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

FEBS Letters

Fink, Anthony L¹  Uversky, Vladimir N¹  Yamin, Ghiam¹ 

[1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA

关键词: Parkinson's disease;    α-Synuclein;    Oxidative stress;    Nitration;    Fibrillation;   

DOI  :  10.1016/S0014-5793(03)00367-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The aggregation of α-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 α-synuclein to fibrillate in vitro. Fibril formation of α-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 α-synuclein led to inhibition of fibrillation of non-modified α-synuclein. These observations suggest that nitration of soluble α-synuclein may be a protective factor in PD, rather than a causative one.

【 授权许可】

Unknown