New roles of glycosaminoglycans in α-synuclein aggregation in a cellular model of Parkinson disease.
Identifieur interne : 000410 ( PubMed/Corpus ); précédent : 000409; suivant : 000411New roles of glycosaminoglycans in α-synuclein aggregation in a cellular model of Parkinson disease.
Auteurs : Sonia Lehri-Boufala ; Mohand-Ouidir Ouidja ; Véronique Barbier-Chassefière ; Emilie Hénault ; Rita Raisman-Vozari ; Laure Garrigue-Antar ; Dulce Papy-Garcia ; Christophe MorinSource :
- PloS one [ 1932-6203 ] ; 2015.
English descriptors
- KwdEn :
- 1-Methyl-4-phenylpyridinium (pharmacology), Amino Acid Sequence, Apoptosis (drug effects), Cathepsin D (metabolism), Cell Line, Tumor, Glycosaminoglycans (biosynthesis), Glycosaminoglycans (metabolism), Humans, Intracellular Space (drug effects), Intracellular Space (metabolism), Parkinson Disease (metabolism), Parkinson Disease (pathology), Protein Aggregates (drug effects), Protein Transport (drug effects), Proteolysis (drug effects), alpha-Synuclein (chemistry), alpha-Synuclein (metabolism).
- MESH :
- chemical , biosynthesis : Glycosaminoglycans.
- chemical , chemistry : alpha-Synuclein.
- chemical , drug effects : Protein Aggregates.
- chemical , metabolism : Cathepsin D, Glycosaminoglycans, alpha-Synuclein.
- chemical , pharmacology : 1-Methyl-4-phenylpyridinium.
- drug effects : Apoptosis, Intracellular Space, Protein Transport, Proteolysis.
- metabolism : Intracellular Space, Parkinson Disease.
- pathology : Parkinson Disease.
- Amino Acid Sequence, Cell Line, Tumor, Humans.
Abstract
The causes of Parkinson disease (PD) remain mysterious, although some evidence supports mitochondrial dysfunctions and α-synuclein accumulation in Lewy bodies as major events. The abnormal accumulation of α-synuclein has been associated with a deficiency in the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Cathepsin D (cathD), the major lysosomal protease responsible of α-synuclein degradation was described to be up-regulated in PD model. As glycosaminoglycans (GAGs) regulate cathD activity, and have been recently suggested to participate in PD physiopathology, we investigated their role in α-synuclein accumulation by their intracellular regulation of cathD activity. In a classical neuroblastoma cell model of PD induced by MPP+, the genetic expression of GAGs-biosynthetic enzymes was modified, leading to an increase of GAGs amounts whereas intracellular level of α-synuclein increased. The absence of sulfated GAGs increased intracellular cathD activity and limited α-synuclein accumulation. GAGs effects on cathD further suggested that specific sequences or sulfation patterns could be responsible for this regulation. The present study identifies, for the first time, GAGs as new regulators of the lysosome degradation pathway, regulating cathD activity and affecting two main biological processes, α-synuclein aggregation and apoptosis. Finally, this opens new insights into intracellular GAGs functions and new fields of investigation for glycobiological approaches in PD and neurobiology.
DOI: 10.1371/journal.pone.0116641
PubMed: 25617759
Links to Exploration step
pubmed:25617759Le document en format XML
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CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</nlm:affiliation></affiliation></author><author><name sortKey="Raisman Vozari, Rita" sort="Raisman Vozari, Rita" uniqKey="Raisman Vozari R" first="Rita" last="Raisman-Vozari">Rita Raisman-Vozari</name><affiliation><nlm:affiliation>CNRS UMR 7225, Hôpital de la Salpêtrière-Bâtiment, ICM (Centre de Recherche de l'Institut du Cerveau et de la Moelle épinière), CRICM, Thérapeutique Expérimentale de la Neurodégénérescence, Université Pierre et Marie Curie, UPMC, 75651, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Garrigue Antar, Laure" sort="Garrigue Antar, Laure" uniqKey="Garrigue Antar L" first="Laure" last="Garrigue-Antar">Laure Garrigue-Antar</name><affiliation><nlm:affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</nlm:affiliation></affiliation></author><author><name sortKey="Papy Garcia, Dulce" sort="Papy Garcia, Dulce" uniqKey="Papy Garcia D" first="Dulce" last="Papy-Garcia">Dulce Papy-Garcia</name><affiliation><nlm:affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</nlm:affiliation></affiliation></author><author><name sortKey="Morin, Christophe" sort="Morin, Christophe" uniqKey="Morin C" first="Christophe" last="Morin">Christophe Morin</name><affiliation><nlm:affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1-Methyl-4-phenylpyridinium (pharmacology)</term><term>Amino Acid Sequence</term><term>Apoptosis (drug 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qualifier="metabolism" xml:lang="en"><term>Cathepsin D</term><term>Glycosaminoglycans</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>1-Methyl-4-phenylpyridinium</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term><term>Intracellular Space</term><term>Protein Transport</term><term>Proteolysis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Space</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Line, Tumor</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The causes of Parkinson disease (PD) remain mysterious, although some evidence supports mitochondrial dysfunctions and α-synuclein accumulation in Lewy bodies as major events. The abnormal accumulation of α-synuclein has been associated with a deficiency in the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Cathepsin D (cathD), the major lysosomal protease responsible of α-synuclein degradation was described to be up-regulated in PD model. As glycosaminoglycans (GAGs) regulate cathD activity, and have been recently suggested to participate in PD physiopathology, we investigated their role in α-synuclein accumulation by their intracellular regulation of cathD activity. In a classical neuroblastoma cell model of PD induced by MPP+, the genetic expression of GAGs-biosynthetic enzymes was modified, leading to an increase of GAGs amounts whereas intracellular level of α-synuclein increased. The absence of sulfated GAGs increased intracellular cathD activity and limited α-synuclein accumulation. GAGs effects on cathD further suggested that specific sequences or sulfation patterns could be responsible for this regulation. The present study identifies, for the first time, GAGs as new regulators of the lysosome degradation pathway, regulating cathD activity and affecting two main biological processes, α-synuclein aggregation and apoptosis. Finally, this opens new insights into intracellular GAGs functions and new fields of investigation for glycobiological approaches in PD and neurobiology.