Accession Number:

ADA467856

Title:

Mechanisms of Alpha-synuclein Aggregation and Toxicity

Descriptive Note:

Annual rept. 1 Sep 2003-31 Aug 2004

Corporate Author:

BOSTON UNIV MA

Personal Author(s):

Report Date:

2004-09-01

Pagination or Media Count:

126.0

Abstract:

Alpha-synuclein is a protein implicated in the pathophysiology of Parkinsons disease. The purpose of this proposal is to study the regulation of synuclein aggregation by metals, the interaction of synuclein with other proteins associated with its pathophysiology and the effects of aggregated alpha-synuclein on the function of neuronal mitochondria. During the current year, we have identified several novel interactions of Alpha-synuclein, including binding to the proteasome and selective inhibition of Mitochondrial complex 1. We have also identified a number of novel pathological changes associated with alpha-synuclein aggregation, including phosphorylation of tau protein and up-regulation of DJ-1 protein. Finally, our studies identify novel chemical and molecular strategies for inhibiting toxicity induced by aggregated alpha-synuclein.

Subject Categories:

  • Biochemistry
  • Anatomy and Physiology
  • Medicine and Medical Research
  • Toxicology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE