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Redox Report
Communications in Free Radical Research
Volume 8, 2003 - Issue 2
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Review

An imbalance in antioxidant defense affects cellular function: the pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse

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Pages 69-79 | Published online: 19 Jul 2013

REFERENCES

  • Commoner B, Townsend J, Pake GE. Free radicals in biological materials. Nature 1954; 174: 689–691.
  • Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol 1956; 11: 298–300.
  • Freeman BA, Crapo JD. Biology of disease: free radicals and tissue injury. Lab Invest 1982; 47: 412–426.
  • Brawn K, Fridovich I. DNA strand scission by enzymically generatedoxygen radicals. Arch Biochem Biophys 1981; 206: 414–419.
  • Sies H. Strategies of antioxidant defense. Eur J Biochem 1993; 215: 213–219.
  • Sies H. Oxidative stress: from basic research to clinical application. Am J Med 1991; 91: 31S-38S.
  • Sohal RS, Allen RG. Oxidative stress as a causal factor in differentiation and aging: a unifying hypothesis. Exp Gerontol 1990; 25: 499–522.
  • Halliwell B, Gutteridge JM. Free radicals and antioxidant protection: mechanisms and significance in toxicology and disease. Hum Toxicol 1988; 7: 7–13.
  • Hageman JJ, Bast A, Vermeulen NP. Monitoring of oxidative free radical damage in vivo: analytical aspects. Chem Biol Interact 1992; 82: 243–293.
  • Stamler JS, Singel DJ, Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science 1992; 258: 1898–1902.
  • Parnham MJ, Englberger W. Regulation of the macrophage oxidative burst by mediators: effects of inhibitors. Agents Actions 1985; 16: 50–51.
  • Kasai H, Okada Y, Nishimura S, Rao MS, Reddy JK. Formation of 8-hydroxydeoxyguanosine in liver DNA of rats following long-term exposure to a peroxisome proliferator. Cancer Res 1989; 49: 2603–2605.
  • Imlay JA, Chin SM, Linn S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 1988; 240: 640–642.
  • Harman, D. Free radical involvement in aging. Pathophysiology and therapeutic implications. Drugs Aging 1993; 3: 60–80.
  • Halliwell B,Chirico S. Lipid peroxidation: its mechanism, measure-ment, and significance. Am J Clin Nutr 1993; 57: 715S-725S.
  • Groner Y, Elroy-Stein O, Avraham KB et al. Down syndrome clinical symptoms are manifested in transfected cells and transgenic mice overexpressing the human Cu/Zn-superoxide dismutase gene. J Physiol (Paris) 1990; 84: 53–77.
  • de Haan JB, Newman JD, Kola I. Cu/Zn superoxide dismutase mRNA and enzyme activity, and susceptibility to lipid peroxidation, increases with aging in murine brains. Mol Brain Res 1992; 13: 179–186.
  • de Haan JB, Cristiano F, Iannello R, Kelner M, Kola I. Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase leads to cellular senescence and this effect is mediated by H202. Hum Mol Genet 1996; 5: 283–292.
  • Ames BN, Shigenaga MK, Hagen TM. Oxidants, antioxidants, and the degenerative diseases of aging. Proc Natl Acad Sci USA 1993; 90: 7915–7922.
  • Chen Q, Ames BN. Senescence-like growth arrest induced by hydrogen peroxide in human diploid fibroblast F65 cells. Proc Natl Acad Sci USA 1994; 91: 4130–4134.
  • Jenner P, Dexter DT, Sian J, Schapira AH, Marsden CD. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease. Ann Neurol 1992; 32: S82–S87.
  • Pappolla MA, Chyan YJ, Omar RA et al. Evidence of oxidative stress and in vivo neurotoxicity of beta-amyloid in a transgenic mouse model of Alzheimer's disease: a chronic oxidative paradigm for testing antioxidant therapies in vivo. Am J Pathol 1998; 152: 871–877.
  • de Haan JB, Iannello RC, Crack PJ, Hertzog PJ, Kola I. Oxid-ative and free radical mechanisms in brain aging. In: Sachdev P. (ed) The Aging Brain: Neurobiology and Neuropsychiatry of Ageing. Amsterdam: SWETS and Zietlinger, 2003; 187–203.
  • Elroy-Stein O, Bernstein Y, Groner Y. Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J 1986; 5: 615–622.
  • Amstad P. Peskin A, Shah G et al. The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress. Biochemistry 1991; 30: 9305–9313.
  • Elroy-Stein O, Groner Y. Impaired neurotransmitter uptake in PC12 cells overexpressing human Cu/Zn-superoxide dismutase-implications for gene dosage effects in Down syndrome. Cell 1988; 52: 259–267.
  • Przedborski S, Kostic V. Jackson-Lewis Vet al. Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity. J Neurosci 1992; 12: 1658–1667.
  • Chan PH, Chu L, Chen SF, Carlson EJ, Epstein CJ. Reduced neurotoxicity in transgenic mice overexpressing human copper-zinc-superoxide dismutase. Stroke 1990; 21: 80–82.
  • Chan PH, Yang GY, Chen SF, Carlson E, Epstein CJ. Cold-induced brain edema and infarction are reduced in transgenic mice overexpressing CuZn-superoxide dismutase. Ann Neurol 1991; 29: 482–486.
  • Kinouchi H, Epstein CJ, Mizui T, Carlson E, Chen SF, Chan PH. Attenuation of focal cerebral ischemic injury in transgenic mice overexpressing CuZn superoxide dismutase. Proc Natl Acad Sci USA 1991; 88: 11158–11162.
  • Kubisch HM, Wang J, Luche R et al. Transgenic copper/zinc superoxide dismutase modulates susceptibility to type 1 diabetes. Proc Natl Acad Sci USA 1994; 91: 9956–9959.
  • Craven PA, Melhem MF, Phillips SL, DeRubertis FR. Overexpression of Cu2./Zn2 superoxide dismutase protects against early diabetic glomerular injury in transgenic mice. Diabetes 2001; 50: 2114–2125.
  • Chen Z, Oberley TD, Ho YS et al. Overexpression of CuZnSOD in coronary vascular cells attenuates myocardial ischemia/reperfusion injury. Free Radic Biol Med 2000; 29: 589–596.
  • Levy R, Glozman S, Milman D et al. Ischemic reperfusion brain injury in fetal transgenic mice with elevated levels of copper-zinc superoxide dismutase. J Perinat Med 2002; 30: 158–165.
  • Avraham KB, Schickkr M, Sapoznikov D, Yarom R, Groner Y. Down's syndrome: abnormal neuromuscular junction in tongue of transgenic mice with elevated levels of human Cu/Zn-superoxide dismutase. Cell 1988; 54: 823–829.
  • Yarom R, Sapoznikov D, Havivi Y, Avraham KB, Schickler M, Groner Y. Premature aging changes in neuromuscular junctions of transgenic mice with an extra human CuZnSOD gene: a model for tongue pathology in Down's syndrome. J Neurol Sci 1988; 88: 41–53.
  • Avraham KB, Sugarman H, Rotshenker S, Groner Y. Down's syndrome: morphological remodelling and increased complexity in the neuromuscular junction of transgenic CuZn-superoxide dismutase mice. J Neurocytol 1991; 20: 208–215.
  • Peled-Kamar M, Lotem J, Wirguin I, Weiner L, Hermalin A, Groner Y. Oxidative stress mediates impairment of muscle function in transgenic mice with elevated level of wild-type Cu/Zn superoxide dismutase. Proc Natl Acad Sci USA 1997; 94: 3883–3887.
  • Feaster WW, Kwok LW, Epstein CJ. Dosage effects for superoxide dismutase-1 in nucleated cells aneuploid for chromosome 21. Am J Hum Genet 1977; 29: 563–570.
  • Brooksbank BWL, Balazs R. Superoxide dismutase, glutathione peroxidase and lipoperoxidation in Down's syndrome fetal brain. Dev Brain Res 1984; 16: 37–44.
  • de Haan JB, Wolvetang E, Cristiano F, Iannello R, Kelner M, Kola I. Reactive oxygen species and their contribution to pathology in Down syndrome. Adv Pharmacol 1997; 38: 379–402.
  • Fahim MA, Robbins N. Ultrastructural studies of young and old mouse-neuromuscular junctions. J Neurocytol 1982; 11: 641–656.
  • Nabarra B, Casanova M, Paris et al. Transgenic mice overexpressing the human Cu/Zn-SOD gene: ultrastructural studies of a premature thymic involution model of Down's syndrome (trisomy 21). Lab Invest 1996; 74: 617–626.
  • Peled-Kamar M, Lotem J, Okon E, Sachs L, Groner Y. Thymic abnormalities and enhanced apoptosis of thymocytes and bone marrow cells in transgenic mice overexpressing Cu/Zn-superoxide dismutase: implications for Down syndrome. EMBO J 1995; 14: 4985–4993.
  • Busciglio J, Yankner BA. Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature 1995; 378: 776–779.
  • Ceballos-Picot I, Nicole A, Clement M, Bourre JM, Sinet PM. Age-related changes in antioxidant enzymes and lipid peroxidation in brains of control and transgenic mice overexpressing copper-zinc superoxide dismutase. Mutat Res 1992; 275: 281–293.
  • Ischiropoulos H, Zhu L, Chen Jet al. Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Arch Biochem Biophys 1992; 298: 431–437.
  • Beckman JS, Chen J, Crow JP, Ye YZ. Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration. Prog Brain Res 1994; 103: 371–380.
  • de Haan JB, Bladier C, Griffiths Pet al. Mice with a homozygous null mutation for the most abundant glutathione peroxidase Gpxl, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J Biol Chem 1998; 273: 22528–22536.
  • Esposito LA, Kokoszka JE, Waymire KG, Catttell B, MacGregor GR, Wallace DC. Mitochondrial oxidative stress in mice lacking the gluta-thione peroxidase-1 gene. Free Radic Biol Med 2000; 28: 754–766.
  • Mercurio SD, Combs GF. Selenium-dependent glutathione peroxidase inhibitors increase toxicity of prooxidant compounds in chicks. J Nutr 1986; 116: 1726–1734.
  • Sunde RA, Thompson BM, Palm MD, Weiss SL, Thompson KM, Evenson JK. Selenium regulation of selenium-dependent glutathione peroxidases in animals and transfected CHO cells. Biomed Environ Sci 1997; 10: 346–355.
  • Ho YS, Magnenat JL, Bronson RT et al. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J Biol Chem 1997; 272: 16644–16651.
  • Brigelius-Flohe R. Tissue-specific functions of individual glutathione peroxidases. Free Radic Biol Med 1999; 27: 951–965.
  • Arthur JR. The glutathione peroxidases. Cell Mol Life Sci 2000; 57: 1825–1835.
  • Reddy VN, Giblin FJ, Lin LR et al. Glutathione peroxidase-1 deficiency leads to increased nuclear light scattering, membrane damage, and cataract formation in gene-knockout mice. Invest Ophthalmol Vis Sci 2001; 42: 3247–3255.
  • Cheng WH, Ho YS, Valentine BA, Ross DA, Combs GF, Lei XG. Cellular glutathione peroxidase is the mediator of body selenium to protect against paraquat lethality in transgenic mice. J Nutr 1998; 128: 1070–1076.
  • Krall J, Speranza MJ, Lynch RE. Paraquat-resistant HeLa cells: increased cellular content of glutathione peroxidase. Arch Biochem Biophys 1991; 286: 311–315.
  • Kelner MJ, Bagnell R. Alteration of endogenous glutathione per-oxidase, manganese superoxide dismutase, and glutathione transferase activity in cells transfected with as copper-zinc superoxide dismutase expression vector. J Biol Chem 1990; 265: 10872–10875.
  • Taylor SD, Davenport LD, Speranza MJ, Mullenbach GT, Lynch RE. Glutathione peroxidase protects cultured mammalian cells from the toxicity of adriamycin and paraquat. Arch Biochem Biophys 1993; 305: 600–605.
