Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells
Identifieur interne : 001D06 ( Istex/Corpus ); précédent : 001D05; suivant : 001D07Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells
Auteurs : Julie Deguil ; David Jailloux ; Guylène Page ; Bernard Fauconneau ; Jean-Luc Houeto ; Michel Philippe ; Jean-Marc Muller ; Stéphanie PainSource :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2007-07.
English descriptors
Abstract
Parkinson's disease (PD) and 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) toxicity are both associated with dopaminergic neuron death in the substantia nigra. Although a variety of evidence has shown that degenerative cells have apoptotic features, the role of apoptosis in disease pathology remains controversial. The 1‐methyl‐4‐phenylpyridinium ion (MPP+), a metabolite of MPTP, was recently shown to alter the expression of proteins involved in translational control. The initiation step of translational control is regulated by a cascade of phosphorylation affecting proteins of the antiapoptotic way controlled by mammalian target of rapamycin (mTOR) and of the proapoptotic way controlled by double‐stranded RNA protein–dependent kinase (PKR). A study showed that MPP+ induced an increase in eIF2α phosphorylation, leading to inhibition of protein synthesis. The aims of our study were: (1) to assess the effects of MPP+ toxicity on molecular factors of PKR and mTOR signaling pathways in murine neuroblastoma cells, and (2) to examine the ability of VIP and PACAP peptides to counteract the MPP+ toxicity. Our findings showed that MPP+ induced phosphorylation of eIF2α and significantly reduced the expression of phosphorylated mTOR, p70S6K, eIF4E, and 4E‐BP1, suggesting its toxicity in controlling protein synthesis. Furthermore, the VIP peptide had no effect on either the PKR or the mTOR signaling pathway. On the contrary, the PACAP 27 neuropeptide prevented MPP+‐induced eIF2α phosphorylation and blocked MPP+ toxicity in molecular factors of the mTOR pathway. And last, PACAP 27 seemed to protect Neuro‐2a cells from the apoptotic process as assessed by the decreased nuclear condensation after DAPI staining. These results could open new paths of research of PACAP in PD. © 2007 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jnr.21318
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ISTEX:D3717CCFF23846F4D89055677846D59FCCF5C856Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title><author><name sortKey="Deguil, Julie" sort="Deguil, Julie" uniqKey="Deguil J" first="Julie" last="Deguil">Julie Deguil</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Jailloux, David" sort="Jailloux, David" uniqKey="Jailloux D" first="David" last="Jailloux">David Jailloux</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Page, Guylene" sort="Page, Guylene" uniqKey="Page G" first="Guylène" last="Page">Guylène 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(PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title><author><name sortKey="Deguil, Julie" sort="Deguil, Julie" uniqKey="Deguil J" first="Julie" last="Deguil">Julie Deguil</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Jailloux, David" sort="Jailloux, David" uniqKey="Jailloux D" first="David" last="Jailloux">David Jailloux</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Page, Guylene" sort="Page, Guylene" uniqKey="Page G" first="Guylène" last="Page">Guylène Page</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Fauconneau, Bernard" sort="Fauconneau, Bernard" uniqKey="Fauconneau B" first="Bernard" last="Fauconneau">Bernard Fauconneau</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Houeto, Jean Uc" sort="Houeto, Jean Uc" uniqKey="Houeto J" first="Jean-Luc" last="Houeto">Jean-Luc Houeto</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service de Neurologie, CHU La Milétrie, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Philippe, Michel" sort="Philippe, Michel" uniqKey="Philippe M" first="Michel" last="Philippe">Michel Philippe</name><affiliation><mods:affiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Muller, Jean Arc" sort="Muller, Jean Arc" uniqKey="Muller J" first="Jean-Marc" last="Muller">Jean-Marc Muller</name><affiliation><mods:affiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</mods:affiliation></affiliation></author><author><name sortKey="Pain, Stephanie" sort="Pain, Stephanie" uniqKey="Pain S" first="Stéphanie" last="Pain">Stéphanie Pain</name><affiliation><mods:affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</mods:affiliation></affiliation><affiliation><mods:affiliation>EA 3808 GREVIC, Pôle de Biologie Santé, 40 avenue du Recteur Pineau, 86022 Poitiers cedex, France</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>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2007-07">2007-07</date><biblScope unit="volume">85</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="2017">2017</biblScope><biblScope unit="page" to="2025">2025</biblScope></imprint><idno type="ISSN">0360-4012</idno></series><idno type="istex">D3717CCFF23846F4D89055677846D59FCCF5C856</idno><idno type="DOI">10.1002/jnr.21318</idno><idno type="ArticleID">JNR21318</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0360-4012</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>MPP+, translational control</term><term>PACAP</term><term>VIP</term><term>neuroblastoma cells</term><term>neuroprotection</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkinson's disease (PD) and 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) toxicity are both associated with dopaminergic neuron death in the substantia nigra. Although a variety of evidence has shown that degenerative cells have apoptotic features, the role of apoptosis in disease pathology remains controversial. The 1‐methyl‐4‐phenylpyridinium ion (MPP+), a metabolite of MPTP, was recently shown to alter the expression of proteins involved in translational control. The initiation step of translational control is regulated by a cascade of phosphorylation affecting proteins of the antiapoptotic way controlled by mammalian target of rapamycin (mTOR) and of the proapoptotic way controlled by double‐stranded RNA protein–dependent kinase (PKR). A study showed that MPP+ induced an increase in eIF2α phosphorylation, leading to inhibition of protein synthesis. The aims of our study were: (1) to assess the effects of MPP+ toxicity on molecular factors of PKR and mTOR signaling pathways in murine neuroblastoma cells, and (2) to examine the ability of VIP and PACAP peptides to counteract the MPP+ toxicity. Our findings showed that MPP+ induced phosphorylation of eIF2α and significantly reduced the expression of phosphorylated mTOR, p70S6K, eIF4E, and 4E‐BP1, suggesting its toxicity in controlling protein synthesis. Furthermore, the VIP peptide had no effect on either the PKR or the mTOR signaling pathway. On the contrary, the PACAP 27 neuropeptide prevented MPP+‐induced eIF2α phosphorylation and blocked MPP+ toxicity in molecular factors of the mTOR pathway. And last, PACAP 27 seemed to protect Neuro‐2a cells from the apoptotic process as assessed by the decreased nuclear condensation after DAPI staining. These results could open new paths of research of PACAP in PD. © 2007 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Julie Deguil</name><affiliations><json:string>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</json:string></affiliations></json:item><json:item><name>David Jailloux</name><affiliations><json:string>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</json:string></affiliations></json:item><json:item><name>Guylène Page</name><affiliations><json:string>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</json:string></affiliations></json:item><json:item><name>Bernard Fauconneau</name><affiliations><json:string>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</json:string><json:string>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</json:string></affiliations></json:item><json:item><name>Jean‐Luc Houeto</name><affiliations><json:string>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</json:string><json:string>Service de Neurologie, CHU La Milétrie, Poitiers, France</json:string></affiliations></json:item><json:item><name>Michel Philippe</name><affiliations><json:string>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</json:string></affiliations></json:item><json:item><name>Jean‐Marc Muller</name><affiliations><json:string>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</json:string></affiliations></json:item><json:item><name>Stéphanie Pain</name><affiliations><json:string>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</json:string><json:string>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</json:string><json:string>EA 3808 GREVIC, Pôle de Biologie Santé, 40 avenue du Recteur Pineau, 86022 Poitiers cedex, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>MPP+, translational control</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neuroblastoma cells</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neuroprotection</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PACAP</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>VIP</value></json:item></subject><articleId><json:string>JNR21318</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Parkinson's disease (PD) and 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) toxicity are both associated with dopaminergic neuron death in the substantia nigra. Although a variety of evidence has shown that degenerative cells have apoptotic features, the role of apoptosis in disease pathology remains controversial. The 1‐methyl‐4‐phenylpyridinium ion (MPP+), a metabolite of MPTP, was recently shown to alter the expression of proteins involved in translational control. The initiation step of translational control is regulated by a cascade of phosphorylation affecting proteins of the antiapoptotic way controlled by mammalian target of rapamycin (mTOR) and of the proapoptotic way controlled by double‐stranded RNA protein–dependent kinase (PKR). A study showed that MPP+ induced an increase in eIF2α phosphorylation, leading to inhibition of protein synthesis. The aims of our study were: (1) to assess the effects of MPP+ toxicity on molecular factors of PKR and mTOR signaling pathways in murine neuroblastoma cells, and (2) to examine the ability of VIP and PACAP peptides to counteract the MPP+ toxicity. Our findings showed that MPP+ induced phosphorylation of eIF2α and significantly reduced the expression of phosphorylated mTOR, p70S6K, eIF4E, and 4E‐BP1, suggesting its toxicity in controlling protein synthesis. Furthermore, the VIP peptide had no effect on either the PKR or the mTOR signaling pathway. On the contrary, the PACAP 27 neuropeptide prevented MPP+‐induced eIF2α phosphorylation and blocked MPP+ toxicity in molecular factors of the mTOR pathway. And last, PACAP 27 seemed to protect Neuro‐2a cells from the apoptotic process as assessed by the decreased nuclear condensation after DAPI staining. These results could open new paths of research of PACAP in PD. © 2007 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>8</score><pdfVersion>1.3</pdfVersion><pdfPageSize>612 x 810 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1817</abstractCharCount><pdfWordCount>6228</pdfWordCount><pdfCharCount>39567</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>264</abstractWordCount></qualityIndicators><title>Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title><refBibs><json:item><author><json:item><name>P Anglade</name></json:item><json:item><name>S Vyas</name></json:item><json:item><name>F Javoy‐Agid</name></json:item><json:item><name>MT Herrero</name></json:item><json:item><name>PP Michel</name></json:item><json:item><name>J Marquez</name></json:item><json:item><name>A Mouatt‐Prigent</name></json:item><json:item><name>M 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Neuro‐2a neuroblastoma cells</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><p>Copyright © 2007 Wiley‐Liss, Inc.</p></availability><date>2007</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title><author xml:id="author-1"><persName><forename type="first">Julie</forename><surname>Deguil</surname></persName><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation></author><author xml:id="author-2"><persName><forename type="first">David</forename><surname>Jailloux</surname></persName><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Guylène</forename><surname>Page</surname></persName><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation></author><author xml:id="author-4"><persName><forename type="first">Bernard</forename><surname>Fauconneau</surname></persName><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><affiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</affiliation></author><author xml:id="author-5"><persName><forename type="first">Jean‐Luc</forename><surname>Houeto</surname></persName><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><affiliation>Service de Neurologie, CHU La Milétrie, Poitiers, France</affiliation></author><author xml:id="author-6"><persName><forename type="first">Michel</forename><surname>Philippe</surname></persName><affiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</affiliation></author><author xml:id="author-7"><persName><forename type="first">Jean‐Marc</forename><surname>Muller</surname></persName><affiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</affiliation></author><author xml:id="author-8"><persName><forename type="first">Stéphanie</forename><surname>Pain</surname></persName><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><affiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</affiliation><affiliation>EA 3808 GREVIC, Pôle de Biologie Santé, 40 avenue du Recteur Pineau, 86022 Poitiers cedex, France</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>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2007-07"></date><biblScope unit="volume">85</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="2017">2017</biblScope><biblScope unit="page" to="2025">2025</biblScope></imprint></monogr><idno type="istex">D3717CCFF23846F4D89055677846D59FCCF5C856</idno><idno type="DOI">10.1002/jnr.21318</idno><idno type="ArticleID">JNR21318</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2007</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Parkinson's disease (PD) and 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) toxicity are both associated with dopaminergic neuron death in the substantia nigra. Although a variety of evidence has shown that degenerative cells have apoptotic features, the role of apoptosis in disease pathology remains controversial. The 1‐methyl‐4‐phenylpyridinium ion (MPP+), a metabolite of MPTP, was recently shown to alter the expression of proteins involved in translational control. The initiation step of translational control is regulated by a cascade of phosphorylation affecting proteins of the antiapoptotic way controlled by mammalian target of rapamycin (mTOR) and of the proapoptotic way controlled by double‐stranded RNA protein–dependent kinase (PKR). A study showed that MPP+ induced an increase in eIF2α phosphorylation, leading to inhibition of protein synthesis. The aims of our study were: (1) to assess the effects of MPP+ toxicity on molecular factors of PKR and mTOR signaling pathways in murine neuroblastoma cells, and (2) to examine the ability of VIP and PACAP peptides to counteract the MPP+ toxicity. Our findings showed that MPP+ induced phosphorylation of eIF2α and significantly reduced the expression of phosphorylated mTOR, p70S6K, eIF4E, and 4E‐BP1, suggesting its toxicity in controlling protein synthesis. Furthermore, the VIP peptide had no effect on either the PKR or the mTOR signaling pathway. On the contrary, the PACAP 27 neuropeptide prevented MPP+‐induced eIF2α phosphorylation and blocked MPP+ toxicity in molecular factors of the mTOR pathway. And last, PACAP 27 seemed to protect Neuro‐2a cells