T.T. Berezov Department of Biochemistry, Peoples' Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, 117198 Moscow, Russia.
Molecules. 2021 Jan 15;26(2):435. doi: 10.3390/molecules26020435.
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.
S-谷胱甘肽化和 S-亚硝化是蛋白质半胱氨酸巯基上的两种可逆翻译后修饰，在生理条件下以及氧化/硝化应激下，细胞内会自发且酶促地发生这两种修饰。它们对于蛋白质功能活性和细胞内过程的调节非常重要。S-谷胱甘肽化和 S-亚硝化之间的连接和“开关”功能可能由 GSNO 执行，其生成取决于 GSH 含量、GSH/GSSG 比和细胞内氧化还原状态。Trx 家族酶（Trx、Grx、PDI）在这些过程的调节中起着重要作用，其活性由细胞氧化还原状态决定，并取决于 GSH/GSSG 比。在这篇综述中，我们分析了有关 GSH/GSSG 在调节 S-谷胱甘肽化和 S-亚硝化及其关系以维持细胞活力方面的作用的数据。
