On the role of the cellular prion protein in the uptake and signaling of pathological aggregates in neurodegenerative diseases.

ABSTRACT: Neurodegenerative disorders are associated with intra- or extra-cellular deposition of aggregates of misfolded insoluble proteins. These deposits composed of tau, amyloid-β or α-synuclein spread from cell to cell, in a prion-like manner. Novel evidence suggests that the circulating soluble oligomeric species of these misfolded proteins could play a major role in pathology, while insoluble aggregates would represent their protective less toxic counterparts. Recent convincing data support the proposition that the cellular prion protein, PrP^C, act as a toxicity-inducing receptor for amyloid-β oligomers. As a consequence, several studies focused their investigations to the role played by PrP^C in binding other protein aggregates, such as tau and α-synuclein, for its possib

SUBMITTER: Legname G 

PROVIDER: S-EPMC7757855 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature