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AGE

, Volume 21, Issue 2, pp 47–76 | Cite as

Oxidative stress and superoxide dismutase in development, aging and gene regulation

  • Robert G. Allen
Article

Abstract

Free radicals and other reactive oxygen species are produced in the metabolic pathways of aerobic cells and affect a number of biological processes. Oxidation reactions have been postulated to play a role in aging, a number of degenerative diseases, differentiation and development as well as serving as subcellular messengers in gene regulatory and signal transduction pathways. The discovery of the activity of superoxide dismutase is a seminal work in free radical biology, because it established that free radicals were generated by cells and because it made removal of a specific free radical substance possible for the first time, which greatly accelerated research in this area. In this review, the role of reactive oxygen in aging, amyotrophic lateral sclerosis (a neurodegenerative disease), development, differentiation, and signal transduction are discussed. Emphasis is also given to the role of superoxide dismutases in these phenomena.

Keywords

Oxidative Stress Reactive Oxygen Species Free Radical Superoxide Signal Transduction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Harman, D: Aging: a theory based on free radical and radiation biology. J. Gerontol., 11: 298–300, 1956.PubMedGoogle Scholar
  2. 2.
    Harman, D: Free radicals in aging. Mol. Cell. Biol., 84: 155–161, 1984.Google Scholar
  3. 3.
    Sohal, RS, and Allen, RG: Oxidative stress as a causal factor in differentiation and aging: a unifying hypothesis. Exp. Geront., 25: 499–522, 1990.CrossRefGoogle Scholar
  4. 4.
    Sohal, RS, Svensson, I, and Brunk, UT: Hydrogen peroxide production by liver mitochondria in different species. Mech. Ageing Dev., 53: 209–215, 1990.PubMedCrossRefGoogle Scholar
  5. 5.
    Sohal, RS, Arnold, LA, and Sohal, BH: Age-related changes in antioxidant enzymes and prooxidant generation in tissues of the rat with special reference to parameters in two insect species. Free Radic. Biol. Med., 9: 495–500, 1990.PubMedCrossRefGoogle Scholar
  6. 6.
    Kong, S, and Davidson, AJ: The role of the interactions between O2, H2O2, OH, e, and ′O2 in the free radical damage to biological systems. J. Biol. Chem., 204: 18–29, 1980.Google Scholar
  7. 7.
    Friguet, B, Stadtman, ER, and Szweda, LI: Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease. J. Biol. Chem., 269: 21639–21643, 1994.Google Scholar
  8. 8.
    Stadtman, ER, Oliver, CN, Starke-Reed, PE, and Rhee, SG: Age-related oxidation reaction in proteins. Toxicology & Industrial Health, 9: 187–196, 1993.Google Scholar
  9. 9.
    Stadtman, ER: Protein modification in aging. J. Gerontol., 43: B112–B120, 1988.PubMedGoogle Scholar
  10. 10.
    Stadtman, ER: Covalent modification reactions are marking steps in protein turnover. Biochemistry, 29: 6323–6331, 1990.PubMedCrossRefGoogle Scholar
  11. 11.
    Stadtman, ER: Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Ann. Rev. Biochem., 62: 797–821, 1993.PubMedCrossRefGoogle Scholar
  12. 12.
    Szweda, LI, Uchida, K, Tsai, L, and Stadtman, ER: Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Selective modification of an active-site lysine. J. Biol. Chem., 268: 3342–3347, 1993.PubMedGoogle Scholar
  13. 13.
    Agarwal, S, and Sohal, RS: Relationship between aging and susceptability to protein oxidative damage. Biochem. Biophys. Res. Commun., 194: 1203–1206, 1993.PubMedCrossRefGoogle Scholar
  14. 14.
    Brawn, K, and Fridovich, I: Superoxide radical and superoxide dismutases: threat and defense. Acta Physiol. Scand. Suppl., 492: 9–18, 1980.PubMedGoogle Scholar
  15. 15.
    Newton, RK, Ducore, JM, and Sohal, RS: Effect of age on endogenous DNA single-strand breakage, strand break induction and repair in the adult housefly, Musca domestica. Mut. Res., 219: 113–120, 1989.Google Scholar
  16. 16.
    Agarwal, S, and Sohal, RS: DNA oxidative damage and life expectancy in houseflies. Proc. Natl. Acad. Sci. USA, 91: 12332–12335, 1994.Google Scholar
  17. 17.
    von Zglinicki, T, Saretzki, G, Döcke, W, and Lotze, C: Mild hyperoxia shortens telomeres and inhibits proliferation of fibroblasts: a model for senescence? Exp. Cell Res., 220: 186–192, 1995.CrossRefGoogle Scholar
  18. 18.
    Yakes, FM, and Houten, BV: Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc. Natl. Acad. Sci. USA, 94: 514–519, 1997.PubMedCrossRefGoogle Scholar
  19. 19.
    Reid, TM, and Loeb, LA: Tandem double CC → TT mutations are produced by reactive oxygen species. Proc. Natl. Acad. Sci. USA, 90: 3904–3907, 1993.PubMedGoogle Scholar
  20. 20.
    Ammendola, R, Mesuraca, M, Russo, T, and Cimino, F: Sp1 DNA binding efficiency is highly reduced in nuclear extracts from aged rat tissues. J. Biol. Chem., 267: 17944–17948, 1992.Google Scholar
  21. 21.
    Ammendola, R, Mesuraca, M, Russo, T, and Cimino, F: The DNA binding efficiency of Sp1 is affected by redox changes. Eur. J. Biochem., 225: 483–489, 1994.PubMedCrossRefGoogle Scholar
  22. 22.
    Pryor, WA: The role of free radical reactions in biological systems, in Free Radicals in Biology, edited by Pryor, WA, Academic Press, New York, 1976, pp. 1–49.Google Scholar
  23. 23.
    Rosen, GM, Barber, MJ, and Rauckman, EJ: Disruption of erythrocyte membrane organization by superoxide. J. Biol. Chem., 258: 2225–2228, 1983.PubMedGoogle Scholar
  24. 24.
    Uchida, K, Toyokuni, S, Nishikawa, K, Kawakishi, S, Oda, H, Hiai, H, and Stadtman, ER: Michael addition-type 4-hydroxy-2-nonenal adducts in modified low-density lipoproteins: markers for atherosclerosis. Biochemistry, 33: 12487–12494, 1994.Google Scholar
  25. 25.
    Kramer, JH, Arroyo, CM, Dickens, BF, and Weglicki, WB: Spin-trapping evidence that graded myocardial ishemia alters post-ischemic superoxide production. Free Radic. Biol. Med., 3: 153–159, 1987.PubMedGoogle Scholar
  26. 26.
    McCord, JM: Oxygen-derived free radicals in postischemic tissue injury. N. Engl. J. Med., 312: 159–163, 1985.PubMedCrossRefGoogle Scholar
  27. 27.
    Darley-Usmar, VM, Smith, DR, O’Leary, H, DLVJ, Stone, D, and Clark, JB: Hyperoxia-reoxygenation induced damage in the myocardium: the role of mitochondria. Biochem. Soc. Trans., 18: 526–528, 1990.PubMedGoogle Scholar
  28. 28.
    Oberley, LW: Superoxide dismutases in cancer, in Superoxide Dismutase, edited by Oberley, LW, Boca Raton, FL, CRC Press, 1983, pp. 127–165.Google Scholar
  29. 29.
    Oberley, LW, and Oberley, TD: The role of superoxide dismutase and gene amplification in carcinogenesis. J. Theor. Biol., 106: 403–422, 1984.PubMedCrossRefGoogle Scholar
  30. 30.
    Weitzman, S, Schmeichel, C, Turk, P, Stevens, C, Tolsma, S, and Bouck, N: Phagocyte-mediated carcinogenesis: DNA from phagocyte transformed C3H T10 1/2 cells can transform NIH/3T3 cells, in Membrane in Cancer Cells, edited by Galeotti, T, Cittadini, A, Neri, G, and Scarpa, A, New York, Annals of the New York Academy of Sciences, 1988, pp. 103–110.Google Scholar
  31. 31.
    Safford, SE, Oberley, TD, Urano, M, and St. Clair, DK: Suppression of fibrosarcoma metastasis by elevated expression of manganese superoxide dismutase. Cancer Res., 54: 4261–4265, 1994.PubMedGoogle Scholar
  32. 32.
    McCord, JM, and Fridovich, I: Superoxide dismutase. J. Biol. Chem., 244: 6049–6055, 1969.PubMedGoogle Scholar
  33. 33.
    Halliwell, B: Free radicals, oxygen toxicity and aging, in Age Pigments, edited by Sohal, RS, Amsterdam, Elsevier/North Holland, 1981, pp. 1–62.Google Scholar
  34. 34.
    Foreman, HJ, and Fischer, AB: Antioxidant defenses, in Oxygen and Living Processes, edited by Gilbert, DL, New York, Springer-Verlag, 1981, pp. 65–90.Google Scholar
  35. 35.
    Allen, RG, and Balin, AK: Oxidative influence on development and differentiation: an overview of a free radical theory of development. Free Radic. Biol. Med., 6: 631–661, 1989.PubMedCrossRefGoogle Scholar
  36. 36.
    Allen, RG: Oxygen-reactive species and antioxidant responses during development: the metabolic paradox of cellular differentiation. Proc. Soc. Exp. Biol. Med., 196: 117–129, 1991.PubMedGoogle Scholar
  37. 37.
    Allen, RG: Role of free radicals in senescence, in Annual Review of Gerontology and Geriatrics, edited by Cristofalo, VJ, and Lawton, MP, New York, Springer Publishing Co., 1990, pp. 198–213.Google Scholar
  38. 38.
    Oberley, LW, and Oberley, TD: Free radicals cancer and aging, in Free Radicals, Aging and Degenerative Diseases, edited by Johnson, JE, Walford, R, Harman, D, and Miquel, J, New York, Alan R. Liss, Inc., 1986, pp. 325–371.Google Scholar
  39. 39.
    Beyer, W, Imlay, J, and Fridovich, I: Superoxide dismutases. Prog. Nucl. Acid Res. Mol. Biol., 40: 221–253, 1991.Google Scholar
  40. 40.
    Keller, G-A, Warner, TG, Steimer, KS, and Hallewell, RA: Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells. Proc. Natl. Acad. Sci. USA, 88: 7381–7385, 1991.PubMedGoogle Scholar
  41. 41.
    Dhaunsi, GS, Gulati, S, Singh, AK, Orak, JH, Asayama, K, and Singh, I: Demonstration of Cu-Zn superoxide dismutase in rat liver peroxisomes. J. Biol. Chem., 267: 6870–6873, 1992.PubMedGoogle Scholar
  42. 42.
    Steinman, HM: Superoxide dismutase: protein chemistry and structure-function relationships, in Superoxide Dismutase, edited by Oberley, LW, Boca Raton, FL, CRC Press, 1982, pp. 11–68.Google Scholar
  43. 43.
    Marklund, SL: Extracellular superoxide dismutase in human tissues and human cell lines. J. Clin. Invest., 74: 1398–1403, 1984.PubMedGoogle Scholar
  44. 44.
    Sohal, RS: The free radical hypothesis of aging: an appraisal of the current status. Aging, 5: 3–17, 1993.PubMedGoogle Scholar
  45. 45.
    Mehlhorn, RJ, and Cole, G: The free radical theory of aging: a critical review. Adv. Free Rad. Biol. Med., 1: 165–223, 1985.CrossRefGoogle Scholar
  46. 46.
