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Gene Review

GPX1  -  glutathione peroxidase 1

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Disease relevance of GPX1

  • However, the low levels of glutathione peroxidase resulting from selenium deficiency cause an increase susceptibility to peroxide-mediated toxicity [1].
  • The activities of GSHPx and the vitamin E levels in plasma were not significantly different in the two groups of herds, and no relationship was found between the two nutrients and the incidence of clinical mastitis [2].
  • No differences occurred between immunization groups in blood selenium and glutathione peroxidase activity, plasma selenium, number of E. coli 727 isolated from secretion after challenge, rectal temperature and SCC response, clinical status of mammary quarters, or DMI [3].
  • Selenium effects on glutathione peroxidase and the immune response of stressed calves challenged with Pasteurella hemolytica [4].
  • No significant differences in body weight, plasma concentrations of urea, or whole blood concentrations of glutathione peroxidase were detected between groups before or after calving [5].

Psychiatry related information on GPX1

  • It was concluded that selenium supplementation in cows with low GPx activity seems to support udder defense mechanisms that favor reduction of the incidence of new mastitis cases [6].

High impact information on GPX1

  • In this study, we tested the hypothesis that overexpression of GPx-1 can restore the normal endothelial phenotype in hyperhomocyst(e)inemic states [7].
  • An elevated level of homocysteine in vivo and in cell culture systems results in a decrease in the activity of cellular glutathione peroxidase (GPx1), an intracellular antioxidant enzyme that reduces hydrogen peroxide and lipid peroxides [8].
  • These data support the conclusion that homocysteine decreases GPx1 activity by altering the translational mechanism essential for the synthesis of this selenocysteine-containing protein [8].
  • Expression of the selenocysteine (SEC)-containing GPx1 protein requires special translational cofactors to "read-through" a UGA-stop codon that specifies SEC incorporation at the active site of the enzyme [8].
  • We investigated the anti-apoptotic effects of intracellular and extracellular nitric oxide (*NO) donors, iron chelators, cell-permeable superoxide dismutase (SOD), glutathione peroxidase mimetics, and nitrone spin traps [9].

