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 in | The Journal of biological chemistry Vol. 288; no. 37; pp. 26497 - 26504 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
13.09.2013
American Society for Biochemistry and Molecular Biology |
| Subjects | |
| Online Access | Get full text |
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| 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. |
|---|---|
| AbstractList | 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. 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. |
| Author | Tew, Kenneth D. Grek, Christina L. Townsend, Danyelle M. Zhang, Jie Manevich, Yefim |
| Author_xml | – sequence: 1 givenname: Christina L. surname: Grek fullname: Grek, Christina L. organization: Departments of Cell and Molecular Pharmacology and Experimental Therapeutics and – sequence: 2 givenname: Jie surname: Zhang fullname: Zhang, Jie organization: Departments of Cell and Molecular Pharmacology and Experimental Therapeutics and – sequence: 3 givenname: Yefim surname: Manevich fullname: Manevich, Yefim organization: Departments of Cell and Molecular Pharmacology and Experimental Therapeutics and – sequence: 4 givenname: Danyelle M. surname: Townsend fullname: Townsend, Danyelle M. organization: Departments of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina 29425-1410 – sequence: 5 givenname: Kenneth D. surname: Tew fullname: Tew, Kenneth D. email: tewk@musc.edu organization: Departments of Cell and Molecular Pharmacology and Experimental Therapeutics and |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23861399$$D View this record in MEDLINE/PubMed |
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| Keywords | Cysteine-mediated Cross-linking Peroxiredoxin Serpin Kinase Signaling Peroxidases Glutathione S-Transferase Nitrosylation Glutathionylation Nitric Oxide Glutathione |
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| PublicationCentury | 2000 |
| PublicationDate | 2013-09-13 |
| PublicationDateYYYYMMDD | 2013-09-13 |
| PublicationDate_xml | – month: 09 year: 2013 text: 2013-09-13 day: 13 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: 9650 Rockville Pike, Bethesda, MD 20814, U.S.A |
| PublicationTitle | The Journal of biological chemistry |
| PublicationTitleAlternate | J Biol Chem |
| PublicationYear | 2013 |
| Publisher | Elsevier Inc American Society for Biochemistry and Molecular Biology |
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| SubjectTerms | 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 |
| Title | Causes and Consequences of Cysteine S-Glutathionylation |
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