from the apoptotic process as assessed by the decreased nuclear condensation after DAPI staining. These results could open new paths of research of PACAP in PD. © 2007 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>keywords</head><item><term>MPP+, translational control</term></item><item><term>neuroblastoma cells</term></item><item><term>neuroprotection</term></item><item><term>PACAP</term></item><item><term>VIP</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="2006-09-22">Received</change><change when="2007-02-12">Registration</change><change when="2007-07">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/D3717CCFF23846F4D89055677846D59FCCF5C856/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>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</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="90"><doi origin="wiley" registered="yes">10.1002/jnr.v85:9</doi><numberingGroup><numbering type="journalVolume" number="85">85</numbering><numbering type="journalIssue">9</numbering></numberingGroup><coverDate startDate="2007-07">July 2007</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="190" status="forIssue"><doi origin="wiley" registered="yes">10.1002/jnr.21318</doi><idGroup><id type="unit" value="JNR21318"></id></idGroup><countGroup><count type="pageTotal" number="9"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title><title type="tocHeading1">Research Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2007 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2006-09-22"></event><event type="manuscriptRevised" date="2007-01-29"></event><event type="manuscriptAccepted" 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href="file:JNR.JNR21318.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="7"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="58"></count><count type="wordTotal" number="6539"></count></countGroup><titleGroup><title type="main" xml:lang="en">Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP<sup>+</sup>‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title><title type="short" xml:lang="en">Parkinson Model and Translational Control</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Julie</givenNames><familyName>Deguil</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>David</givenNames><familyName>Jailloux</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Guylène</givenNames><familyName>Page</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1 #af2"><personName><givenNames>Bernard</givenNames><familyName>Fauconneau</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1 #af3"><personName><givenNames>Jean‐Luc</givenNames><familyName>Houeto</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af4"><personName><givenNames>Michel</givenNames><familyName>Philippe</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af4"><personName><givenNames>Jean‐Marc</givenNames><familyName>Muller</familyName></personName></creator><creator xml:id="au8" creatorRole="author" affiliationRef="#af1 #af2" corresponding="yes"><personName><givenNames>Stéphanie</givenNames><familyName>Pain</familyName></personName><contactDetails><email normalForm="stephanie.pain@univ-poitiers.fr">stephanie.pain@univ‐poitiers.fr</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="FR" type="organization"><unparsedAffiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="FR" type="organization"><unparsedAffiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="FR" type="organization"><unparsedAffiliation>Service de Neurologie, CHU La Milétrie, Poitiers, France</unparsedAffiliation></affiliation><affiliation xml:id="af4" countryCode="FR" type="organization"><unparsedAffiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">MPP<sup>+</sup>, translational control</keyword><keyword xml:id="kwd2">neuroblastoma cells</keyword><keyword xml:id="kwd3">neuroprotection</keyword><keyword xml:id="kwd4">PACAP</keyword><keyword xml:id="kwd5">VIP</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Parkinson's disease (PD) and 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) toxicity are both associated with dopaminergic neuron death in the substantia nigra. Although a variety of evidence has shown that degenerative cells have apoptotic features, the role of apoptosis in disease pathology remains controversial. The 1‐methyl‐4‐phenylpyridinium ion (MPP<sup>+</sup>), a metabolite of MPTP, was recently shown to alter the expression of proteins involved in translational control. The initiation step of translational control is regulated by a cascade of phosphorylation affecting proteins of the antiapoptotic way controlled by mammalian target of rapamycin (mTOR) and of the proapoptotic way controlled by double‐stranded RNA protein–dependent kinase (PKR). A study showed that MPP<sup>+</sup> induced an increase in eIF2α phosphorylation, leading to inhibition of protein synthesis. The aims of our study were: (1) to assess the effects of MPP<sup>+</sup> toxicity on molecular factors of PKR and mTOR signaling pathways in murine neuroblastoma cells, and (2) to examine the ability of VIP and PACAP peptides to counteract the MPP<sup>+</sup> toxicity. Our findings showed that MPP<sup>+</sup> induced phosphorylation of eIF2α and significantly reduced the expression of phosphorylated mTOR, p70S6K, eIF4E, and 4E‐BP1, suggesting its toxicity in controlling