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Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.
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. Expand
Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells*
  • Jun Wang, E. Boja, +5 authors P. B. Chock
  • Medicine, Biology
  • The Journal of Biological Chemistry
  • 21 December 2001
A novel physiological relevance of actin polymerization regulated by reversible glutathionylation of the penultimate cysteine mediated by growth factor stimulation is revealed. Expand
Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress.
This review focuses primarily on mechanisms of catalysis in mammalian systems, and insight into cellular mechanisms of protein glutathionylation and deglutathionyation will enrich the understanding of redox signal transduction and identify new therapeutic targets for diseases in which oxidative stress perturbs normal redox signaling. Expand
Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation.
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. Expand
Acute Cadmium Exposure Inactivates Thioltransferase (Glutaredoxin), Inhibits Intracellular Reduction of Protein-glutathionyl-mixed Disulfides, and Initiates Apoptosis*
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. Expand
Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
Thioltransferase (glutaredoxin) appears to be specific for glutathione-containing mixed disulfides, and in separate experiments, TTase from rat liver displayed analogous selectivity. Expand
Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation.
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. Expand
Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.
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. Expand
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. Expand
Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFκB*
In murine embryonic fibroblasts, N-acetyl-l-cysteine (NAC), a GSH generating agent, enhances hypoxic apoptosis by blocking the NFκB survival pathway (Qanungo, S., Wang, M., and Nieminen, A. L. (2004)Expand