Dopamine induces the accumulation of insoluble prion protein and affects autophagic flux.

ABSTRACT: Accumulation of protein aggregates is a histopathological hallmark of several neurodegenerative diseases, but in most cases the aggregation occurs without defined mutations or clinical histories, suggesting that certain endogenous metabolites can promote aggregation of specific proteins. One example that supports this hypothesis is dopamine and its metabolites. Dopamine metabolism generates several oxidative metabolites that induce aggregation of α-synuclein, and represents the main etiology of Parkinson's diseases. Because dopamine and its metabolites are unstable and can be highly reactive, we investigated whether these molecules can also affect other proteins that are prone to aggregate, such as cellular prion protein (PrP(C)). In this study, we showed that dopamine treatment of neurona

SUBMITTER: da Luz MH 

PROVIDER: S-EPMC4313710 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature