[Is Parkinson's disease a prion disease?].
Identifieur interne : 000253 ( PubMed/Curation ); précédent : 000252; suivant : 000254[Is Parkinson's disease a prion disease?].
Auteurs : J-P Brandel [France] ; A-G Corbillé [France] ; P. Derkinderen [France] ; S. Haïk [France]Source :
- Revue neurologique [ 0035-3787 ] ; 2015.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Prions, Synucleins.
- etiology : Parkinson Disease.
- Humans, Prion Diseases.
Abstract
The accumulation of a specific protein in aggregated form is a common phenomenon in human neurodegenerative diseases. In Parkinson's disease, this protein is α-synuclein which is a neuronal protein of 143 amino acids. With a monomeric conformation in solution, it also has a natural capacity to aggregate into amyloid structures (dimers, oligomers, fibrils and Lewy bodies or neurites). It therefore fulfils the characteristics of a prion protein (different conformations, seeding and spreading). In vitro and in vivo experimental evidence in transgenic and wild animals indicates a prion-like propagation of Parkinson's disease. The sequential and predictive distribution of α-synuclein demonstrated by Braak et al. and its correlation with non-motor signs are consistent with the prion-like progression. Although the triggering factor causing the misfolding and aggregation of the target protein is unknown, Parkinson's disease is a highly relevant model for the study of these mechanisms and also to test specific treatments targeting the assemblies of α-synuclein and propagation from pre-motor phase of the disease. Despite this prion-like progression, there is currently no argument indicating a risk of human transmission of Parkinson's disease.
DOI: 10.1016/j.neurol.2015.10.005
PubMed: 26563663
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Derkinderen</name><affiliation wicri:level="1"><nlm:affiliation>Département de neurologie, CHU de Nantes, 44093 Nantes, France; Inserm, U913, 44093 Nantes, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Département de neurologie, CHU de Nantes, 44093 Nantes, France; Inserm, U913, 44093 Nantes</wicri:regionArea></affiliation></author><author><name sortKey="Haik, S" sort="Haik, S" uniqKey="Haik S" first="S" last="Haïk">S. Haïk</name><affiliation wicri:level="1"><nlm:affiliation>Inserm U 1127, CNRS UMR 7225, Sorbonne universités, UPMC University Paris 06 UMR S 1127, institut du cerveau et de la mœlle épinière, ICM, 75013 Paris, France; Cellule nationale de référence des maladies de Creutzfeldt-Jakob, groupe hospitalier Pitié-Salpêtrière, AP-HP, 47-83, boulevard de l'Hôpital, 75651 Paris cedex 13, France; Centre national de référence des agents transmissibles non conventionnels, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm U 1127, CNRS UMR 7225, Sorbonne universités, UPMC University Paris 06 UMR S 1127, institut du cerveau et de la mœlle épinière, ICM, 75013 Paris, France; Cellule nationale de référence des maladies de Creutzfeldt-Jakob, groupe hospitalier Pitié-Salpêtrière, AP-HP, 47-83, boulevard de l'Hôpital, 75651 Paris cedex 13, France; Centre national de référence des agents transmissibles non conventionnels, 75013 Paris</wicri:regionArea></affiliation></author></analytic><series><title level="j">Revue neurologique</title><idno type="ISSN">0035-3787</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Humans</term><term>Parkinson Disease (etiology)</term><term>Prion Diseases</term><term>Prions (metabolism)</term><term>Synucleins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Prions</term><term>Synucleins</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Prion Diseases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The accumulation of a specific protein in aggregated form is a common phenomenon in human neurodegenerative diseases. In Parkinson's disease, this protein is α-synuclein which is a neuronal protein of 143 amino acids. With a monomeric conformation in solution, it also has a natural capacity to aggregate into amyloid structures (dimers, oligomers, fibrils and Lewy bodies or neurites). It therefore fulfils the characteristics of a prion protein (different conformations, seeding and spreading). In vitro and in vivo experimental evidence in transgenic and wild animals indicates a prion-like propagation of Parkinson's disease. The sequential and predictive distribution of α-synuclein demonstrated by Braak et al. and its correlation with non-motor signs are consistent with the prion-like progression. Although the triggering factor causing the misfolding and aggregation of the target protein is unknown, Parkinson's disease is a highly relevant model for the study of these mechanisms and also to test specific treatments targeting the assemblies of α-synuclein and propagation from pre-motor phase of the disease. Despite this prion-like progression, there is currently no argument indicating a risk of human transmission of Parkinson's disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26563663</PMID><DateCreated><Year>2015</Year><Month>12</Month><Day>15</Day></DateCreated><DateCompleted><Year>2016</Year><Month>09</Month><Day>19</Day></DateCompleted><DateRevised><Year>2015</Year><Month>12</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0035-3787</ISSN><JournalIssue CitedMedium="Internet"><Volume>171</Volume><Issue>12</Issue><PubDate><Year>2015</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Revue neurologique</Title><ISOAbbreviation>Rev. Neurol. (Paris)</ISOAbbreviation></Journal><ArticleTitle>[Is Parkinson's disease a prion disease?].