Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress

Free Radical Biology and Medicine

Volumn 27, Issue 5-6, 1999, Pages 605-611

  Fu, Yangxin ^a   Cheng, Wen Hsing ^a   Porres, Jesus M ^a   Ross, Deborah A ^a   Lei, Xin Gen ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

Alanine aminotransferase; Carbonyl; Cellular glutathione peroxidase; Diquat; F2 isoprostanes; Free radicals; Knockout; Selenium

Indexed keywords

ALANINE AMINOTRANSFERASE; CARBONYL DERIVATIVE; DIQUAT; FREE RADICAL; GLUTATHIONE PEROXIDASE; PROSTAGLANDIN DERIVATIVE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; KNOCKOUT GENE; LIPID PEROXIDATION; MORTALITY; MOUSE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; SELENIUM DEFICIENCY; SURVIVAL TIME;

ALANINE TRANSAMINASE; ANIMALS; CATALASE; DIQUAT; GLUTATHIONE PEROXIDASE; LIVER; MICE; MICE, KNOCKOUT; OXIDATIVE STRESS; PROSTAGLANDINS; PROTEINS; SELENIUM; SELENOPROTEINS; SUPEROXIDE DISMUTASE; TIME FACTORS;

ANIMALIA;

EID: 0032820359     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00104-5     Document Type: Article

References (37)

