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Gene Review

Gsr  -  glutathione reductase

Rattus norvegicus

Synonyms: GR, GRase, Glutathione reductase
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Disease relevance of Gsr

  • In conclusion, the results obtained indicate that the activity of SOD, GPX, and GR in renal and cardiac tissues is decreased in hyperthyroidism and that antioxidant treatment with tempol ameliorates T4-induced hypertension [1].
  • Regarding changes in the enzyme activities accompanying development of iron epilepsy, the data showed that although SOD and G6P increased by approximately 60% and GR increased by approximately 40%, the increases in the enzyme GP and CA were much lower, less than 20% [2].
  • CONCLUSIONS: We conclude that L-NAME-induced hypertension is associated with an upregulation of antioxidant SOD, GPX, and GR activities [3].
  • Whereas body weight, testis weight, relative weight of testis, ABP, lactate and specific activities of SOD, CAT, GPx, GR, GST, gamma-GT were all decreased, the levels of hydrogen peroxide, hydroxyl radical and LPO were significantly increased in the Sertoli cells of Aroclor 1254 treated rats [4].
  • Protein deficiency in normal rats resulted in a significant increase in hepatic lipid peroxidation and in catalase, Gpx, GR and GST activity [5].

Psychiatry related information on Gsr


High impact information on Gsr

  • After weanling rats were put on a riboflavin-deficient diet, the development of the deficiency was monitored by the growth rate and the erythrocyte glutathione reductase activation coefficient [7].
  • The hepatic activities of glucose-6-phosphate dehydrogenase, glutathione reductase, and glutathione-S-transferases were markedly elevated while catalase and superoxide dismutase activities were unchanged [8].
  • Taken together, these observations suggest that GSH acts directly on the enzyme in the crude microsomal fraction, whereas NADPH acts within the cytosol, possibly by increasing the concentration of GSH through the action of the enzyme glutathione reductase, for which NADPH is a cofactor [9].
  • Surprisingly, all residues directly interacting with the substrate glutathione disulfide in GR are conserved despite the failure of glutathione disulfide to act as a substrate for TrxR [10].
  • The overall structure is similar to that of glutathione reductase (GR), including conserved amino acid residues binding the cofactors FAD and NADPH [10].

Chemical compound and disease context of Gsr


Biological context of Gsr


Anatomical context of Gsr


Associations of Gsr with chemical compounds

  • It is concluded that increases in the lung complement of SOD, GR, GP, and GSH in the neonatal rat during oxygen challenge may provide the mechanism(s) for their increased tolerance to hyperoxia-induced lung injury as compared to the adults [26].
  • The changes in T + DES-treated VP were most dramatic with a marked activation of GPx (by one-fold), GR (by one-fold), and G6PD (by five-fold) [27].
  • In renal cortex, SOD activity was decreased in the T4-75 group, and there was a dose-related increase in CAT activity and decrease in GPX and GR activities in T4-treated groups [1].
  • Both gp120 and Tat significantly decreased the levels of intracellular GSH, GPx, and GR and increased the levels of MDA in RBE4 cells, showing that the cells were oxidatively challenged [28].
  • Cochlear SOD, CAT, GSH-Px, and GR activities and MDA concentrations were restored in the rats injected with cisplatin plus graded doses of lipoate than those with cisplatin alone [29].

Physical interactions of Gsr


Enzymatic interactions of Gsr


Regulatory relationships of Gsr


Other interactions of Gsr


Analytical, diagnostic and therapeutic context of Gsr

  • Joint immobilization (11 wk) did not affect GPX, GRD, and GST of RG, but total glutathione decreased [41].
  • The resultant antibody specifically reacted with rat GPX1 and was, together with the Glutathione reductase (GR) antibody, used in a Western blot analysis and immunohistochemistry experiments [42].
  • For co-cultures, however, after some initial variations GR and GPx activities reached stabilized levels which were not only significantly lower than those observed for pure cultures, but were also maintained throughout the whole culture period [43].
  • When Hepes buffer with a low oxygen content was used in cell isolation, pure cultures showed significantly lower GR and GPx activities than those first mentioned.(ABSTRACT TRUNCATED AT 250 WORDS)[43]
  • The activity of glutathione reductase (GR) was suppressed by EB short time, only 2 h following treatment, whereas P increased the enzyme activity 24 h after treatment [44].


