Nitration inhibits fibrillation of human α-synuclein in vitro by formation of soluble oligomers

被引：133

作者：

Yamin, G

Uversky, VN

Fink, AL ^{[1
]}

机构：

[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA

[2] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142290, Moscow Region, Russia

来源：

FEBS LETTERS | 2003年 / 542卷 / 1-3期

关键词：

Parkinson's disease; alpha-synuclein; oxidative stress; nitration; fibrillation;

D O I：

10.1016/S0014-5793(03)00367-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The aggregation of alpha-synuclein in dopaminergic neurons is a critical factor in the etiology of Parkinson's disease (PD). Oxidative and nitrative stress is also implicated in PD. We examined the effect of nitration on the propensity of alpha-synuclein to fibrillate in vitro. Fibril formation of a-synuclein was completely inhibited by nitration, due to the formation of stable soluble oligomers (apparently octamers). More importantly the presence of sub-stoichiometric concentrations of nitrated a-synuclein led to inhibition of fibrillation of non-modifled a-synuclein. These observations suggest that nitration of soluble a-synuclein may be a protective factor in PD, rather than a causative one. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：147 / 152

页数：6

共 46 条

[1] Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity [J].