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

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.

Авторы
Журнал
Издательство
MDPI AG
Номер выпуска
2
Язык
Английский
Статус
Опубликовано
Том
26
Год
2021
Организации
  • 1 T.T. Berezov Department of Biochemistry, Peoples' Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya StreetMoscow 117198, Russian Federation
Ключевые слова
GSH; nitrosoglutathione; redox-regulation; S-glutathionylation; S-nitrosylation
Дата создания
20.04.2021
Дата изменения
20.04.2021
Постоянная ссылка
https://repository.rudn.ru/ru/records/article/record/72186/
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