title: [Is Parkinson's disease a prion disease?].
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.
authors.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.
authors.forename: J-P
authors.initials: JP
authors.lastname: Brandel
authors.affiliation: Département de neurologie, CHU de Nantes, 44093 Nantes, France; Inserm, U913, 44093 Nantes, France.
authors.forename: A-G
authors.initials: AG
authors.lastname: Corbillé
authors.affiliation: Département de neurologie, CHU de Nantes, 44093 Nantes, France; Inserm, U913, 44093 Nantes, France.
authors.forename: P
authors.initials: P
authors.lastname: Derkinderen
authors.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.
authors.forename: S
authors.initials: S
authors.lastname: Haïk
mesh_terms: D006801:Humans; D010300:Parkinson Disease / Q000209:etiology*; D017096:Prion Diseases; D011328:Prions / Q000378:metabolism; D051843:Synucleins / Q000378:metabolism
chemical_list: D011328:Prions; D051843:Synucleins
keywords: Maladie de Parkinson; Parkinson's disease; Prion-like; α-Synuclein