Chemical compound and disease context of GPX1


Biological context of GPX1


Anatomical context of GPX1


Associations of GPX1 with chemical compounds


Physical interactions of GPX1


Regulatory relationships of GPX1


Other interactions of GPX1


Analytical, diagnostic and therapeutic context of GPX1


  1. Selenium deficiency in cultured adrenocortical cells: restoration of glutathione peroxidase and resistance to hydroperoxides on addition of selenium. Hornsby, P.J., Pearson, D.W., Autor, A.P., Aldern, K.A., Harris, S.E. J. Cell. Physiol. (1985) [Pubmed]
  2. Studies on the incidence of clinical mastitis and blood levels of vitamin E and selenium in dairy herds in England. Ndiweni, N., Field, T.R., Williams, M.R., Booth, J.M., Finch, J.M. Vet. Rec. (1991) [Pubmed]
  3. Intramammary challenge with Escherichia coli following immunization with a curli-producing Escherichia coli. Todhunter, D.A., Smith, K.L., Hogan, J.S., Nelson, L. J. Dairy Sci. (1991) [Pubmed]
  4. Selenium effects on glutathione peroxidase and the immune response of stressed calves challenged with Pasteurella hemolytica. Stabel, J.R., Spears, J.W., Brown, T.T., Brake, J. J. Anim. Sci. (1989) [Pubmed]
  5. Effects of monensin on the metabolism of periparturient dairy cows. Stephenson, K.A., Lean, I.J., Hyde, M.L., Curtis, M.A., Garvin, J.K., Lowe, L.B. J. Dairy Sci. (1997) [Pubmed]
  6. Effects of oral selenium supplementation on mastitis markers and pathogens in Estonian cows. Malbe, M., Klaassen, E., Kaartinen, L., Attila, M., Atroshi, F. Vet. Ther. (2003) [Pubmed]
  7. Overexpression of cellular glutathione peroxidase rescues homocyst(e)ine-induced endothelial dysfunction. Weiss, N., Zhang, Y.Y., Heydrick, S., Bierl, C., Loscalzo, J. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Homocysteine down-regulates cellular glutathione peroxidase (GPx1) by decreasing translation. Handy, D.E., Zhang, Y., Loscalzo, J. J. Biol. Chem. (2005) [Pubmed]
  9. Inhibition of oxidized low-density lipoprotein-induced apoptosis in endothelial cells by nitric oxide. Peroxyl radical scavenging as an antiapoptotic mechanism. Kotamraju, S., Hogg, N., Joseph, J., Keefer, L.K., Kalyanaraman, B. J. Biol. Chem. (2001) [Pubmed]
  10. 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]
  11. Are ruminal bacteria protected against environmental stress by plant antioxidants? Holovská, K., Lenártová, V., Holovská, K., Pristas, P., Javorský, P. Lett. Appl. Microbiol. (2002) [Pubmed]
  12. Studies on serum tocopherol, selenium levels and blood glutathione peroxidase activities in calves with white muscle disease. Hoshino, Y., Ichijo, S., Osame, S., Takahashi, E. Nippon Juigaku Zasshi (1989) [Pubmed]
  13. The effect of buparvaquone treatment on the levels of some antioxidant vitamins, lipid peroxidation and glutathione peroxidase in cattle with theileriosis. Naziroğlu, M., Saki, C.E., Sevgili, M. Zentralblatt Veterinarmedizin Reihe B (1999) [Pubmed]
  14. The amino-acid sequence of bovine glutathione peroxidase. Günzler, W.A., Steffens, G.J., Grossmann, A., Kim, S.M., Otting, F., Wendel, A., Flohé, L. Hoppe-Seyler's Z. Physiol. Chem. (1984) [Pubmed]
  15. Subcellular localization of adrenal cortical glutathione peroxidase and protective role of the mitochondrial enzyme against lipid peroxidative damage. Timcenko-Youssef, L., Yamazaki, R.K., Kimura, T. J. Biol. Chem. (1985) [Pubmed]
  16. Altered eicosanoid biosynthesis in selenium-deficient endothelial cells. Cao, Y.Z., Reddy, C.C., Sordillo, L.M. Free Radic. Biol. Med. (2000) [Pubmed]
  17. Expression of apoptosis regulatory genes by retinal pericytes after rapid glucose reduction. Li, W., Liu, X., He, Z., Yanoff, M., Jian, B., Ye, X. Invest. Ophthalmol. Vis. Sci. (1998) [Pubmed]
  18. Glucose 6-phosphate dehydrogenase of calf trabecular meshwork. Nguyen, K., Lee, D.A., Anderson, P.J., Epstein, D.L. Invest. Ophthalmol. Vis. Sci. (1986) [Pubmed]
  19. Homocyst(e)ine decreases bioavailable nitric oxide by a mechanism involving glutathione peroxidase. Upchurch, G.R., Welch, G.N., Fabian, A.J., Freedman, J.E., Johnson, J.L., Keaney, J.F., Loscalzo, J. J. Biol. Chem. (1997) [Pubmed]
  20. Effect of cell substrate on antioxidant enzyme activities in cultured renal glomerular epithelium. Yang, A.H., Oberley, T.D., Oberley, L.W., Ramanathan, R. Am. J. Pathol. (1988) [Pubmed]
  21. Glutathione peroxidase of calf trabecular meshwork. Scott, D.R., Karageuzian, L.N., Anderson, P.J., Epstein, D.L. Invest. Ophthalmol. Vis. Sci. (1984) [Pubmed]
  22. Evidence for a peroxide-initiated free radical mechanism of prostaglandin biosynthesis. Hemler, M.E., Lands, W.E. J. Biol. Chem. (1980) [Pubmed]
  23. Characterization of a Rac1 signaling pathway to cyclin D(1) expression in airway smooth muscle cells. Page, K., Li, J., Hodge, J.A., Liu, P.T., Vanden Hoek, T.L., Becker, L.B., Pestell, R.G., Rosner, M.R., Hershenson, M.B. J. Biol. Chem. (1999) [Pubmed]
  24. L-Homocysteine and L-homocystine stereospecifically induce endothelial nitric oxide synthase-dependent lipid peroxidation in endothelial cells. Heydrick, S.J., Weiss, N., Thomas, S.R., Cap, A.P., Pimentel, D.R., Loscalzo, J., Keaney, J.F. Free Radic. Biol. Med. (2004) [Pubmed]
  25. Increased 15-HPETE production decreases prostacyclin synthase activity during oxidant stress in aortic endothelial cells. Weaver, J.A., Maddox, J.F., Cao, Y.Z., Mullarky, I.K., Sordillo, L.M. Free Radic. Biol. Med. (2001) [Pubmed]
  26. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Peshenko, I.V., Shichi, H. Free Radic. Biol. Med. (2001) [Pubmed]
  27. Effect of ebselen on IL-1-induced alterations in cartilage metabolism. Pratta, M.A., Ackerman, N.R., Arner, E.C. Inflamm. Res. (1998) [Pubmed]
  28. Estrogen selectively up-regulates the phospholipid hydroperoxide glutathione peroxidase in the oviducts. Lapointe, J., Kimmins, S., Maclaren, L.A., Bilodeau, J.F. Endocrinology (2005) [Pubmed]
  29. Effects of high dietary sulphur on enzyme activities, selenium concentrations and body weights of cattle. Khan, A.A., Lovejoy, D., Sharma, A.K., Sharma, R.M., Prior, M.G., Lillie, L.E. Can. J. Vet. Res. (1987) [Pubmed]
  30. Modulation of hydrogen peroxide release from vascular endothelial cells by oxygen. Kinnula, V.L., Mirza, Z., Crapo, J.D., Whorton, A.R. Am. J. Respir. Cell Mol. Biol. (1993) [Pubmed]
  31. Antioxidant defenses are modulated in the cow oviduct during the estrous cycle. Lapointe, J., Bilodeau, J.F. Biol. Reprod. (2003) [Pubmed]
  32. Glutathione-dependent detoxification of peroxide in bovine ciliary body. Shichi, H. Exp. Eye Res. (1990) [Pubmed]
  33. Activity staining of glutathione peroxidase after electrophoresis on native and sodium dodecyl sulfate polyacrylamide gels. Lin, C.L., Chen, H.J., Hou, W.C. Electrophoresis (2002) [Pubmed]
  34. Glutathione S-transferases of the bovine retina. Evidence that glutathione peroxidase activity is the result of glutathione S-transferase. Saneto, R.P., Awasthi, Y.C., Srivastava, S.K. Biochem. J. (1982) [Pubmed]
  35. Characterization and immunological properties of selenium-containing glutathione peroxidase induced by selenite in Chlamydomonas reinhardtii. Shigeoka, S., Takeda, T., Hanaoka, T. Biochem. J. (1991) [Pubmed]
  36. Antioxidative defence mechanisms against reactive oxygen species in bovine retained and not-retained placenta: activity of glutathione peroxidase, glutathione transferase, catalase and superoxide dismutase. Kankofer, M. Placenta (2001) [Pubmed]
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