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  2. Lipid peroxidation and glutathione peroxidase, glutathione reductase, superoxide dismutase, catalase, and glucose-6-phosphate dehydrogenase activities in FeCl3-induced epileptogenic foci in the rat brain. Singh, R., Pathak, D.N. Epilepsia (1990) [Pubmed]
  3. Antioxidant enzymes and effects of tempol on the development of hypertension induced by nitric oxide inhibition. Sainz, J., Wangensteen, R., Rodríguez Gómez, I., Moreno, J.M., Chamorro, V., Osuna, A., Bueno, P., Vargas, F. Am. J. Hypertens. (2005) [Pubmed]
  4. Effects of Vitamin C and E on PCB (Aroclor 1254) induced oxidative stress, androgen binding protein and lactate in rat Sertoli cells. Senthil kumar, J., Banudevi, S., Sharmila, M., Murugesan, P., Srinivasan, N., Balasubramanian, K., Aruldhas, M.M., Arunakaran, J. Reprod. Toxicol. (2004) [Pubmed]
  5. Protective effects of zinc on oxidative stress enzymes in liver of protein deficient rats. Sidhu, P., Garg, M.L., Dhawan, D.K. Nutrición hospitalaria : organo oficial de la Sociedad Española de Nutrición Parenteral y Enteral. (2004) [Pubmed]
  6. Effect of inhibition of glutathione reductase by carmustine on central nervous system oxygen toxicity. Powell, S.R., Puglia, C.D. J. Pharmacol. Exp. Ther. (1987) [Pubmed]
  7. Effects of riboflavin deficiency on metabolism of nitrosamines by rat liver microsomes. Wang, T., Miller, K.W., Tu, Y.Y., Yang, C.S. J. Natl. Cancer Inst. (1985) [Pubmed]
  8. Modulation of azaserine-induced pancreatic foci by phenolic antioxidants in rats. Roebuck, B.D., MacMillan, D.L., Bush, D.M., Kensler, T.W. J. Natl. Cancer Inst. (1984) [Pubmed]
  9. Observations on the factors that control the generation of triiodothyronine from thyroxine in rat liver and the nature of the defect induced by fasting. Balsam, A., Ingbar, S.H. J. Clin. Invest. (1979) [Pubmed]
  10. Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme. Sandalova, T., Zhong, L., Lindqvist, Y., Holmgren, A., Schneider, G. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  11. Chemopreventive potential of luteolin during colon carcinogenesis induced by 1,2-dimethylhydrazine. Manju, V., Nalini, N. Ital. J. Biochem. (2005) [Pubmed]
  12. Protective effect of glycine supplementation on the levels of lipid peroxidation and antioxidant enzymes in the erythrocyte of rats with alcohol-induced liver injury. Senthilkumar, R., Sengottuvelan, M., Nalini, N. Cell Biochem. Funct. (2004) [Pubmed]
  13. Neuroprotective effect of N-acetyl cysteine on hypoxia-induced oxidative stress in primary hippocampal culture. Jayalakshmi, K., Sairam, M., Singh, S.B., Sharma, S.K., Ilavazhagan, G., Banerjee, P.K. Brain Res. (2005) [Pubmed]
  14. Differential inhibition of rat hepatic glutathione S-transferase isoenzymes in the course of fascioliasis. Galtier, P., Vandenberghe, Y., Coecke, S., Eeckhoutte, C., Larrieu, G., Vercruysse, A. Mol. Biochem. Parasitol. (1991) [Pubmed]
  15. Changes in the glutathione redox system during ischemia and reperfusion in rat liver. Kobayashi, H., Nonami, T., Kurokawa, T., Kitahara, S., Harada, A., Nakao, A., Sugiyama, S., Ozawa, T., Takagi, H. Scand. J. Gastroenterol. (1992) [Pubmed]
  16. Antioxidant S-allylcysteine prevents gentamicin-induced oxidative stress and renal damage. Maldonado, P.D., Barrera, D., Rivero, I., Mata, R., Medina-Campos, O.N., Hernández-Pando, R., Pedraza-Chaverrí, J. Free Radic. Biol. Med. (2003) [Pubmed]
  17. Acutely administered melatonin reduces oxidative damage in lung and brain induced by hyperbaric oxygen. Pablos, M.I., Reiter, R.J., Chuang, J.I., Ortiz, G.G., Guerrero, J.M., Sewerynek, E., Agapito, M.T., Melchiorri, D., Lawrence, R., Deneke, S.M. J. Appl. Physiol. (1997) [Pubmed]
  18. The capacity of glutathione reductase in cell protection from the toxic effect of heated oils. Saka, S., Aouacheri, W., Abdennour, C. Biochimie (2002) [Pubmed]
  19. Effects of ethanol on antioxidant capacity in isolated rat hepatocytes. Yang, S.S., Huang, C.C., Chen, J.R., Chiu, C.L., Shieh, M.J., Lin, S.J., Yang, S.C. World J. Gastroenterol. (2005) [Pubmed]
  20. Effect of disulfiram administration on rat brain glutathione metabolism. Nagendra, S.N., Shetty, K.T., Rao, K.M., Rao, B.S. Alcohol (1994) [Pubmed]
  21. Effects of chlorpromazine on the activities of antioxidant enzymes and lipid peroxidation in the various regions of aging rat brain. Roy, D., Pathak, D.N., Singh, R. J. Neurochem. (1984) [Pubmed]
