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J Biol Chem. 2013 Sep 13;288(37):26497-504. doi: 10.1074/jbc.R113.461368. Epub 2013 Jul 16.

Causes and consequences of cysteine S-glutathionylation.

Author information

1
From the Departments of Cell and Molecular Pharmacology and Experimental Therapeutics and.

Abstract

Post-translational S-glutathionylation occurs through the reversible addition of a proximal donor of glutathione to thiolate anions of cysteines in target proteins, where the modification alters molecular mass, charge, and structure/function and/or prevents degradation from sulfhydryl overoxidation or proteolysis. Catalysis of both the forward (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that can also regulate certain protein functional clusters, including those involved in redox-dependent cell signaling events. For translational application, S-glutathionylated serum proteins may be useful as biomarkers in individuals (who may also have polymorphic expression of glutathione S-transferase P) exposed to agents that cause oxidative or nitrosative stress.

KEYWORDS:

Cysteine-mediated Cross-linking; Glutathione; Glutathione S-Transferase; Glutathionylation; Kinase Signaling; Nitric Oxide; Nitrosylation; Peroxidases; Peroxiredoxin; Serpin

PMID:
23861399
PMCID:
PMC3772197
DOI:
10.1074/jbc.R113.461368
[Indexed for MEDLINE]
Free PMC Article

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