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25617759</PMID><DateCreated><Year>2015</Year><Month>01</Month><Day>25</Day></DateCreated><DateCompleted><Year>2016</Year><Month>01</Month><Day>05</Day></DateCompleted><DateRevised><Year>2015</Year><Month>01</Month><Day>31</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>1</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>New roles of glycosaminoglycans in α-synuclein aggregation in a cellular model of Parkinson disease.</ArticleTitle><Pagination><MedlinePgn>e0116641</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0116641</ELocationID><Abstract><AbstractText>The causes of Parkinson disease (PD) remain mysterious, although some evidence supports mitochondrial dysfunctions and α-synuclein accumulation in Lewy bodies as major events. The abnormal accumulation of α-synuclein has been associated with a deficiency in the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Cathepsin D (cathD), the major lysosomal protease responsible of α-synuclein degradation was described to be up-regulated in PD model. As glycosaminoglycans (GAGs) regulate cathD activity, and have been recently suggested to participate in PD physiopathology, we investigated their role in α-synuclein accumulation by their intracellular regulation of cathD activity. In a classical neuroblastoma cell model of PD induced by MPP+, the genetic expression of GAGs-biosynthetic enzymes was modified, leading to an increase of GAGs amounts whereas intracellular level of α-synuclein increased. The absence of sulfated GAGs increased intracellular cathD activity and limited α-synuclein accumulation. GAGs effects on cathD further suggested that specific sequences or sulfation patterns could be responsible for this regulation. The present study identifies, for the first time, GAGs as new regulators of the lysosome degradation pathway, regulating cathD activity and affecting two main biological processes, α-synuclein aggregation and apoptosis. Finally, this opens new insights into intracellular GAGs functions and new fields of investigation for glycobiological approaches in PD and neurobiology.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lehri-Boufala</LastName><ForeName>Sonia</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ouidja</LastName><ForeName>Mohand-Ouidir</ForeName><Initials>MO</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barbier-Chassefière</LastName><ForeName>Véronique</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hénault</LastName><ForeName>Emilie</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Raisman-Vozari</LastName><ForeName>Rita</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>CNRS UMR 7225, Hôpital de la Salpêtrière-Bâtiment, ICM (Centre de Recherche de l'Institut du Cerveau et de la Moelle épinière), CRICM, Thérapeutique Expérimentale de la Neurodégénérescence, Université Pierre et Marie Curie, UPMC, 75651, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Garrigue-Antar</LastName><ForeName>Laure</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Papy-Garcia</LastName><ForeName>Dulce</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morin</LastName><ForeName>Christophe</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Université Paris-Est Créteil, Laboratoire CRRET-EAC CNRS 7149, 61 Avenue de Général de Gaulle, 94010, Créteil, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>01</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006025">Glycosaminoglycans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D066329">Protein Aggregates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.5</RegistryNumber><NameOfSubstance UI="D002402">Cathepsin D</NameOfSubstance></Chemical><Chemical><RegistryNumber>R865A5OY8J</RegistryNumber><NameOfSubstance UI="D015655">1-Methyl-4-phenylpyridinium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>J Cell Sci. 2005 Jan 1;118(Pt 1):253-64</RefSource><PMID Version="1">15615789</PMID></CommentsCorrections><CommentsCorrections 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effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002402" MajorTopicYN="N">Cathepsin D</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006025" MajorTopicYN="N">Glycosaminoglycans</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042541" MajorTopicYN="N">Intracellular Space</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066329" MajorTopicYN="Y">Protein Aggregates</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4305359</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>06</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>12</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>1</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>1</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>1</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25617759</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0116641</ArticleId><ArticleId IdType="pii">PONE-D-14-26635</ArticleId><ArticleId IdType="pmc">PMC4305359</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce 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