Article

The accumulation of a specific protein in aggregated form is a common phenomenon
in human neurodegenerative diseases. In Parkinson's disease, this protein is
alpha-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 alpha-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 alpha-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.
CI - Copyright (c) 2015 Elsevier Masson SAS. All rights reserved.

Langue : FRANCAIS