    Allen, RG: Free radicals and differentiation: the interrelationship of development and aging, in Free Radicals in Aging, edited by Yu, BP, Boca Raton, FL, CRC Press, 1993, pp. 11–37.Google Scholar
  47. 47.
    Newton, RK, Ducore, JM, and Sohal, RS: Relationship between life expectancy and endogenous DNA single-strand breakage, strand break induction and DNA repair capicity in the adult housefly, Musca clomestica. Mech. Ageing Dev., 49: 259–270, 1989.PubMedCrossRefGoogle Scholar
  48. 48.
    McCord, JM: Human disease, free radicals, and the oxidant/antioxidant balance. Clin. Biochem, 26: 351–357, 1993.PubMedCrossRefGoogle Scholar
  49. 49.
    Leff, JA, Parsons, PE, Day, CE, Taniguchi, N, Jochum, M, Fritz, H, Moore, FA, Moore, EE, McCord, JM, and Repine, JE: Serum antioxidants as predictors of adult respiratory distress syndrome in patients with sepsis. Lancet, 341: 777–780, 1993.PubMedCrossRefGoogle Scholar
  50. 50.
    McCord, JM, Gao, B, Left, J, and Flores, SC: Neutrophil-generated free radicals: possible mechanisms of injury in adult respiratory distress syndrome. Env. Health Per., 102Supp 110: 57–60, 1994.Google Scholar
  51. 51.
    Oberley, LW: Free radicals and diabetes. Free Radic. Biol. Med., 5: 113–124, 1988.PubMedCrossRefGoogle Scholar
  52. 52.
    Kubisch, HM, Wang, J, Luche, R, Carlson, E, Bray, TM, Epstein, CJ, and Phillips, JP: Transgenic copper/zinc superoxide dismutase modulates susceptibility to type I diabetes. Proc. Natl. Acad. Sci. USA, 91: 9956–9959, 1994.PubMedGoogle Scholar
  53. 53.
    Asayama, K, Uchida, N, Nakane, T, Hayashibe, H, Dobashi, K, Amemiya, S, Kato, K, and Nakazawa, S: Antioxidants in the serum of children with insulin-dependent diabetes mellitus. Free Radic. Biol. Med., 15: 597–602, 1993.PubMedCrossRefGoogle Scholar
  54. 54.
    Juurlink, BHJ: Response of glial cells to ischemia-roles of reactive oxygen species and glutathione. Neuroscience & Biobehavioral Reviews, 21: 151–166, 1997.CrossRefGoogle Scholar
  55. 55.
    Mikawa, S, Sharp, FR, Kamii, H, Kinouchi, H, Epstein, CJ, and Chan, PH: Expression of c-fos and hsp70 mRNA after tramatic brain injury in transgenic mice overexpressing Cu/Zn-superoxide dismutase. Mol. Brain Res., 33: 288–294, 1995.PubMedCrossRefGoogle Scholar
  56. 56.
    Fabia, R, Ar’Rajab. Willen, R, Marklund, S, and Andersson, R: The role of transient mucosal ischemia in acetic acid-induced colitis in the rat. J. Surg. Res., 63: 406–412, 1996.PubMedCrossRefGoogle Scholar
  57. 57.
    Ishimoto, H, Natori, M, Tanaka, M, Miyazaki, T, Kobayashi, T, and Yoshimura, Y: Role of oxygen-derived free radicals in free growth retardation induced by ischemia-reperfusion in rats. Am. J. Physiol., 272: H701–H705, 1997.PubMedGoogle Scholar
  58. 58.
    Yamanoi, A, Nagasue, N, Kohno, H, Kimoto, T, and Nakamura, T: Clinical and enzymatic investigation of induction of oxygen free radicals by ischemia and reperfusion in human hepatocellular carcinoma and adjacent liver. HPB Surgery, 8: 193–199, 1995.PubMedGoogle Scholar
  59. 59.
    Hirano, T, Furuyama, H, Kawakami, Y, Ando, K, and Tsuchitani, T: Protective effects of prophylaxis with a protease inhibitor and a free radical scavenger against a temporary ischemia model of pancreatitis. Can. J. Surg., 38: 241–248, 1995.PubMedGoogle Scholar
  60. 60.
    Pisarenko, OI, Studneva, IM, Lakomkin, VL, Timoshin, AA, and Kapelko, VI: Human recombinant extracellular-superoxide dismutase type C improves cardioplegic protection against ischemia/reperfusion injury in isolated rat heart. Journal of Cardiovascular Pharmacology, 24: 655–663, 1994.PubMedGoogle Scholar
  61. 61.
    Karwinski, W, Bolann, B, Ulvik, R, Farstad, M, and Soreide, O: Normothermic liver ischemia in rats: xanthine oxidase is not the main source of oxygen free radicals. Res. Exp. Med., 193: 275–283, 1993.Google Scholar
  62. 62.
    Yoritaka, A, Hattori, N, Uchida, K, Tanaka, M, Stadtman, ER, and Mizuno, Y: Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc. Natl. Acad. Sci. USA, 93: 2696–2701, 1996.PubMedCrossRefGoogle Scholar
  63. 63.
    Nelson, SK, Wong, GH, and McCord, JM: Leukemia inhibitory factor and tumor necrosis factor induce manganese superoxide dismutase and protect rabbit hearts from reperfusion injury. J. Mol. Cell. Cardiol., 27: 223–229, 1995.PubMedGoogle Scholar
  64. 64.
    Chan, PH, Epstein, CJ, Kinouchi, H, Kamii, H, Chen, SF, Carlson, E, Gafni, J, Yang, G, and Reola, L: Neuroprotective role of CuZn-superoxide dismutase in ischemic brain damage. Adv. Neurol., 71: 271–280, 1996.PubMedGoogle Scholar
  65. 65.
    Karlsson, K, Sandstrom, J, Edlund, A, Edlund, T, and Marklund, SL: Pharmacokinetics of extracellular-superoxide dismutase in the vascular system. Free Radic. Biol. Med., 14: 185–190, 1993.PubMedCrossRefGoogle Scholar
  66. 66.
    Omar, BA, and McCord, JM: The cardioprotective effect of Mn-superoxide dismutase is lost at high doses in the postischemic isolated rabbit heart. Free Radic. Biol. Med., 9: 473–478, 1990.PubMedCrossRefGoogle Scholar
  67. 67.
    Omar, BA, Gad, NM, Jordan, MC, Striplin, SP, Russell, WJ, Downey, JM, and McCord, JM: Cardioprotection by Cu,Zn-superoxide dismutase is lost at high doses in the reoxygenated heart. Free Radic. Biol. Med., 9: 465–471, 1990.PubMedCrossRefGoogle Scholar
  68. 68.
    Matsuo, M: Age-related alterations in antioxidant defense, in Free Radicals in Aging, edited by Yu, BP, Boca Raton, FL, CRC Press, 1993, pp. 143–181.Google Scholar
  69. 69.
    Noy, N, Schwartz, H, and Gafni, A: Age-related changes in the redox status of rat muscle cells and their role in enzyme aging. Mech. Ageing Dev., 29: 63–69, 1985.PubMedCrossRefGoogle Scholar
  70. 70.
    Sohal, RS, Farmer, KJ, Allen, RG, and Cohen, NR: Effects of age on oxygen consumption, superoxide dismutase, catalase, glutathione, inorganic peroxides, and chloroform-soluble antioxidants in the adult male housefly, Musca domestica. Mech. Ageing Dev., 24: 185–195, 1983.CrossRefGoogle Scholar
  71. 71.
    Sohal, RS, Svensson, I, Sohal, BH, and Brunk, UT: Superoxide radical production in different animal species. Mech. Ageing Dev., 49: 129–135, 1989.PubMedCrossRefGoogle Scholar
  72. 72.
    Farmer, KJ, and Sohal, RS: Relationship between superoxide anion generation and aging in the housefly, Musca domestica. Free Radic. Biol. Med., 7: 23–29, 1989.PubMedCrossRefGoogle Scholar
  73. 73.
    Nohl, H, and Hegner, D: Do mitochondria produce oxygen radicals in vivo? Eur. J. Biochem., 82: 563–567, 1978.PubMedCrossRefGoogle Scholar
  74. 74.
    Nohl, H: Oxygen release in mitochondria: influence of age, in Free Radicals, Aging, and Degenerative Disease, edited by Johnson, JE, Walford, R, Harman, D, and Miquel, J, New York, Alan Liss, 1986, pp. 79–97.Google Scholar
  75. 75.
    Hegner, D: Age-dependence of molecular and functional changes in biological membranes. Mech. Ageing Dev., 14: 101–118, 1980.PubMedCrossRefGoogle Scholar
  76. 76.
    Ku, H-H, Brunk, UT, and Sohal, RS: Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species. Free Radic. Biol. Med., 15: 621–627, 1993.PubMedCrossRefGoogle Scholar
  77. 77.
    Allen, RG, Farmer, KJ, and Sohal, RS: Effect of catalase inactivation on the levels of inorganic peroxides, superoxide dismutase, glutathione, oxygen consumption and life span in adult houseflies. (Musca domestica). Biochem. J., 216: 503–506, 1983.PubMedGoogle Scholar
  78. 78.
    Sohal, RS: Aging, cytochrome oxidase activity, and hydrogen peroxide release by mitochondria. Free Radic. Biol. Med., 14: 583–588, 1993.PubMedCrossRefGoogle Scholar
  79. 79.
    Sohal, RS, and Sohal, BH: Hydrogen peroxide release by mitochondria increases during aging. Mech. Ageing Dev., 57: 187–202, 1991.PubMedCrossRefGoogle Scholar
  80. 80.
    Lang, CA, Naryshkin, S, Schneider, DL, Mills, BJ, and Linderman, RD: Low blood glutathione levels in healthy aging adults. J. Lab. Clin. Med., 120: 720–725, 1992.PubMedGoogle Scholar
  81. 81.
    Rikans, LE, and Moore, DR: Effects of aging on aqueous-phase antioxidants in tissues of male Fischer rats. Biochim. Biophys. Acta., 966: 269, 1988.PubMedGoogle Scholar
  82. 82.
    Orr, WC, and Sohal, RS: Extension of lifespan by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science, 263: 1128–1130, 1994.PubMedGoogle Scholar
  83. 83.
    Sohal, RS, Agarwal, A, Agarwal, S, and Orr, WC: Simultaneous overexpression of copper-and zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster. J. Biol. Chem., 270: 15671–15674, 1995.Google Scholar
  84. 84.
    Benzi, G, Pastoris, O, Marzatico, RF, Villa, RF, and Curti, D: The mitochondrial electron transfer alterations as a factor involved in brain aging. Neurobiol. Aging, 13: 361–368, 1992.PubMedCrossRefGoogle Scholar
  85. 85.
    Sugiyama, S, Takasawa, M, Hayakawa, M, and Ozawa, T: Changes in skeletal muscle, heart and liver mitochondrial electron transport activities in rats and dogs of various ages. Biochem. Mol. Biol. Int., 30: 937–944, 1993.PubMedGoogle Scholar
  86. 86.
    Boffoli, D, Scacco, SC, Vergari, R, Persio, MT, Solarino, G, Laforgia, R, and Papa, S: Ageing is associated in females with a decline in the content and activity of the b-c 1 complex in skeletal muscle mitochondria. Biochim. Biophys. Acta., 1315: 66–72, 1996.PubMedGoogle Scholar
  87. 87.
    Boffoli, D, Scacco, SC, Vergari, R, Solarino, G, Santacroce, G, and Papa, S: Decline with age of the respiratory chain activity in human skeletal muscle. Biochim. Biophys. Acta., 1226: 73–82, 1994.PubMedGoogle Scholar
  88. 88.
