. Bennett Jr.Source :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2000-09-15.
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- KwdEn :
Abstract
Death of dopamine neurons in Parkinson disease (PD) may arise from consequences of the complex I (C‐I) defect in the mitochondrial electron transport chain (ETC). Whether cells activate programmed death (apoptosis) pathways derives, in part, from relative activities of proteins such as bcl‐2 and bcl‐XL , that have anti‐apoptotic actions. We studied the responses of bcl‐2 and bcl‐XL genes in pharmacologic (acute incubation with methylpyridinium (MPP+)) and mitochondrial transgenic (“cybrid”) models of Parkinson disease C‐I defects. MPP+ incubation increased levels of bcl‐2 and bcl‐XL proteins in native SH‐SY5Y cells but not in ρ0 cells devoid of ETC activity. MPP+ increased bcl‐2 mRNA levels by 40% at 8 hr. Confocal microscopic imaging showed that the intracellular distribution of immunoreactive bcl‐2 was not significantly associated with mitochondrial membranes at baseline but was associated with mitochondria after 12 hr of MPP+. Immunoreactive bcl‐XL protein was significantly and equally associated with mitochondrial membranes both at baseline and after MPP+. PD cybrids showed increased basal levels of bcl‐2 and bcl‐XL proteins, similar to the maximum levels found after MPP+ treatment of control SY5Y cells. After MPP+ exposure, bcl‐2 protein levels increased in control cybrids but did not increase further in PD cybrids. Both pharmacologically generated and transgenically induced C‐I inhibition increases levels of anti‐apoptotic bcl proteins, possibly from increased gene transcription. Augmentation of bcl‐2 and bcl‐XL expression may delay neurodegeneration in PD. J. Neurosci. Res. 61:693–700, 2000. © 2000 Wiley‐Liss, Inc.
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DOI: 10.1002/1097-4547(20000915)61:6<693::AID-JNR13>3.0.CO;2-4
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PD cybrids showed increased basal levels of bcl‐2 and bcl‐XL proteins, similar to the maximum levels found after MPP+ treatment of control SY5Y cells. After MPP+ exposure, bcl‐2 protein levels increased in control cybrids but did not increase further in PD cybrids. Both pharmacologically generated and transgenically induced C‐I inhibition increases levels of anti‐apoptotic bcl proteins, possibly from increased gene transcription. Augmentation of bcl‐2 and bcl‐XL expression may delay neurodegeneration in PD. J. Neurosci. Res. 61:693–700, 2000. © 2000 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>George A. 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Swerdlow</name><affiliations><json:string>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</json:string></affiliations></json:item><json:item><name>W. Davis Parker Jr.</name><affiliations><json:string>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</json:string></affiliations></json:item><json:item><name>James P. 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Whether cells activate programmed death (apoptosis) pathways derives, in part, from relative activities of proteins such as bcl‐2 and bcl‐XL , that have anti‐apoptotic actions. We studied the responses of bcl‐2 and bcl‐XL genes in pharmacologic (acute incubation with methylpyridinium (MPP+)) and mitochondrial transgenic (“cybrid”) models of Parkinson disease C‐I defects. MPP+ incubation increased levels of bcl‐2 and bcl‐XL proteins in native SH‐SY5Y cells but not in ρ0 cells devoid of ETC activity. MPP+ increased bcl‐2 mRNA levels by 40% at 8 hr. Confocal microscopic imaging showed that the intracellular distribution of immunoreactive bcl‐2 was not significantly associated with mitochondrial membranes at baseline but was associated with mitochondria after 12 hr of MPP+. Immunoreactive bcl‐XL protein was significantly and equally associated with mitochondrial membranes both at baseline and after MPP+. PD cybrids showed increased basal levels of bcl‐2 and bcl‐XL proteins, similar to the maximum levels found after MPP+ treatment of control SY5Y cells. After MPP+ exposure, bcl‐2 protein levels increased in control cybrids but did not increase further in PD cybrids. Both pharmacologically generated and transgenically induced C‐I inhibition increases levels of anti‐apoptotic bcl proteins, possibly from increased gene transcription. Augmentation of bcl‐2 and bcl‐XL expression may delay neurodegeneration in PD. J. Neurosci. 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Davis</forename><surname>Parker Jr.</surname></persName><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation></author><author><persName><forename type="first">James P.</forename><surname>Bennett Jr.</surname></persName><note type="correspondence"><p>Correspondence: Box 394 UVA‐HSC, Charlottesville, VA 22908</p></note><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation></author></analytic><monogr><title level="j">Journal of Neuroscience Research</title><title level="j" type="abbrev">J. Neurosci. 