  • Cheng WH, Fu YX, Pones JM, Ross DA, Lei XG. Selenium-dependent cellular glutathione peroxidase protects mice against a pro-oxidant-induced oxidation of NADPH, NADH, lipids, and protein. FASEB J 1999; 13: 1467–1475.
  • Ursini F, Bindoli A. The role of selenium peroxidases in the protection against oxidative damage of membranes. Chem Phys Lipids 1987; 44: 255–276.
  • Bar-Peled 0, Korkotian E, Segal M, Groner Y. Constitutive77.overexpression of Cu/Zn superoxide dismutase exacerbates kainic acid-induced apoptosis of transgenic-Cu/Zn superoxide dismutase neurons. Proc Natl Acad Sci USA 1996; 93: 8530–8535.
  • Crack PJ, Taylor J, Flentjar NJ et al. Increased infarct size and78.exacerbated apoptosis in the glutathione peroxidase-1 knockout mouse brain in response to ischemia reperfusion injury. J Neurochem 2001; 78: 1389–1399.
  • Carmody RJ, Cotter TG. Signalling apoptosis: a radical approach.79. Redox Report 2001; 6: 77–90.
  • Weisbrot-Lefkowitz M, Reuhl K, Perry B, Chan PH, Inouye M, Mirochnitchenko O. Overexpression of human glutathione peroxidase protects transgenic mice against focal cerebral80.ischemia/reperfusion damage. Mol Brain Res 1998; 53: 333–338.
  • Crack PJ, Taylor JM. de Haan JB, Kola I, Hertzog P. Iannello R. Glutathione peroxidase-1 contributes to the neuroprotection seen in the superoxide dismutase-1 transgenic mouse in response to ischemia/ reperfusion injury. J Cerebr Blood Flow Metab 2003; 23: 19-22.81.
  • Fkntjar NJ, Crack PJ, Hertzog PJ, Iannello RC, de Haan JB, Kola I. Mice lacking glutathione peroxidase-1 activity show increased TUNEL staining and an accelerated inflammatory response in brain following a cold-induced injury. Exp Neurol 2002; 177: 9-20.82.
  • Zhang J, Graham DG, Montine TJ, Ho YS. Enhanced N-methyl-4-pheny1-1,2,3,6-tetrahydropyridine toxicity in mice deficient in CuZn-superoxide dismutase or glutathione peroxidase. J83. Neuropathol Exp Neurol 2000; 59: 53–61.
  • Tolmasoff JM, Ono T, Cutler RG. Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species. ProcNatl Acad Sci USA 1980; 77: 2777-2781.84.
  • Dudas SP, Arking R. A coordinate upregulation of antioxidant gene activities is associated with the delayed onset of senescence in a long-lived strain of Drosophila. J Gerontol Series A-Biol Sci Med 85. Sci 1995; 50: B117–B127.
  • Kretz-Remy C, Mehkn P. Mirault ME, Arrigo AP. Inhibition of I kappa B-alpha phosphorylation and degradation and subsequent NF-86.kappa B activation by glutathione peroxidase overexpression. J Cell Biol 1996; 133: 1083–1093.
  • Mirault ME, Tremblay A, Furling D et al. Transgenic glutathione87.peroxidase mouse models for neuroprotection studies. Ann NY Acad Sci 1994; 738: 104–115.
  • Yoshida T, Maulik N, Engelman RM et al. Glutathione peroxidase knockout mice are susceptible to myocardial ischemia reperfusion88.injury. 1997; 96 (Suppl II): 216-220.
  • Beck MA, Esworthy RS, Ho YS, Chu FF. Glutathione peroxidase protects mice from viral-induced myocarditis. FASEB J1999; 12: 89.1143-1149.
  • Jaeschke H, Ho YS, Fisher MA, Lawson JA, Farhood A.Glutathione peroxidase-deficient mice are more susceptible to90.neutrophil-mediated hepatic parenchymal cell injury during endotoxemia: importance of an intracellular oxidant stress.91. Hepatology 1999; 29: 443–450.