protein synthesis. Furthermore, the VIP peptide had no effect on either the PKR or the mTOR signaling pathway. On the contrary, the PACAP 27 neuropeptide prevented MPP<sup>+</sup>‐induced eIF2α phosphorylation and blocked MPP<sup>+</sup> toxicity in molecular factors of the mTOR pathway. And last, PACAP 27 seemed to protect Neuro‐2a cells from the apoptotic process as assessed by the decreased nuclear condensation after DAPI staining. These results could open new paths of research of PACAP in PD. © 2007 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Parkinson Model and Translational Control</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Neuroprotective effects of pituitary adenylate cyclase–activating polypeptide (PACAP) in MPP+‐induced alteration of translational control in Neuro‐2a neuroblastoma cells</title></titleInfo><name type="personal"><namePart type="given">Julie</namePart><namePart type="family">Deguil</namePart><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David</namePart><namePart type="family">Jailloux</namePart><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Guylène</namePart><namePart type="family">Page</namePart><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Bernard</namePart><namePart type="family">Fauconneau</namePart><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><affiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean‐Luc</namePart><namePart type="family">Houeto</namePart><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><affiliation>Service de Neurologie, CHU La Milétrie, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michel</namePart><namePart type="family">Philippe</namePart><affiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean‐Marc</namePart><namePart type="family">Muller</namePart><affiliation>Institut de Physiologie et Biologie Cellulaires, UFR SFA, Pôle Biologie Santé, Poitiers, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Stéphanie</namePart><namePart type="family">Pain</namePart><affiliation>Groupe de Recherche sur le Vieillissement Cérébral GReViC, Pôle de Biologie Santé, Poitiers, France</affiliation><affiliation>Service de Pharmacologie Clinique, CHU la Milétrie, Poitiers, France</affiliation><affiliation>EA 3808 GREVIC, Pôle de Biologie Santé, 40 avenue du Recteur Pineau, 86022 Poitiers cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2007-07</dateIssued><dateCaptured encoding="w3cdtf">2006-09-22</dateCaptured><dateValid encoding="w3cdtf">2007-02-12</dateValid><copyrightDate encoding="w3cdtf">2007</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">58</extent><extent unit="words">6539</extent></physicalDescription><abstract lang="en">Parkinson's disease (PD) and 1‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine (MPTP) toxicity are both associated with dopaminergic neuron death in the substantia nigra. Although a variety of evidence has shown that degenerative cells have apoptotic features, the role of apoptosis in disease pathology remains controversial. The 1‐methyl‐4‐phenylpyridinium ion (MPP+), a metabolite of MPTP, was recently shown to alter the expression of proteins involved in translational control. The initiation step of translational control is regulated by a cascade of phosphorylation affecting proteins of the antiapoptotic way controlled by mammalian target of rapamycin (mTOR) and of the proapoptotic way controlled by double‐stranded RNA protein–dependent kinase (PKR). A study showed that MPP+ induced an increase in eIF2α phosphorylation, leading to inhibition of protein synthesis. The aims of our study were: (1) to assess the effects of MPP+ toxicity on molecular factors of PKR and mTOR signaling pathways in murine neuroblastoma cells, and (2) to examine the ability of VIP and PACAP peptides to counteract the MPP+ toxicity. Our findings showed that MPP+ induced phosphorylation of eIF2α and significantly reduced the expression of phosphorylated mTOR, p70S6K, eIF4E, and 4E‐BP1, suggesting its toxicity in controlling protein synthesis. Furthermore, the VIP peptide had no effect on either the PKR or the mTOR signaling pathway. On the contrary, the PACAP 27 neuropeptide prevented MPP+‐induced eIF2α phosphorylation and blocked MPP+ toxicity in molecular factors of the mTOR pathway. And last, PACAP 27 seemed to protect Neuro‐2a cells from the apoptotic process as assessed by the decreased nuclear condensation after DAPI staining. These results could open new paths of research of PACAP in PD. © 2007 Wiley‐Liss, Inc.</abstract><subject lang="en"><genre>keywords</genre><topic>MPP+, translational control</topic><topic>neuroblastoma cells</topic><topic>neuroprotection</topic><topic>PACAP</topic><topic>VIP</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>2007</date><detail type="volume"><caption>vol.</caption><number>85</number></detail><detail type="issue"><caption>no.</caption><number>9</number></detail><extent unit="pages"><start>2017</start><end>2025</end><total>9</total></extent></part></relatedItem><identifier type="istex">D3717CCFF23846F4D89055677846D59FCCF5C856</identifier><identifier type="DOI">10.1002/jnr.21318</identifier><identifier type="ArticleID">JNR21318</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2007 Wiley‐Liss, 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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