1. Farrington J.A., Ebert M., Land E.J., Fletcher K. Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implication for the mode of action of bipyridyl herbicides. Biochim. Biophys. Acta. 314:1973;372-381.
2. Burk R.F., Lawrence R.A., Lane J.M. Liver necrosis and lipid peroxidation in the rat as the result of paraquat and diquat administration. J. Clin. Invest. 65:1980;1024-1031.
3. Burk R.F., Hill K.E., Awad J.A., Morrow J.D., Kato T., Cockell K.A., Lyons P.R. Pathogenesis of diquat-induced liver necrosis in selenium-deficient rat assessment of the role of lipid peroxidation and selenoprotein P . Hepatology. 21:1995;561-569.
4. Awad J.A., Burk R.F., Roberts L.J. Effect of selenium deficiency and glutathione-modulating agents on diquat toxicity and lipid peroxidation in rats. J. Pharmacol. Exp. Ther. 270:1994;858-864.
5. Smith C.V. Evidence for participation of lipid peroxidation and iron in diquat-induced hepatic necrosis in vivo. Mol. Pharmacol. 32:1987;417-422.
6. Smith C.V., Hughes H., Lauterburg B.H., Mitchell J.R. Oxidant stress and hepatic necrosis in rats treated with diquat. J. Pharmacol. Exp. Ther. 235:1985;172-177.
7. Smith C.V. Effect of BCNU pretreatment on diquat-induced oxidant stress and hepatotoxicity. Biochem. Biophys. Res. Commun. 144:1987;415-421.
8. Flohé L., Günzler W.A., Schock H.H. Glutathione peroxidase a selenoenzyme . FEBS Lett. 32:1973;132-134.
9. Rotruck J.T., Pope A.L., Ganther H.E., Swanson A.B., Hafeman D.G., Hoekstra W.G. Selenium biochemical role as a component of glutathione peroxidase . Science. 179:1973;588-590.
10. Cheng W.-H., Ho Y.-S., Ross D.A., Valentine B.A., Combs G.F. Jr, Lei X.G. Cellular glutathione peroxidase knockout mice express normal levels of selenium-dependent plasma and phospholipid hydroperoxide glutathione peroxidase in various tissues. J. Nutr. 127:1997;1445-1450.
11. Sunde R.A. Intracellular glutathione peroxidase - structures, regulation, and functions. Burk R.F. Selenium in biology and human health. 1994;45-77 Springer-Verlag, New York.
12. Ho Y.-S., Magnenat J.L., Bronson R.T., Cao J., Gargano M., Sugawara M., Funk C.D. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem. 272:1997;16644-16651.
13. Cheng W.-H., Ho Y.-S., Valentine B.A., Ross D.A., Combs G.F. Jr, Lei X.G. Cellular glutathione peroxidase is the mediator of the body selenium to protect against paraquat lethality in transgenic mice. J. Nutr. 128:1998;1070-1076.
14. de Haan J.B., Bladier C., Griffiths P., Kelner M., O'Shea R.D., Cheung N.S., Bronson R.T., Silvestro M.J., Wild S., Zheng S.S., Beart P.M., Hertzog P.J., Kola I. Mice with a homozygous null mutation for the most abundant glutathione peroxidase, GPX1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J. Biol. Chem. 273:1998;22528-22536.
15. 2-like compounds are produced in vivo in human by a non-cyclooxygenase, free radical-catalyzed mechanism. Proc. Natl. Acad. Sci. USA. 87:1990;9383-9387.
16. 2-isoprostane produced by non-cyclooxygenase free radical-catalyzed mechanism . Methods Enzymol. 233:1994;163-174.
17. Levine R.L., Garland D., Oliver C.N., Amici A., Climent I., Lenz A.G., Ahn B.W., Shaltiel S., Stadtman E.R. Determination of carbonyl contents in oxidatively modified protein. Methods Enzymol. 186:1990;464-478.
18. Reznick A.Z., Packer L. Oxidative damage to protein spectrophotometric method for carbonyl assay . Methods Enzymol. 233:1994;357-363.
19. Lawrence R.A., Sunde R.A., Schwartz G.L., Hoekstra W.G. Glutathione peroxidase activity in rat lens and other tissues in relation to dietary selenium intake. Exp. Eye Res. 18:1974;563-569.
20. Maiorino M., Gregolin C., Ursini F. Phospholipid hydroperoxide glutathione peroxidase. Methods Enzymol. 186:1990;448-457.
21. Holmgren A., Björnstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol. 252:1995;199-208.
22. Aebi H. Catalase. in vitro. Methods Enzymol. 105:1984;121-126.
23. Ukeda H., Maeda S., Ishii T., Sawamura M. Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3′-{1-[(phenylamino)-carbonyl]-3,4-terazolium}-bis(4-methoxy-6-intro) benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase. Anal. Biochem. 251:1997;206-209.
24. Bermano G., Nicol F., Dyer J.A., Sunde R.A., Beckett G.J., Arthur J.R., Hesketh J.E. Tissue specific regulation of selenoenzyme gene expression during selenium deficiency in rats. Biochem. J. 311:1995;425-430.
25. Christensen M.J., Cammack P.M., Wray C.D. Tissue specificity of selenoprotein gene expression in rats. J. Nutr. Biochem. 6:1995;367-372.
26. Takahashi K., Avissar N., Whitin J., Cohen H. Purification and characterization of human plasma glutathione peroxidase a selenoglycoprotein distinct from the known cellular enzyme . Arch. Biochem. Biophys. 256:1987;677-686.
27. Vadhanaviki S., Ganther H.E. Selenium requirement of rats for normal hepatic and thyroidal 5′-deiodinase (type I) activities. J. Nutr. 123:1993;1124-1128.
28. Vendeland S.C., Belstein M.A., Yeh J.-Y., Ream W., Whanger P.D. Rat skeletal muscle selenoprotein W cDNA clone and mRNA modulation by dietary selenium . Proc. Natl. Acad. Sci. USA. 92:1995;8749-8753.
29. Weiss S.L., Evenson J.K., Thompson K.T., Sunde R.A. The selenium requirement for glutathione peroxidase mRNA level is half of the selenium requirement for glutathione peroxidase activity in female rats. J. Nutr. 126:1996;2260-2267.
30. Yang J.-G., Hill K.E., Burk R.F. Dietary selenium intake controls rat plasma selenoprotein P concentration. J. Nutr. 119:1989;1010-1012.
31. Shacter E., Williams J.A., Lim M., Levine R.L. Differential susceptibility of plasma proteins to oxidative modification examination by Western blot immunoassay . Free Radic. Biol. Med. 17:1994;429-437.
32. Suzuki T., Kim C.H., Yasumoto K. Deterioration of membrane morphology, phospholipids, and cytoskeletal protein in rat erythrocytes exposed to tert-butyl hydroperoxide protection by exogenous glutathione fails in selenium deficiency . J. Nutr. Vitaminol. 34:(Tokyo):1988;491-506.
33. Maiorino M., Wissing J.B., Brigelius-Flohé R., Calabrese F., Roveri A., Steinert P., Ursini F., Flohé L. Testosterone mediates expression of the selenoprotein PHGPx by induction of spermatogenesis and not by direct transcriptional gene activation. FASEB J. 12:1998;1359-1370.
34. Makino N., Mochizuki Y., Bannai S., Sugita Y. Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. J. Biol. Chem. 269:1994;1020-1025.
35. Kelner M.J., Bagnell R. Alteration of endogenous glutathione peroxidase, manganese superoxide dismutase, and glutathione transferase activity in cells transfected with a copper-zinc superoxide dismutase expression vector. J. Biol. Chem. 265:1990;10872-10875.
36. de Haan J.B., Cristiano F., Iannello R., Bladier C., Kelner M.J., Kola I. Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxide activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. Hum. Mol. Genet. 5:1996;283-292.
37. Amstad P., Moret R., Cerutti P. Glutathione peroxidase compensates for the hypersensitivity of Cu, Zn-superoxide dismutase overproducers to oxidant stress. J. Biol. Chem. 269:1994;1606-1609.