Tau enhances α-synuclein aggregation and toxicity in cellular models of synucleinopathy.

ABSTRACT:

Background

The simultaneous accumulation of different misfolded proteins in the central nervous system is a common feature in many neurodegenerative diseases. In most cases, co-occurrence of abnormal deposited proteins is observed in different brain regions and cell populations, but, in some instances, the proteins can be found in the same cellular aggregates. Co-occurrence of tau and α-synuclein (α-syn) aggregates has been described in neurodegenerative disorders with primary deposition of α-syn, such as Parkinson's disease and dementia with Lewy bodies. Although it is known that tau and α-syn have pathological synergistic effects on their mutual fibrillization, the underlying biological effects remain unclear.

Methodology/principal findings

We used different cell models of

SUBMITTER: Badiola N 

PROVIDER: S-EPMC3200341 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature