Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

被引：82

作者：

Kalinina, Elena ^{[1
]}

Novichkova, Maria ^{[1
]}

机构：

[1] RUDN Univ, Peoples Friendship Univ Russia, TT Berezov Dept Biochem, 6 Miklukho Maklaya St, Moscow 117198, Russia

来源：

MOLECULES | 2021年 / 26卷 / 02期

关键词：

S-glutathionylation; S-nitrosylation; GSH; nitrosoglutathione; redox-regulation; NITRIC-OXIDE;

D O I：

10.3390/molecules26020435

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：

S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the functional activity of proteins and intracellular processes. Connecting link and "switch" functions between S-glutathionylation and S-nitrosylation may be performed by GSNO, the generation of which depends on the GSH content, the GSH/GSSG ratio, and the cellular redox state. An important role in the regulation of these processes is played by Trx family enzymes (Trx, Grx, PDI), the activity of which is determined by the cellular redox status and depends on the GSH/GSSG ratio. In this review, we analyze data concerning the role of GSH/GSSG in the modulation of S-glutathionylation and S-nitrosylation and their relationship for the maintenance of cell viability.

引用

页数：19

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