Causes and Consequences of Cysteine S-Glutathionylation

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...

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Published inThe Journal of biological chemistry Vol. 288; no. 37; pp. 26497 - 26504
Main Authors Grek, Christina L., Zhang, Jie, Manevich, Yefim, Townsend, Danyelle M., Tew, Kenneth D.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 13.09.2013
American Society for Biochemistry and Molecular Biology
Subjects
Animals
Cysteine - metabolism
Cysteine-mediated Cross-linking
Gene Expression Regulation, Enzymologic
Glutaredoxins - metabolism
Glutathione
Glutathione - metabolism
Glutathione S-Transferase
Glutathione Transferase - metabolism
Glutathionylation
Humans
Kinase Signaling
Minireviews
Nitric Oxide
Nitric Oxide - metabolism
Nitrogen - metabolism
Nitrosylation
Oxidation-Reduction
Oxidative Stress
Peroxidases
Peroxidases - metabolism
Peroxiredoxin
Protein Processing, Post-Translational
Reactive Oxygen Species - metabolism
Serpin
Serpins - metabolism
Sulfhydryl Compounds - metabolism
Cysteine-mediated Cross-linking
Peroxiredoxin
Serpin
Kinase Signaling
Peroxidases
Glutathione S-Transferase
Nitrosylation
Glutathionylation
Nitric Oxide
Glutathione
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Summary: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.
Bibliography:ObjectType-Article-2
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.R113.461368