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Whether cells activate programmed death (apoptosis) pathways derives, in part, from relative activities of proteins such as bcl‐2 and bcl‐XL , that have anti‐apoptotic actions. We studied the responses of bcl‐2 and bcl‐XL genes in pharmacologic (acute incubation with methylpyridinium (MPP+)) and mitochondrial transgenic (“cybrid”) models of Parkinson disease C‐I defects. MPP+ incubation increased levels of bcl‐2 and bcl‐XL proteins in native SH‐SY5Y cells but not in ρ0 cells devoid of ETC activity. MPP+ increased bcl‐2 mRNA levels by 40% at 8 hr. Confocal microscopic imaging showed that the intracellular distribution of immunoreactive bcl‐2 was not significantly associated with mitochondrial membranes at baseline but was associated with mitochondria after 12 hr of MPP+. Immunoreactive bcl‐XL protein was significantly and equally associated with mitochondrial membranes both at baseline and after MPP+. PD cybrids showed increased basal levels of bcl‐2 and bcl‐XL proteins, similar to the maximum levels found after MPP+ treatment of control SY5Y cells. After MPP+ exposure, bcl‐2 protein levels increased in control cybrids but did not increase further in PD cybrids. Both pharmacologically generated and transgenically induced C‐I inhibition increases levels of anti‐apoptotic bcl proteins, possibly from increased gene transcription. Augmentation of bcl‐2 and bcl‐XL expression may delay neurodegeneration in PD. J. Neurosci. 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Neurosci. Res.</title></titleGroup></publicationMeta><publicationMeta level="part" position="60"><doi origin="wiley" registered="yes">10.1002/1097-4547(20000915)61:6<>1.0.CO;2-3</doi><numberingGroup><numbering type="journalVolume" number="61">61</numbering><numbering type="journalIssue">6</numbering></numberingGroup><coverDate startDate="2000-09-15">15 September 2000</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="13" status="forIssue"><doi origin="wiley" registered="yes">10.1002/1097-4547(20000915)61:6<693::AID-JNR13>3.0.CO;2-4</doi><idGroup><id type="unit" value="JNR13"></id></idGroup><countGroup><count type="pageTotal" number="8"></count></countGroup><titleGroup><title type="articleCategory">Article</title><title type="tocHeading1">Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2000 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2000-02-28"></event><event type="manuscriptRevised" date="2000-04-24"></event><event type="manuscriptAccepted" date="2000-04-25"></event><event type="firstOnline" date="2000-08-30"></event><event type="publishedOnlineFinalForm" date="2000-08-30"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-15"></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">693</numbering><numbering type="pageLast">700</numbering></numberingGroup><correspondenceTo>Box 394 UVA‐HSC, Charlottesville, VA 22908</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JNR.JNR13.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="7"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="35"></count><count type="wordTotal" number="4724"></count></countGroup><titleGroup><title type="main" xml:lang="en">Disrupted mitochondrial electron transport function increases expression of anti‐apoptotic Bcl‐2 and Bcl‐X<sub>L</sub> proteins in SH‐SY5Y neuroblastoma and in Parkinson disease cybrid cells through oxidative stress</title><title type="short" xml:lang="en">Methylpyridinium Effects on Bcl Proteins</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>George A.</givenNames><familyName>Veech</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Jameel</givenNames><familyName>Dennis</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Paula M.</givenNames><familyName>Keeney</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Christopher P.</givenNames><familyName>Fall</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Russell H.</givenNames><familyName>Swerdlow</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af1"><personName><givenNames>W. Davis</givenNames><familyName>Parker</familyName><nameSuffix>Jr.</nameSuffix></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>James P.</givenNames><familyName>Bennett</familyName><nameSuffix>Jr.</nameSuffix></personName><contactDetails><email>Bennett@virginia.edu</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">Parkinson disease</keyword><keyword xml:id="kwd2">cybrids</keyword><keyword xml:id="kwd3">methylpyridinium</keyword><keyword xml:id="kwd4">bcl‐2</keyword><keyword xml:id="kwd5">bcl‐X<sub>L</sub></keyword><keyword xml:id="kwd6">oxidative stress</keyword></keywordGroup><fundingInfo><fundingAgency>NIH</fundingAgency><fundingNumber>NS35325</fundingNumber><fundingNumber>AG14373</fundingNumber><fundingNumber>NS39788</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Death of dopamine neurons in Parkinson disease (PD) may arise from consequences of the complex I (C‐I) defect in the mitochondrial electron transport chain (ETC). Whether cells activate programmed death (apoptosis) pathways derives, in part, from relative activities of proteins such as bcl‐2 and bcl‐X<sub>L</sub> , that have anti‐apoptotic actions. We studied the responses of bcl‐2 and bcl‐X<sub>L</sub> genes in pharmacologic (acute incubation with methylpyridinium (MPP+)) and mitochondrial transgenic (“cybrid”) models of Parkinson disease C‐I defects. MPP+ incubation increased levels of bcl‐2 and bcl‐X<sub>L</sub> proteins in native SH‐SY5Y cells but not in ρ<sup>0</sup> cells devoid of ETC activity. MPP+ increased bcl‐2 mRNA levels by 40% at 8 hr. Confocal microscopic imaging showed that the