Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.
- J. Mieyal, M. Gallogly, S. Qanungo, Elizabeth A. Sabens, M. Shelton
- Biology, ChemistryAntioxidants and Redox Signaling
- 1 November 2008
A large number of proteins have been identified as potentially regulated by reversible S-glutathionylation, but only a few studies have documented glutathioneylation-dependent changes in activity of specific proteins in a physiological context.
Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells*
A novel physiological relevance of actin polymerization regulated by reversible glutathionylation of the penultimate cysteine mediated by growth factor stimulation is revealed.
Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress.
- M. Gallogly, J. Mieyal
- Biology, ChemistryCurrent opinion in pharmacology (Print)
- 1 August 2007
Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation.
- M. Shelton, P. Chock, J. Mieyal
- Biology, ChemistryAntioxidants and Redox Signaling
- 10 February 2005
Specific criteria were used to evaluate current data on cellular regulation via S-glutathionylation, and actin, protein tyrosine phosphatase-1B, and Ras stand out as the best current examples for establishing this regulatory mechanism.
Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
- S. Gravina, J. Mieyal
- Biology, ChemistryBiochemistry
- 6 April 1993
Thioltransferase (glutaredoxin) appears to be specific for glutathione-containing mixed disulfides, and in separate experiments, TTase from rat liver displayed analogous selectivity.
Protein-thiol oxidation and cell death: regulatory role of glutaredoxins.
Knowledge of the effects of Grx is essential for developing novel therapeutic approaches for treating diseases involving dysregulated apoptosis, such as cancer, heart disease, diabetes, and neurodegenerative diseases, where alterations in redox homeostasis are hallmarks for pathogenesis.
Acute Cadmium Exposure Inactivates Thioltransferase (Glutaredoxin), Inhibits Intracellular Reduction of Protein-glutathionyl-mixed Disulfides, and Initiates Apoptosis*
- C. Chrestensen, D. W. Starke, J. Mieyal
- Biology, ChemistryJournal of Biological Chemistry
- 25 August 2000
Exposure of H9 and Jurkat cells to cadmium inhibited intracellular protein-SSG reduction, and this correlated with inhibition of the thiol transferase system, suggesting that thioltransferase has a vital role in sulfhydryl homeostasis and cell survival.
Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation.
- M. Gallogly, D. W. Starke, J. Mieyal
- Biology, ChemistryAntioxidants and Redox Signaling
- 7 April 2009
A forum review of the mechanism of the deglutathionylation reaction catalyzed by prototypical dithiol glutaredoxins and potential mechanisms for in vivo regulation of Grx activity are presented, providing avenues for future studies.
Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.
- Y. Yang, S. Jao, S. Nanduri, D. W. Starke, J. Mieyal, J. Qin
- Biology, ChemistryBiochemistry
- 8 December 1998
To understand the molecular basis of TTase specificity for the glutathione moiety, a quadruple Cys to Ser mutant of human TTase is engineered which displays the same catalytic efficiency and specificity for glutathionyl mixed disulfide substrates as wild-type TTase, indicating that the Cys-25-SH moiety is not required for catalysis or glutathIONyl specificity.
Dysregulation of Glutathione Homeostasis in Neurodegenerative Diseases
- W. M. Johnson, A. Wilson-Delfosse, J. Mieyal
- BiologyNutrients
- 1 October 2012
The pros and cons of administration of N-acetylcysteine or glutathione as therapeutic agents for neurodegenerative diseases, as well as the potential utility of serum glutATHione as a biomarker, are critically evaluated.
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