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Reduced anti-oxidative stress activities of DJ-1 mutants found in Parkinson's disease patients.

Abstract：

:DJ-1 is a multi-functional protein that plays roles in transcriptional regulation and anti-oxidative stress, and loss of its function is thought to result in onset of Parkinson's disease. We have previously reported that L166P, a mutant DJ-1 found in Parkinson's disease patients, had no activity to prevent hydrogen peroxide (H2O2)-induced cell death. In this study, we analyzed other mutants of DJ-1 found in Parkinson's disease patients, including M26I, R98Q, and D149A, as well as L166P. We first found that all of the mutants made heterodimers with wild-type DJ-1, while all of the mutants except for L166P made homodimers. We then found that M26I and L166P, both of which are derived from homozygous mutations of the DJ-1 gene, were unstable and that their stabilities were recovered, in part, in the presence of proteasome inhibitor, MG132. NIH3T3 cell lines stably expressing these mutants of DJ-1 showed that cell lines of L166P and C106S, a mutant for protease activity (-) of DJ-1, had no activity to scavenge even endogenously producing reactive oxygen species. These cell lines also showed that all of the mutants had reduced activities to eliminate exogenously added H2O2 and that these activities, except for that of D149A, were parallel to those preventing H2O2-induced cell death.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Takahashi-Niki K,Niki T,Taira T,Iguchi-Ariga SM,Ariga H

doi

10.1016/j.bbrc.2004.05.187

subject

Has Abstract

pub_date

2004-07-23 00:00:00

pages

389-97

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X04012094

journal_volume

320

pub_type

杂志文章

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