Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity.

ABSTRACT: Synucleinopathies are a group of progressive disorders characterized by the abnormal aggregation and accumulation of α-synuclein (aSyn), an abundant neuronal protein that can adopt different conformations and biological properties. Recently, aSyn pathology was shown to spread between neurons in a prion-like manner. Proteins like aSyn that exhibit self-propagating capacity appear to be able to adopt different stable conformational states, known as protein strains, which can be modulated both by environmental and by protein-intrinsic factors. Here, we analyzed these factors and found that the unique combination of the neurodegeneration-related metal copper and the pathological H50Q aSyn mutation induces a significant alteration in the aggregation properties of aSyn. We compared the aggregati

SUBMITTER: Villar-Pique A 

PROVIDER: S-EPMC5081623 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature