Cellular response of human neuroblastoma cells to α-synuclein fibrils, the main constituent of Lewy bodies.
Identifieur interne : 000195 ( PubMed/Checkpoint ); précédent : 000194; suivant : 000196Cellular response of human neuroblastoma cells to α-synuclein fibrils, the main constituent of Lewy bodies.
Auteurs : Laura Pieri [France] ; Philippe Chafey [France] ; Morgane Le Gall [France] ; Guilhem Clary [France] ; Ronald Melki [France] ; Virginie Redeker [France]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2016.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : alpha-Synuclein.
- chemical , physiology : alpha-Synuclein.
- chemical : Proteome.
- chemistry : Lewy Bodies.
- pathology : Neuroblastoma.
- Cell Line, Tumor, Humans, Protein Processing, Post-Translational, Two-Dimensional Difference Gel Electrophoresis.
Abstract
α-Synuclein (α-Syn) fibrils are the main constituent of Lewy bodies and a neuropathological hallmark of Parkinson's disease (PD). The propagation of α-Syn assemblies from cell to cell suggests that they are involved in PD progression. We previously showed that α-Syn fibrils are toxic because of their ability to bind and permeabilize cell membranes. Here, we document the cellular response in terms of proteome changes of SH-SY5Y cells exposed to exogenous α-Syn fibrils.
DOI: 10.1016/j.bbagen.2015.10.007
PubMed: 26468903
Affiliations:
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Inserm U1016, Institut Cochin, Paris, France; CNRS, UMR8104, Paris</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Paris</settlement></placeName><orgName type="university">Université Paris-Descartes</orgName></affiliation></author><author><name sortKey="Clary, Guilhem" sort="Clary, Guilhem" uniqKey="Clary G" first="Guilhem" last="Clary">Guilhem Clary</name><affiliation wicri:level="4"><nlm:affiliation>Plate-forme protéomique 3P5, Université Paris Descartes, Sorbonne Paris Cité, France; Inserm U1016, Institut Cochin, Paris, France; CNRS, UMR8104, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Plate-forme protéomique 3P5, Université Paris Descartes, Sorbonne Paris Cité, France; Inserm U1016, Institut Cochin, Paris, France; CNRS, UMR8104, Paris</wicri:regionArea><placeName><region type="region">Île-de-France</region><region type="old region">Île-de-France</region><settlement type="city">Paris</settlement></placeName><orgName type="university">Université Paris-Descartes</orgName></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation wicri:level="3"><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Gif-sur-Yvette</settlement></placeName></affiliation></author><author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name><affiliation wicri:level="3"><nlm:affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette, France. Electronic address: virginie.redeker@lebs.cnrs-gif.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Gif-sur-Yvette</settlement></placeName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line, Tumor</term><term>Humans</term><term>Lewy Bodies (chemistry)</term><term>Neuroblastoma (pathology)</term><term>Protein Processing, Post-Translational</term><term>Proteome</term><term>Two-Dimensional Difference Gel Electrophoresis</term><term>alpha-Synuclein (chemistry)</term><term>alpha-Synuclein (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Proteome</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Lewy Bodies</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neuroblastoma</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Humans</term><term>Protein Processing, Post-Translational</term><term>Two-Dimensional Difference Gel Electrophoresis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">α-Synuclein (α-Syn) fibrils are the main constituent of Lewy bodies and a neuropathological hallmark of Parkinson's disease (PD). The propagation of α-Syn assemblies from cell to cell suggests that they are involved in PD progression. We previously showed that α-Syn fibrils are toxic because of their ability to bind and permeabilize cell membranes. Here, we document the cellular response in terms of proteome changes of SH-SY5Y cells exposed to exogenous α-Syn fibrils.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26468903</PMID><DateCreated><Year>2015</Year><Month>12</Month><Day>07</Day></DateCreated><DateCompleted><Year>2016</Year><Month>05</Month><Day>02</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1860</Volume><Issue>1 Pt A</Issue><PubDate><Year>2016</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation></Journal><ArticleTitle>Cellular response of human neuroblastoma cells to α-synuclein fibrils, the main constituent of Lewy bodies.</ArticleTitle><Pagination><MedlinePgn>8-19</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2015.10.007</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(15)00271-8</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">α-Synuclein (α-Syn) fibrils are the main constituent of Lewy bodies and a neuropathological hallmark of Parkinson's disease (PD). The propagation of α-Syn assemblies from cell to cell suggests that they are involved in PD progression. We previously showed that α-Syn fibrils are toxic because of their ability to bind and permeabilize cell membranes. Here, we document the cellular response in terms of proteome changes of SH-SY5Y cells exposed to exogenous α-Syn fibrils.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">We compare the proteomes of cells of neuronal origin exposed or not either to oligomeric or fibrillar α-Syn using two dimensional differential in-gel electrophoresis (2D-DIGE) and mass spectrometry.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Only α-Syn fibrils induce significant changes in the proteome of SH-SY5Y cells. In addition to proteins associated to apoptosis and toxicity, or proteins previously linked to neurodegenerative diseases, we report an overexpression of proteins involved in intracellular vesicle trafficking. We also report a remarkable increase in fibrillar α-Syn heterogeneity, mainly due to C-terminal truncations.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Our results show that cells of neuronal origin adapt their proteome to exogenous α-Syn fibrils and actively modify those assemblies.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE" NlmCategory="CONCLUSIONS">Cells of neuronal origin adapt their proteome to exogenous toxic α-Syn fibrils and actively modify those assemblies. Our results bring insights into the cellular response and clearance events the cells implement to face the propagation of α-Syn assemblies associated to pathology.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pieri</LastName><ForeName>Laura</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chafey</LastName><ForeName>Philippe</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Plate-forme protéomique 3P5, Université Paris Descartes, Sorbonne Paris Cité, France; Inserm U1016, Institut Cochin, Paris, France; CNRS, UMR8104, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Le Gall</LastName><ForeName>Morgane</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Plate-forme protéomique 3P5, Université Paris Descartes, Sorbonne Paris Cité, France; Inserm U1016, Institut Cochin, Paris, France; CNRS, UMR8104, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Clary</LastName><ForeName>Guilhem</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Plate-forme protéomique 3P5, Université Paris Descartes, Sorbonne Paris Cité, France; Inserm U1016, Institut Cochin, Paris, France; CNRS, UMR8104, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Melki</LastName><ForeName>Ronald</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Redeker</LastName><ForeName>Virginie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience, CNRS, Université Paris-Saclay, Avenue de la terrasse, 91190 Gif-sur-Yvette, France. Electronic address: virginie.redeker@lebs.cnrs-gif.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>10</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016631" MajorTopicYN="N">Lewy Bodies</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009447" MajorTopicYN="N">Neuroblastoma</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057825" MajorTopicYN="N">Two-Dimensional Difference Gel Electrophoresis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">2D-DIGE</Keyword><Keyword MajorTopicYN="N">Parkinson's Disease</Keyword><Keyword MajorTopicYN="N">Post-translational modifications</Keyword><Keyword MajorTopicYN="N">Proteomic</Keyword><Keyword MajorTopicYN="N">α-Synuclein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>06</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>09</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>10</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>10</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>10</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>5</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26468903</ArticleId><ArticleId IdType="pii">S0304-4165(15)00271-8</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2015.10.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li><li>Paris</li></settlement><orgName><li>Université Paris-Descartes</li></orgName></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Pieri, Laura" sort="Pieri, Laura" uniqKey="Pieri L" first="Laura" last="Pieri">Laura Pieri</name></region><name sortKey="Chafey, Philippe" sort="Chafey, Philippe" uniqKey="Chafey P" first="Philippe" last="Chafey">Philippe Chafey</name><name sortKey="Clary, Guilhem" sort="Clary, Guilhem" uniqKey="Clary G" first="Guilhem" last="Clary">Guilhem Clary</name><name sortKey="Le Gall, Morgane" sort="Le Gall, Morgane" uniqKey="Le Gall M" first="Morgane" last="Le Gall">Morgane Le Gall</name><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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