    Hayashi, J-I, Ohta, S, Kagawa, Y, Kondo, H, Kaneda, H, Yonekawa, H, Takai, D, and Miyabayashi, S: Nuclear but not mitochondrial genome involvement in human age-related mitochondrial dysfunction. J. Biol. Chem., 269: 6878–6883, 1994.PubMedGoogle Scholar
  89. 89.
    Brierley, EJ, Johnson, MA, James, OFW, and Turnbull, DM: Mitochondrial involvement in the ageing process, facts and controversies. Mol. Cell. Biochem., 174: 325–328, 1997.PubMedCrossRefGoogle Scholar
  90. 90.
    Paradies, G, and Ruggiero, FM: Effect of aging on the activity of the phosphate carrier and on the lipid composition in rat liver mitochondria. Arch. Biochem. Biophys., 284: 332–337, 1991.PubMedCrossRefGoogle Scholar
  91. 91.
    Vorbeck, ML, Martin, AP, Long, JW, Smith, JM, and Orr, RR: Aging-dependent modification of lipid composition and lipid structural order of hepatic mitochondria. Arch. Biochem. Biophys., 217: 351–361, 1982.PubMedCrossRefGoogle Scholar
  92. 92.
    Paradies, G, Ruggiero, M, and Dinoi, P: Decreased activity of the phosphate carrier and modification of lipids in cardiac mitochondria from senescent rats. Int. J. Biochem., 24: 783–787, 1992.PubMedCrossRefGoogle Scholar
  93. 93.
    Paradies, G, Ruggiero, FM, Petrosillo, G, Gadaleta, MN, and Quagliariello, E: Effects of aging and acetyl-L-carnitine on the activity of cytochrome oxidase and adenine nucleotide translocase in rat heart mitochondria. FEBS Lett., 350: 213–215, 1994.PubMedCrossRefGoogle Scholar
  94. 94.
    Paradies, G, Ruggiero, FM, Gadaleta, MN, and Quagliariello, E: Effects of aging and acetyI-L-carnitine on the activity of the phosphate carrier and on the phospholipid composition in rat heart mitochondria. Biochim. Biophys. Acta., 1103: 324–326, 1992.PubMedGoogle Scholar
  95. 95.
    Hansford, RG, Hogue, BA, and Mildaziene, V: Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age. Journal of Bioenergetics & Biomembranes, 29: 89–95, 1997.CrossRefGoogle Scholar
  96. 96.
    Zhan, H, Sun, C-P, Liu, C-G, and Zhou, J-H: Age-related change of free radical generation in liver and sex glands of rats. Mech. Ageing Dev., 62: 111–116, 1992.PubMedCrossRefGoogle Scholar
  97. 97.
    Yu, BP, and Yang, R: Critical elvaluation of the free radical theory: a proposal for the oxidative stress hypothesis. Ann. New York Acad. Sci., 786: 1–11, 1996.Google Scholar
  98. 98.
    Beal, MF: Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol., 38: 357–366, 1995.PubMedCrossRefGoogle Scholar
  99. 99.
    Bowling, AC, and Beal, MF: Bioenergetic and oxidative stress in neurodegenerative disease. Life Sci., 56: 1151–1171, 1995.PubMedCrossRefGoogle Scholar
  100. 100.
    Eisen, A: Amyotrophic lateral sclerosis is a multifactorial disease. Muscle and Nerve, 18: 741–752, 1995.PubMedCrossRefGoogle Scholar
  101. 101.
    Anderson, PL, Forsgren, L, Binzer, M, Nilsson, P, Ala-Hurula, V, Keränen, M-L, Bergmark, L, Saarinen, A, Haltia, T, Tarvainen, I, Kinnunen, E, Udd, B, and Marklund, SL: Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation: A clinical and genealogical study of 36 patients. Brain, 119: 1153–1172, 1996.Google Scholar
  102. 102.
    Gusella, JF, Wexler, NS, Conneally, PM, Naylor, SL, Anderson, MA, Tanzi, RE, Watkins, PC, Ottina, K, Wallace, MR, Sakaguchi, AY, Young, AB, Shoulson, I, Bonilla, E, and Martin, JB: A polymorphic DNA marker genetically linked to Huntington’s disease. Nature, 306: 234–238, 1983.PubMedCrossRefGoogle Scholar
  103. 103.
    Aoki, M, Abe, K, Houi, K, Ogasawara, M, Matsubara, Y, Kobayashi, T, Mochio, S, Narisawa, K, and Itoyama: Variance of age at onset in a Japanese family with amyotrophic lateral sclerosis associated with a novel Cu/Zn superoxide dismutase mutation. Ann. Neurol., 37: 676–679, 1995.PubMedCrossRefGoogle Scholar
  104. 104.
    Eisen, AA: Amyotrophic lateral sclerosis: a multifactorial disease. Adv. Neurol., 68: 121–134, 1995.PubMedGoogle Scholar
  105. 105.
    Curti, D, Malaspina, A, Facchetti, G, Camana, C, Mazzini, L, Tosca, MD, Zerbi, F, and Ceroni, M: Amytrophic lateral sclerosis: oxidative energy metabolism and calcium homeostasis in peripheral blood lymphocytes. Neurol., 47: 1060–1064, 1996.Google Scholar
  106. 106.
    Chandrasekaran, K, Giordano, T, Brady, DR, Stoll, J, Martin, LJ, and Rapoport, SI: Impairment in mitochondrial cytochrome oxidase gene expression in Alzheimer disease. Mol. Brain Res., 24: 336–340, 1994.PubMedCrossRefGoogle Scholar
  107. 107.
    Mutisya, EM, Bowling, AC, and Beal, MF: Cortical cytochrome oxidase activity is reduced in Alzheimer’s disease. J. Neurochem., 63: 2179–2184, 1994.PubMedCrossRefGoogle Scholar
  108. 108.