</ArticleTitle><Pagination><MedlinePgn>812-24</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.neurol.2015.10.005</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0035-3787(15)00876-0</ELocationID><Abstract><AbstractText>The accumulation of a specific protein in aggregated form is a common phenomenon in human neurodegenerative diseases. In Parkinson's disease, this protein is α-synuclein which is a neuronal protein of 143 amino acids. With a monomeric conformation in solution, it also has a natural capacity to aggregate into amyloid structures (dimers, oligomers, fibrils and Lewy bodies or neurites). It therefore fulfils the characteristics of a prion protein (different conformations, seeding and spreading). In vitro and in vivo experimental evidence in transgenic and wild animals indicates a prion-like propagation of Parkinson's disease. The sequential and predictive distribution of α-synuclein demonstrated by Braak et al. and its correlation with non-motor signs are consistent with the prion-like progression. Although the triggering factor causing the misfolding and aggregation of the target protein is unknown, Parkinson's disease is a highly relevant model for the study of these mechanisms and also to test specific treatments targeting the assemblies of α-synuclein and propagation from pre-motor phase of the disease. Despite this prion-like progression, there is currently no argument indicating a risk of human transmission of Parkinson's disease.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Brandel</LastName><ForeName>J-P</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Inserm U 1127, CNRS UMR 7225, Sorbonne universités, UPMC University Paris 06 UMR S 1127, institut du cerveau et de la mœlle épinière, ICM, 75013 Paris, France; Cellule nationale de référence des maladies de Creutzfeldt-Jakob, groupe hospitalier Pitié-Salpêtrière, AP-HP, 47-83, boulevard de l'Hôpital, 75651 Paris cedex 13, France; Centre national de référence des agents transmissibles non conventionnels, 75013 Paris, France; Unité James-Parkinson, Fondation ophtalmologique Rothschild, 75019 Paris, France. Electronic address: jean-philippe.brandel@aphp.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corbillé</LastName><ForeName>A-G</ForeName><Initials>AG</Initials><AffiliationInfo><Affiliation>Département de neurologie, CHU de Nantes, 44093 Nantes, France; Inserm, U913, 44093 Nantes, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Derkinderen</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Département de neurologie, CHU de Nantes, 44093 Nantes, France; Inserm, U913, 44093 Nantes, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haïk</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Inserm U 1127, CNRS UMR 7225, Sorbonne universités, UPMC University Paris 06 UMR S 1127, institut du cerveau et de la mœlle épinière, ICM, 75013 Paris, France; Cellule nationale de référence des maladies de Creutzfeldt-Jakob, groupe hospitalier Pitié-Salpêtrière, AP-HP, 47-83, boulevard de l'Hôpital, 75651 Paris cedex 13, France; Centre national de référence des agents transmissibles non conventionnels, 75013 Paris, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>fre</Language><PublicationTypeList><PublicationType UI="D004740">English Abstract</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><VernacularTitle>La maladie de Parkinson est-elle une maladie à prion?</VernacularTitle><ArticleDate DateType="Electronic"><Year>2015</Year><Month>11</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Rev Neurol (Paris)</MedlineTA><NlmUniqueID>2984779R</NlmUniqueID><ISSNLinking>0035-3787</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051843">Synucleins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000209" MajorTopicYN="Y">etiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017096" MajorTopicYN="Y">Prion Diseases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011328" MajorTopicYN="N">Prions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051843" MajorTopicYN="N">Synucleins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Maladie de Parkinson</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">Prion-like</Keyword><Keyword MajorTopicYN="N">α-Synuclein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>09</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>10</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>10</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>11</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>11</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>9</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26563663</ArticleId><ArticleId IdType="pii">S0035-3787(15)00876-0</ArticleId><ArticleId IdType="doi">10.1016/j.neurol.2015.10.005</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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