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Gene Review

GSR  -  glutathione reductase

Bos taurus

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Disease relevance of GSR

 

High impact information on GSR

  • In the oxidized enzyme, we demonstrated two nonflavin redox centers by chemical modification and peptide sequencing: one was a disulfide within the sequence -Cys(59)-Val-Asn-Val-Gly-Cys(64), identical to the active site of GR; the other was a selenenylsulfide formed from Cys(497)-SeCys(498) and confirmed by mass spectrometry [3].
  • Mammalian thioredoxin reductases (TrxR) are homodimers, homologous to glutathione reductase (GR), with an essential selenocysteine (SeCys) residue in an extension containing the conserved C-terminal sequence -Gly-Cys-SeCys-Gly [3].
  • These findings suggest specifically N-nitrosation of glutathione reductase as a likely mechanism of inhibition elicited by dinitrosyl-iron complex and demonstrate in general that structural resemblance of an NO carrier with a natural ligand enhances NO+ transfer to the ligand-binding protein [4].
  • Preincubation of cells with the glutathione reductase inhibitor, carmustine, led to elevated basal [Ca2+]i, yet the cells remained responsive to bradykinin [5].
  • The effects of oxidant stress and inhibition of glutathione reductase on the bradykinin-stimulated changes in cytosolic free Ca2+ concentration ([Ca2+]i) of calf pulmonary artery endothelial cells were determined using the intracellular fluorescent probe, fura-2 [5].
 

Biological context of GSR

 

Anatomical context of GSR

 

Associations of GSR with chemical compounds

 

Other interactions of GSR

 

Analytical, diagnostic and therapeutic context of GSR

References

  1. Enzymes of oxidant defence system of leucocytes and erythrocytes in bovine anaplasmosis. More, T., Reddy, G.R., Sharma, S.P., Singh, L.N. Vet. Parasitol. (1989) [Pubmed]
  2. Thiol oxidation activates a novel redox-regulated coronary vasodilator mechanism involving inhibition of Ca2+ influx. Iesaki, T., Wolin, M.S. Arterioscler. Thromb. Vasc. Biol. (2000) [Pubmed]
  3. Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Zhong, L., Arnér, E.S., Holmgren, A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  4. Inhibition of glutathione reductase by dinitrosyl-iron-dithiolate complex. Boese, M., Keese, M.A., Becker, K., Busse, R., Mülsch, A. J. Biol. Chem. (1997) [Pubmed]
  5. Carmustine augments the effects of tert-butyl hydroperoxide on calcium signaling in cultured pulmonary artery endothelial cells. Elliott, S.J., Schilling, W.P. J. Biol. Chem. (1990) [Pubmed]
  6. Glycation (non-enzymic glycosylation) inactivates glutathione reductase. Blakytny, R., Harding, J.J. Biochem. J. (1992) [Pubmed]
  7. Regulation of hydrogen peroxide generation in cultured endothelial cells. Kinnula, V.L., Whorton, A.R., Chang, L.Y., Crapo, J.D. Am. J. Respir. Cell Mol. Biol. (1992) [Pubmed]
  8. A direct link between LY83583, a selective repressor of cyclic GMP formation, and glutathione metabolism. Lüönd, R.M., McKie, J.H., Douglas, K.T. Biochem. Pharmacol. (1993) [Pubmed]
  9. Glutathione-dependent detoxification of peroxide in bovine ciliary body. Shichi, H. Exp. Eye Res. (1990) [Pubmed]
  10. Redox state of pyridine nucleotides, but not glutathione, regulate Ca2+ release by H2O2 from mitochondria of pulmonary smooth muscle. Roychoudhury, S., Chakraborti, T., Ghosh, J.J., Ghosh, S.K., Chakraborti, S. Indian J. Biochem. Biophys. (1996) [Pubmed]
  11. Effect of Prototheca zopfii on neutrophil function from bovine milk. Cunha, L.T., Pugine, S.P., Valle, C.R., Ribeiro, A.R., Costa, E.J., De Melo, M.P. Mycopathologia (2006) [Pubmed]
  12. NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals. Shi, X.L., Dalal, N.S. FEBS Lett. (1990) [Pubmed]
  13. Reduction of a trisulfide derivative of glutathione by glutathione reductase. Moutiez, M., Aumercier, M., Teissier, E., Parmentier, B., Tartar, A., Sergheraert, C. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  14. Deferoxamine inhibition of Cr(V)-mediated radical generation and deoxyguanine hydroxylation: ESR and HPLC evidence. Shi, X.G., Sun, X.L., Gannett, P.M., Dalal, N.S. Arch. Biochem. Biophys. (1992) [Pubmed]
  15. Glucose-6-phosphate dehydrogenase overexpression decreases endothelial cell oxidant stress and increases bioavailable nitric oxide. Leopold, J.A., Zhang, Y.Y., Scribner, A.W., Stanton, R.C., Loscalzo, J. Arterioscler. Thromb. Vasc. Biol. (2003) [Pubmed]
  16. Drug-induced changes in selenium-dependent glutathione peroxidase activity in the chick. Mercurio, S.D., Combs, G.F. J. Nutr. (1985) [Pubmed]
  17. The changes of prooxidant and antioxidant enzyme activities in bovine leukemia virus-transformed cells. Their influence on quinone cytotoxicity. Nemeikaite, A., Cenas, N. FEBS Lett. (1993) [Pubmed]
  18. Glutathione redox cycle regulates nitric oxide-mediated glyceraldehyde-3-phosphate dehydrogenase inhibition. Padgett, C.M., Whorton, A.R. Am. J. Physiol. (1997) [Pubmed]
  19. Susceptibility of glutathione peroxidase and glutathione reductase to oxidative damage and the protective effect of spin trapping agents. Tabatabaie, T., Floyd, R.A. Arch. Biochem. Biophys. (1994) [Pubmed]
 
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