Oxidoreduction of protein thiols in redox regulation

被引：107

作者：

Ghezzi, P ^{[1
]}

机构：

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

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2005年 / 33卷

关键词：

antioxidant; disulphide; glutathione; glutathionylation; redox regulation; thiol;

D O I：

10.1042/BST0331378

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：

Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide formation, glutathionylation and S-nitrosylation). While in the past these were viewed as protein damage in the context of oxidative stress, there is growing interest in oxidoreduction of protein thiols/disulphides as a regulatory mechanism. This review discusses the evolution of the concept of redox regulation from that of oxidative stress and the redox state of protein cysteines in different cellular compartments.

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页码：1378 / 1381

页数：4

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