    Bowling, AC, Schulz, JB, Brown, RH, and Beal, MF: Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem., 61: 2322–2325, 1993.PubMedGoogle Scholar
  109. 109.
    Fujita, K, Yamauchi, M, Shibayama, K, Ando, M, Hondo, M, and Nagata, Y: Decreased cytochrome c oxidase activity but unchanged superoxide dismutase and glutathione peroxidase activities in the spinal cords of patients with amyotrophic lateral sclerosis. J. Neurosci. Res., 45: 276–281, 1996.PubMedCrossRefGoogle Scholar
  110. 110.
    Hosler, BA, and Brown, RH: Copper/Zinc superoxide dismutase mutations and free radical damage in amyotrophic lateral sclerosis. Adv. Neurol., 68: 41–46, 1995.PubMedGoogle Scholar
  111. 111.
    Schapira, AHV: Oxidative stress and mitochondrial dysfunction in neurodegeneration. Curr. Opin. Neurol., 9: 260–264, 1996.PubMedGoogle Scholar
  112. 112.
    Simonian, NA, and Coyle, JT: Oxidative stress in neurodegenerative disease. Annu. Rev. Pharmacol. Toxicol., 36: 83–106, 1996.PubMedCrossRefGoogle Scholar
  113. 113.
    Bergeron, C: Oxidative stress: its role in the pathogenesis of amyotrophic lateral sclerosis. J. Neurol. Sci., 129(Suppl.): 81–84, 1995.PubMedCrossRefGoogle Scholar
  114. 114.
    Rosen, DR, Siddique, T, Patterson, D, Figlewics, DA, Snapp, P, Hentati, A, Donaldson, D, Goto, J, Deng, H-X, Rahmani, Z, Krizus, A, McKenna-Yasek, D, Cayabyab, A, Gaston, SM, Berger, R, Tanzi, RE, Halperin, JJ, Hertzfeldt, B, Van der Bergh, R, Hung, W-Y, Bird, T, Deng, G, Mulder, DW, Smyth, C, Laing, NG, Soriano, E, Pericak-Vance, MA, Haines, J, Rouleau, GA, Gusella, JS, Horvitz, HR, and Brown, RH: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature, 362: 59–62, 1993.PubMedCrossRefGoogle Scholar
  115. 115.
    Cudkowicz, ME, and Brown, RH: An update on superoxide dismutase 1 in familial amyotrophic lateral sclerosis. J. Neurol. Sci., 139(Suppl.): 10–15, 1996.PubMedCrossRefGoogle Scholar
  116. 116.
    Mulder, DW, Kurland, LT, Offord, KP, and Beard, CM: Familial adult motor neuron disease: amyotrophic lateral sclerosis. Neurol., 36: 511–517, 1986.Google Scholar
  117. 117.
    Przedborski, S, Dhawan, V, Donaldson, DM, Murphy, PL, McKenna-Yasek, D, Mandel, FS, Brown, RH, and Eidelberg, D: Nigrostriatal dopaminergic function in familial amyotrophic lateral sclerosis patients with and without copper/zinc superoxide dismutase mutations. Neurol., 47: 1546–1551, 1996.Google Scholar
  118. 118.
    Radunovic, A, and Leigh, PN: Cu/Zn superoxide dismutase gene mutations in amyotrophic lateral sclerosis: correlation between genotype and clinical features. J. Neurol. Neurosurg. Psychiatry, 61: 565–572, 1996.PubMedGoogle Scholar
  119. 119.
    Orrell, RW, King, AW, Hilton, DA, Campbell, MJ, Lane, RJM, and de Belleroche, JS: Familial amyotrophic lateral sclerosis with a point mutation of SOD-1: intrafamilial heterogeneity of disease duration associated with neurofibrillary tangles. J. Neurol. Neurosurg. Psychiatry, 59: 266–270, 1995.PubMedGoogle Scholar
  120. 120.
    Rouleau, GA, Clark, AW, Rooke, K, Pramatarova, A, Krizus, A, Suchowersky, O, Julien, J-P, and Figlewicz, D: SOD1 mutation is associated with accumulation of neurofilaments in amyotrophic lateral sclerosis. Ann. Neurol., 39: 128–131, 1996.PubMedCrossRefGoogle Scholar
  121. 121.
    Calder, VL, Domigan, NM, George, PM, Donaldson, IM, and Winterbourn, CC: Superoxide dismutase (glu100→gly) in a family with inherited neuron disease: detection of mutant superoxide dismutase activity and the presence of heterodimers. Neurosci. Lett., 189: 143–146, 1995.PubMedCrossRefGoogle Scholar
  122. 122.
    Hosler, BA, Nicholson, GA, Sapp, PC, Chin, W, Orrell, RW, de Belleroche, JS, Esteban, J, Hayward, LJ, McKenna-Yasek, D, Yeung, L, Cherryson, AK, Dench, JE, Wilton, SD, Laing, NG, Horvitz, RH, and Brown, RH: Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis. Neuromusc. Disord., 6: 361–366, 1996.PubMedCrossRefGoogle Scholar
  123. 123.
    Luche, RM, Maiwald, R, Carlson, EJ, and Epstein, CJ: Novel mutations in an otherwise strictly conserved domain of CuZn superoxide dismutase. Mol. Cell. Biochem., 168: 191–194, 1997.PubMedCrossRefGoogle Scholar
  124. 124.
    Deng, H-X, Hentati, A, Tainer, JA, Iqbal, Z, Cayabyab, A, Hung, W-Y, Getzoff, ED, Hu, P, Herzfeldt, B, Roos, RP, Warner, C, Deng, G, Soriano, E, Smyth, C, Parge, HE, Ahmed, A, Roses, AD, Hallewell, RA, Pericak-Vance, MA, and Siddique, T: Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science, 261: 1047–1051, 1993.PubMedGoogle Scholar
  125. 125.
