Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation
T.T. Berezov Department of Biochemistry, Peoples’ Friendship University of Russia (RUDN University), 6 Miklukho-Maklaya Street, 117198 Moscow, Russia
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Molecules 2021, 26(2), 435; https://doi.org/10.3390/molecules26020435
Received: 12 November 2020
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Revised: 8 January 2021
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Accepted: 12 January 2021
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Published: 15 January 2021
(This article belongs to the Special Issue Glutathione: Chemistry and Biochemistry)
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.
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Keywords:
S-glutathionylation; S-nitrosylation; GSH; nitrosoglutathione; redox-regulation
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MDPI and ACS Style
Kalinina, E.; Novichkova, M. Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation. Molecules 2021, 26, 435. https://doi.org/10.3390/molecules26020435
AMA Style
Kalinina E, Novichkova M. Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation. Molecules. 2021; 26(2):435. https://doi.org/10.3390/molecules26020435
Chicago/Turabian StyleKalinina, Elena, and Maria Novichkova. 2021. "Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation" Molecules 26, no. 2: 435. https://doi.org/10.3390/molecules26020435
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