Regulation of protein function by glutathionylation

被引：218

作者：

Ghezzi, P ^{[1
]}

机构：

[1] Mario Negri Inst Pharmacol Res, I-20157 Milan, Italy

来源：

FREE RADICAL RESEARCH | 2005年 / 39卷 / 06期

关键词：

glutathione; cysteines; thiol-disulfide exchange; dethiolating agent;

D O I：

10.1080/10715760500072172

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 main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive oxygen scavenger. However, in the context of redox regulation, the ratio between GSH and its oxidized form (GSSG) determines the redox state of redox-sensitive cysteines in some proteins and, thus, acts as a signaling system. While GSH/GSSG can catalyze oxido-reduction of intra- and inter-chain disulfides by thiol-disulfide exchange, this review focuses on the formation of mixed disulfides between glutathione and proteins, also known as glutathionylation. The review discusses the regulatory role of this post-translational modification and the role of protein disulfide oxidoreductases (thioredoxin/thioredoxin reductase, glutaredoxin, protein disulfide isomerase) in the reversibility of this process.

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收藏

页码：573 / 580

页数：8

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