    Wiedau-Pazos, M, Goto, JJ, Rabizadeh, S, Gralla, EB, Roe, JA, Lee, MK, Valentine, JS, and Bredesen, DE: Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science, 271: 515–517, 1996.PubMedGoogle Scholar
  126. 126.
    Shibata, N, Hirano, A, Kobashi, M, Siddique, T, Deng, H-X, Hung, W-Y, Kato, T, and Asayama, K: Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. J. Neuropath. Exp. Neurol., 55: 481–490 1996.PubMedGoogle Scholar
  127. 127.
    Nakano R, Sato, S, Inuzuka, T, Sakimura, K, Mishina M, Takahashi, H, Ikuta, F, Honma, Y, Fuji, J, Taniguchi, N, and Tsui, S: A novel mutation in Cu/Zn superoxide dismutase gene in Japanese familial amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun., 200: 695–703, 1994.PubMedCrossRefGoogle Scholar
  128. 128.
    Nakano, R, Inuzuka, T, Kikugawa, K, Takahashi, H, Sakimura, K, Fujji, J, Taniguchi, N, and Tsuji, S: Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis. Neurosci. Lett., 211: 129–131, 1996.PubMedCrossRefGoogle Scholar
  129. 129.
    Morita, M, Aoki, M, Abe, K, Hasegawa, T, Sakuma, R, Onodera, Y, Ichikawa, N, Nishizawa, M, and Itoyama, Y: A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan. Neurosci. Lett., 205: 79–82, 1996.PubMedCrossRefGoogle Scholar
  130. 130.
    Deng, HX, Tainer, JA, Mitsuamoto, H, Ohnishi, A, He, X, Hung, WY, Zhao, Y, Juneja, T, Henati, A, and Siddique, T: Two novel SOD1 mutations in patients with familial amyotrophic lateral sclerosis. Hum. Mol. Genet., 4: 1113–1116, 1995.PubMedGoogle Scholar
  131. 131.
    Jones, CT, Swingler, RJ, and Brock, DJ: Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of IIe 113Thr in three others. Hum. Mol. Genet., 3: 649–650, 1994.PubMedGoogle Scholar
  132. 132.
    Aoki, M, Ogasawara, M, Matsubara, Y, Narisawa, K, Nakamura, S, Itoyama, Y, and Abe, K: Mild ALS in japan associated with novel SOD mutation. Nature Genetics, 5: 323–324, 1993.PubMedCrossRefGoogle Scholar
  133. 133.
    Abe, K, Aoki, M, Ikeda, M, Watanabe, M, Hirai, S, and Itoyama, Y: Clinical characteristics of familial amyotrophic lateral sclerosis with Cu/Zn superoxide dismutase gene mutations. J. Neurol. Sci., 136: 108–116, 1996.PubMedCrossRefGoogle Scholar
  134. 134.
    Enayat, ZE, Orrell, RW, Claus, A, Ludolph, A, Bachus, R, Brockmüller, J, Ray-Chaudhri, K, Radunovic, A, Shaw, C, Wilkinson, J, Swash, M, Leigh, PN, de Belleroche, J, and Powell, J: Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis. Hum. Mol. Genet., 4: 1239–1240, 1995.PubMedGoogle Scholar
  135. 135.
    Kunst, CB, Mezey, E, Brownstein, MJ, and Patterson, D: Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions. Nature Genetics, 15: 91–94, 1997.PubMedCrossRefGoogle Scholar
  136. 136.
    Själander, A, Beckman, G, Deng, H-X, Iqbal, Z, Tainer, JA, and Siddique, T: The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in northern Sweden and Finland. Hum. Mol. Genet., 4: 1105–1108, 1995.PubMedGoogle Scholar
  137. 137.
    Anderson, PM, Nilsson, P, Ala-Hurula, V, Keränen, M-L, Tarvainer, I, Hultia, T, Nilsson, L, Binzer, M, Forsgren, L, and Marklund, SL: Amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala mutation in CuZn-superoxide dismutase. Nature Genetics, 10: 61–65, 1995.CrossRefGoogle Scholar
  138. 138.
    Robberecht, W, Aguirre, T, Bosch, VD, Tilkin, P, Cassiman, JJ, and Matthijs, G: D90A heterozygosity in the SOD1 gene is associated with familial and apparently sporadic amyotrophic lateral sclerosis. Neurol., 47: 1336–1339, 1996.Google Scholar
  139. 139.
    Esteban, J, Rosen, DR, Bowling, AC, Sapp, P, McKenna-Yasek, D, O’Regan, JP, Beal, MF, Horowitz, HR, and Brown, RH: Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclerosis. Hum. Mol. Genet., 3: 997–998, 1994.PubMedGoogle Scholar
  140. 140.
    Elshafey, A, Lanyon, WG, and Connor, JM: Identification of a new missense point mutation in exon 4 of the Cu/Zn superoxide dismutase (SOD-1) gene in a family with amyotrophic lateral sclerosis. Hum. Mol. Genet., 3: 363–364, 1994.PubMedGoogle Scholar
  141. 141.
    Jones, CT, Swingle, RJ, Simpson, SA, and Brock, DJH: Superoxide dismutase mutations in an unselected cohort of Scottish amyotrophic lateral sclerosis patients. J. Mol. Genet., 32: 290–292, 1995.Google Scholar
  142. 142.
    Orrell, R, de Belleroche, J, Marklund, S, Bowe, F, and Hallewell, R: A novel SOD mutant and ALS. Nature, 374: 504–505, 1995.PubMedCrossRefGoogle Scholar
  143. 143.
    Ince, PG, Shaw, PJ, Slade, JY, Jones, C, and Hudgson, P: Familial amyotrophic lateral sclerosis with a mutation in exon 4 of the Cu/Zn superoxide dismutase gene: pathological and immunolo-cytochemical changes. Acta Neuropathol., 92: 395–403, 1996.PubMedCrossRefGoogle Scholar
  144. 144.