intracellular distribution of immunoreactive bcl‐2 was not significantly associated with mitochondrial membranes at baseline but was associated with mitochondria after 12 hr of MPP+. Immunoreactive bcl‐X<sub>L</sub> protein was significantly and equally associated with mitochondrial membranes both at baseline and after MPP+. PD cybrids showed increased basal levels of bcl‐2 and bcl‐X<sub>L</sub> proteins, similar to the maximum levels found after MPP+ treatment of control SY5Y cells. After MPP+ exposure, bcl‐2 protein levels increased in control cybrids but did not increase further in PD cybrids. Both pharmacologically generated and transgenically induced C‐I inhibition increases levels of anti‐apoptotic bcl proteins, possibly from increased gene transcription. Augmentation of bcl‐2 and bcl‐X<sub>L</sub> expression may delay neurodegeneration in PD. J. Neurosci. Res. 61:693–700, 2000. © 2000 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Disrupted mitochondrial electron transport function increases expression of anti‐apoptotic Bcl‐2 and Bcl‐XL proteins in SH‐SY5Y neuroblastoma and in Parkinson disease cybrid cells through oxidative stress</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Methylpyridinium Effects on Bcl Proteins</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Disrupted mitochondrial electron transport function increases expression of anti‐apoptotic Bcl‐2 and Bcl‐X</title></titleInfo><name type="personal"><namePart type="given">George A.</namePart><namePart type="family">Veech</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jameel</namePart><namePart type="family">Dennis</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Paula M.</namePart><namePart type="family">Keeney</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christopher P.</namePart><namePart type="family">Fall</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Russell H.</namePart><namePart type="family">Swerdlow</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W. Davis</namePart><namePart type="family">Parker Jr.</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">James P.</namePart><namePart type="family">Bennett Jr.</namePart><affiliation>Center for the Study of Neurodegenerative Diseases, University of Virginia Health Sciences Center, Charlottesville, Virginia</affiliation><description>Correspondence: Box 394 UVA‐HSC, Charlottesville, VA 22908</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">2000-09-15</dateIssued><dateCaptured encoding="w3cdtf">2000-02-28</dateCaptured><dateValid encoding="w3cdtf">2000-04-25</dateValid><copyrightDate encoding="w3cdtf">2000</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">7</extent><extent unit="references">35</extent><extent unit="words">4724</extent></physicalDescription><abstract lang="en">Death of dopamine neurons in Parkinson disease (PD) may arise from consequences of the complex I (C‐I) defect in the mitochondrial electron transport chain (ETC). Whether cells activate programmed death (apoptosis) pathways derives, in part, from relative activities of proteins such as bcl‐2 and bcl‐XL , that have anti‐apoptotic actions. We studied the responses of bcl‐2 and bcl‐XL genes in pharmacologic (acute incubation with methylpyridinium (MPP+)) and mitochondrial transgenic (“cybrid”) models of Parkinson disease C‐I defects. MPP+ incubation increased levels of bcl‐2 and bcl‐XL proteins in native SH‐SY5Y cells but not in ρ0 cells devoid of ETC activity. MPP+ increased bcl‐2 mRNA levels by 40% at 8 hr. Confocal microscopic imaging showed that the intracellular distribution of immunoreactive bcl‐2 was not significantly associated with mitochondrial membranes at baseline but was associated with mitochondria after 12 hr of MPP+. Immunoreactive bcl‐XL protein was significantly and equally associated with mitochondrial membranes both at baseline and after MPP+. PD cybrids showed increased basal levels of bcl‐2 and bcl‐XL proteins, similar to the maximum levels found after MPP+ treatment of control SY5Y cells. After MPP+ exposure, bcl‐2 protein levels increased in control cybrids but did not increase further in PD cybrids. Both pharmacologically generated and transgenically induced C‐I inhibition increases levels of anti‐apoptotic bcl proteins, possibly from increased gene transcription. Augmentation of bcl‐2 and bcl‐XL expression may delay neurodegeneration in PD. J. Neurosci. Res. 61:693–700, 2000. © 2000 Wiley‐Liss, Inc.</abstract><note type="funding">NIH - No. NS35325; No. AG14373; No. NS39788; </note><subject lang="en"><genre>Keywords</genre><topic>Parkinson disease</topic><topic>cybrids</topic><topic>methylpyridinium</topic><topic>bcl‐2</topic><topic>bcl‐XL</topic><topic>oxidative stress</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>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>2000</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>693</start><end>700</end><total>8</total></extent></part></relatedItem><identifier type="istex">4EA767327FDBDB4FDC2C5E0DB91CDAC6211B849D</identifier><identifier type="DOI">10.1002/1097-4547(20000915)61:6<693::AID-JNR13>3.0.CO;2-4</identifier><identifier type="ArticleID">JNR13</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2000 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)
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