  22. Role of lipid peroxidation and the glutathione-dependent antioxidant system in the impairment of endothelium-dependent relaxations with age. Rodríguez-Martínez, M.A., Alonso, M.J., Redondo, J., Salaíces, M., Marín, J. Br. J. Pharmacol. (1998) [Pubmed]
  23. Diallyl trisulfide modulates cell viability and the antioxidation and detoxification systems of rat primary hepatocytes. Wu, C.C., Lii, C.K., Tsai, S.J., Sheen, L.Y. J. Nutr. (2004) [Pubmed]
  24. Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria. Panfili, E., Sandri, G., Ernster, L. FEBS Lett. (1991) [Pubmed]
  25. Antioxidant systems in rat epididymal spermatozoa. Tramer, F., Rocco, F., Micali, F., Sandri, G., Panfili, E. Biol. Reprod. (1998) [Pubmed]
  26. Oxygen toxicity: comparison of lung biochemical responses in neonatal and adult rats. Yam, J., Frank, L., Roberts, R.J. Pediatr. Res. (1978) [Pubmed]
  27. Sex hormone-induced alterations in the activities of antioxidant enzymes and lipid peroxidation status in the prostate of Noble rats. Tam, N.N., Ghatak, S., Ho, S.M. Prostate (2003) [Pubmed]
  28. HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells. Price, T.O., Ercal, N., Nakaoke, R., Banks, W.A. Brain Res. (2005) [Pubmed]
  29. Dose dependent protection by lipoic acid against cisplatin-induced ototoxicity in rats: antioxidant defense system. Rybak, L.P., Husain, K., Whitworth, C., Somani, S.M. Toxicol. Sci. (1999) [Pubmed]
  30. An investigation into the effect of sulfonylurea glyburide on glutathione peroxidase activity in streptozotocin-induced diabetic rat muscle tissue. Kiliç, N., Malhatun, E., Elmali, E., Altan, N. Gen. Pharmacol. (1998) [Pubmed]
  31. Regional distribution of glutathione reductase in the adult rat brain. Brannan, T.S., Maker, H.S., Raes, I., Weiss, C. Brain Res. (1980) [Pubmed]
  32. Antioxidant defense mechanisms in cultured pleural mesothelial cells. Kinnula, V.L., Everitt, J.I., Mangum, J.B., Chang, L.Y., Crapo, J.D. Am. J. Respir. Cell Mol. Biol. (1992) [Pubmed]
  33. Involvement of reactive oxygen species and stress-activated MAPKs in satratoxin H-induced apoptosis. Nusuetrong, P., Yoshida, M., Tanitsu, M.A., Kikuchi, H., Mizugaki, M., Shimazu, K., Pengsuparp, T., Meksuriyen, D., Oshima, Y., Nakahata, N. Eur. J. Pharmacol. (2005) [Pubmed]
  34. Semichronic inhibition of glutathione reductase promotes oxidative damage to proteins and induces both transcription and translation of tyrosine hydroxylase in the nigrostriatal system. Romero-Ramos, M., Venero, J.L., Garcia-Rodriguez, S., Ayala, A., Machado, A., Cano, J. Free Radic. Res. (2003) [Pubmed]
  35. The effect of haloalkene cysteine conjugates on rat renal glutathione reductase and lipoyl dehydrogenase activities. Lock, E.A., Schnellmann, R.G. Toxicol. Appl. Pharmacol. (1990) [Pubmed]
  36. Acteoside and its aglycones protect primary cultures of rat cortical cells from glutamate-induced excitotoxicity. Koo, K.A., Kim, S.H., Oh, T.H., Kim, Y.C. Life Sci. (2006) [Pubmed]
  37. Protective effect of SnCl2 on K2Cr2O7-induced nephrotoxicity in rats: the indispensability of HO-1 preinduction and lack of association with some antioxidant enzymes. Barrera, D., Maldonado, P.D., Medina-Campos, O.N., Hernández-Pando, R., Ibarra-Rubio, M.E., Pedraza-Chaverrí, J. Life Sci. (2003) [Pubmed]
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  39. Acinar distribution of glutathione-dependent detoxifying enzymes. Low glutathione peroxidase activity in perivenous hepatocytes. Kera, Y., Sippel, H.W., Penttilä, K.E., Lindros, K.O. Biochem. Pharmacol. (1987) [Pubmed]
  40. Influence of rat brain superoxide dismutase inhibition by diethyldithiocarbamate upon the rate of development of central nervous system oxygen toxicity. Puglia, C.D., Loeb, G.A. Toxicol. Appl. Pharmacol. (1984) [Pubmed]
  41. Skeletal muscle and liver glutathione homeostasis in response to training, exercise, and immobilization. Sen, C.K., Marin, E., Kretzschmar, M., Hänninen, O. J. Appl. Physiol. (1992) [Pubmed]
  42. Differential expression of glutathione reductase and cytosolic glutathione peroxidase, GPX1, in developing rat lungs and kidneys. Fujii, T., Endo, T., Fujii, J., Taniguchi, N. Free Radic. Res. (2002) [Pubmed]
  43. Glutathione dependent detoxication in adult rat hepatocytes under various culture conditions. Mertens, K., Rogiers, V., Vercruysse, A. Arch. Toxicol. (1993) [Pubmed]
  44. Effects of progesterone and estradiol benzoate on glutathione dependent antioxidant enzyme activities in the brain of female rats. Pajović, S.B., Saicić, Z.S., Spasić, M.B., Petrović, V.M., Martinović, J.V. Gen. Physiol. Biophys. (1999) [Pubmed]
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