[Is Parkinson's disease a prion disease?].
Identifieur interne : 000451 ( Main/Exploration ); précédent : 000450; suivant : 000452[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.
Descripteurs français
- mix :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Prions, Synucleins.
- etiology : Parkinson Disease.
- Humans, Prion Diseases.
- mix :
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.
Url:
DOI: 10.1016/j.neurol.2015.10.005
PubMed: 26563663
Affiliations:
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Le document en format XML
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Derkinderen</name><affiliation wicri:level="3"><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><placeName><region type="region" nuts="2">Pays de la Loire</region><settlement type="city">Nantes</settlement></placeName></affiliation></author><author><name sortKey="Haik, S" sort="Haik, S" uniqKey="Haik S" first="S" last="Haïk">S. Haïk</name><affiliation wicri:level="3"><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><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></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><keywords scheme="mix" xml:lang="en"><term>Parkinson's disease</term><term>Prion-like</term><term>α-Synuclein</term></keywords><keywords scheme="mix" xml:lang="fr"><term>Maladie de Parkinson</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><affiliations><list><country><li>France</li></country><region><li>Pays de la Loire</li><li>Île-de-France</li></region><settlement><li>Nantes</li><li>Paris</li></settlement></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Brandel, J P" sort="Brandel, J P" uniqKey="Brandel J" first="J-P" last="Brandel">J-P Brandel</name></region><name sortKey="Corbille, A G" sort="Corbille, A G" uniqKey="Corbille A" first="A-G" last="Corbillé">A-G Corbillé</name><name sortKey="Derkinderen, P" sort="Derkinderen, P" uniqKey="Derkinderen P" first="P" last="Derkinderen">P. Derkinderen</name><name sortKey="Haik, S" sort="Haik, S" uniqKey="Haik S" first="S" last="Haïk">S. Haïk</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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