  • Fu Y, Cheng WH, Porres JM, Ross DA, Lei XG. Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress. Free Radic Biol Med 1999; 27: 605–611.
  • Klivenyi P. Andreassen OA, Ferrante RJ et al. Mice deficient in cellular glutathione peroxidase show increased vulnerability to malonate, 3-nitropropionic acid, and 1-methy1-4-pheny1-1,2,5,6-tetrahydropyridine. J Neurosci 2000; 20: 1–7.
  • Guo ZM, Van Remmen H, Yang H et al. Changes in expression of antioxidant enzymes affect cell-mediated LDL oxidation and oxidized LDL-induced apoptosis in mouse aortic cells. Arterioscler Thromb Vase Biol 2001; 21: 1131–1138.
  • Fu Y, McCormick CC, Roneker C, Lei XG. Lipopolysaccharide and interferon-y-induced nitric oxide production and protein oxidation in mouse peritoneal macrophages are affected by glutathione peroxidase-1 gene knockout. Free Radic Biol Med 2001; 31: 450–459.
  • Ohkmiller KK, McFadden SL, Ding DL, Lear PM, Ho YS. Targeted mutation of the gene for cellular glutathione peroxidase (Gpxl) increases noise-induced hearing loss in mice. JARO 2000; 1: 245–254.
  • Esworthy RS, Aranda R, Martin MG, Doroshow JH, Binder SW, Chu FF. Mice with combined disruption of Gpxl and Gpx2 genes have colitis. Am J Physiol 2001; 281: G848–G855.
  • Jiang D, Akopian G, Ho YS, Walsh JP, Andersen JK. Chronic brain oxidation in a glutathione peroxidase knockout mouse model results in increased resistance to induced epileptic seizures. Exp Neurol 2000; 164: 257–268.
  • Esworthy RS, Maim JR, Sam M, Chu FF. Low glutathione peroxidase activity in Gpxl knockout mice protects jejunum crypts from a-irradiation damage. Am J Physiol 2000; 279: G426-G436. Johnson RM, Goyette G, Ravindranath Y, Ho YS. Red cells from glutathione peroxidase- 1 -deficient mice have nearly normal defenses against exogenous peroxides. Blood 2000; 96: 1985-1988. Reddy VN, Lin LR, Ho YS et al. Peroxide-induced damage in lenses of transgenic mice with deficient and elevated levels of glutathione peroxidase. Ophthalmologica 1997; 211: 192-200. Spector A, Yang Y, Ho YS et al. Variation in cellular glutathione peroxidase activity in lens epithelial cells, transgenics and knockouts does not significantly change the response to H202 stress. Exp Eye Res 1999; 62: 521–540.
  • Johnson RM, Goyette G, Ravindranath Y, Ho YS. Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides. Blood 2000; 96: 1985–1988.
  • Reddy VN, Lin LR, Ho YS et al. Peroxide-induced damage in lenses of transgenic mice with deficient and elevated levels of glutathione peroxidase. Ophthalmologica 1997; 211: 192–200.
  • Spector A, Yang Y, Ho YS et al. Variation in cellular glutathione peroxidase activity in lens epithelial cells, transgenics and knockouts does not significantly change the response to H2O2 stress. Exp Eye Res 1999; 62: 521–540.
  • Spector A, Kuszak JR, Ma W, Wang RR, Ho YS, Yang Y. The effect of photochemical stress upon the lenses of normal and glutathione peroxidase-1 knockout mice. Exp Eye Res 1998; 67: 457–471.
  • Spector A, Kuszak JR, Ma W, Wang RR. The effect of aging on glutathione peroxidase-1 knockout mice-Resistance of the lens to oxidative stress. Exp Eye Res 2001; 72: 533–545.
  • Sies H. Ebselen, a selenoorganic compound as glutathione peroxidase mimic. Free Radic Biol Med 1993; 14: 313–323.
  • Neve J. Physiological and nutritional importance of selenium. Experientia 1991; 47: 187–193.

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