    Orrell, RW, Habgood, J, Rudge, P, Lane, RJM, and de Belleroche, JS: Difficulties in distinguishing sporadic from familial amyotrophic lateral sclerosis. Ann. Neurol., 39: 810–812, 1996.PubMedCrossRefGoogle Scholar
  145. 145.
    Suthers, G, Laing, N, Wilton, S, Dorosz, S, and Waddy, H: “Sporadic” motoneuron disease due to familial SOD1 mutation with low penetrance. Lancet, 344: 1773, 1994.PubMedCrossRefGoogle Scholar
  146. 146.
    Yulug, IG, Katsanis, N, de Belleroche, J, Collinge, J, and Fisher, EM: An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4. Hum. Mol. Genet., 4: 1101–1104, 1995.PubMedGoogle Scholar
  147. 147.
    Ikeda, M, Abe, K, Aoki, M, Sahara, M, Watanabe, M, Shoji, M, St. George-Hyslop, PH, Hirai, S, and Itoyama, Y: Variable clinical symptoms in familial amyotrophic lateral sclerosis witha novel point mutation in the Cu/Zn superoxide dismutase gene. Neurol., 45: 2038–2042, 1995.Google Scholar
  148. 148.
    Hayward, C, Swingler, RJ, Simpson, SA, and Brock, DJH: A specific superoxide dismutase mutation is on the same genetic background in sporadic and familial cases of amyotrophic lateral sclerosis. Am. J. Hum. Genet., 59: 1165–1167, 1996.PubMedGoogle Scholar
  149. 149.
    Kostrzewa, M, Burck-Lehmann, U, and Muller, U: Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene. Hum. Mol. Genet., 3: 2261–2264, 1994.PubMedGoogle Scholar
  150. 150.
    Pramatarova, A, Goto, J, Nanba, E, Nakashima, K, Takahashi, K, Takagi, A, Kanazawa, I, Figlewicz, DA, and Rouleau, GA: A two basepair deletion in the SOD 1 gene causes familial amyotrophic lateral sclerosis. Hum. Mol. Genet., 3: 2061–2062, 1994.PubMedGoogle Scholar
  151. 151.
    Watanabe, Y, Kono, Y, Nanba, E, Ohama, E, and Nakashima, K: Instability of expressed Cu/Zn superoxide dismutase with 2 bp deletion found in familial amyotrophic lateral sclerosis. FEBS Lett., 400: 108–112, 1997.PubMedCrossRefGoogle Scholar
  152. 152.
    Nakashima, K, Watanabe, Y, Kuno, N, Nanba, E, and Takahashi, K: Abnormality of Cu/Zn superoxide dismutase (SOD1) activity in Japanese familial amyotrophic lateral sclerosis with two base pair deletion in the SOD1 gene. Neurol., 45: 1019–1020, 1995.Google Scholar
  153. 153.
    Kato, S, Shimoda, M, Watanabe, Y, Nakashima, K, Takahashi, K, and Ohama, E: Familial amyotrophic lateral sclerosis with a two base deletion in superoxide dismutase 1 gene: multisystem degeneration with intracytoplasmic hyline inclusions in astrocytes. J. Neuropath. Exp. Neurol., 55: 1089–1101, 1996.PubMedGoogle Scholar
  154. 154.
    Pramatarova, A, Figlewicz, DA, Krizus, A, Han, FY, Ceballos-Picot, I, Nicole, A, Dib, M, Meinger, V, Brown, RH, and Rouleau, GA: Identification of new mutations in the Cu/Zn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis. Am. J. Hum. Genet., 53: 592–596, 1995.Google Scholar
  155. 155.
    Ikeda, M, Abe, K, Aoki, M, Ogasawara, M, Kameya, T, Watanabe, M, Shoji, M, Hirai, S, Hirai, S, and Itoyama, Y: A novel gene mutation in the Cu/Zn superoxide dismutase gene in a patient with familial lateral sclerosis. Hum. Mol. Genet., 4: 491–492, 1995.PubMedGoogle Scholar
  156. 156.
    Kostrzewa, M, Damian, MS, and Müller, U: Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis. Hum. Genet., 98: 48–50, 1996.PubMedCrossRefGoogle Scholar
  157. 157.
    Sapp, PC, Rosen, DR, Hosler, BA, Esteban, J, McKenna-Yasek, D, O’Regan, JP, Horvitz, HR, and Brown, RH: Identification of three novel mutations in gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis. Neuromusc. Disord., 5: 353–357, 1995.PubMedCrossRefGoogle Scholar
  158. 158.
    Parge, HE, Hallewell, RA, and Tainer, JA: Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. USA, 89: 6109–6113, 1992.PubMedGoogle Scholar
  159. 159.
    Garofalo, O, Figlewicz, DA, Thomas, SM, Butler, R, Lebuis, L, Rouleau, G, Meininger, V, and Leigh, PN: Superoxide dismutase activity in lymphoblastoid cells from motor neuron disease/amyotrophic lateral sclerosis (MNS/ALS) patients. J. Neurol. Sci., 129(Suppl.): 90–92, 1995.PubMedCrossRefGoogle Scholar
  160. 160.
    Przedborski, S, Donaldson, DM, Murphy, PL, Hirsch, O, Lange, D, Naini, AB, McKenna-Yasek, D, and Brown, RH: Blood superoxide dismutase, catalase and glutathione peroxidase activities in familial and sporadic amyotrophic lateral sclerosis. Neurodegen., 5: 57–64, 1996.CrossRefGoogle Scholar
  161. 161.
    Brown, RH: Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function. Curr. Opin. Neurobiol., 5: 841–846, 1995.PubMedCrossRefGoogle Scholar
  162. 162.
    Bowling, AC, Barkowski, EE, McKenna-Yasek, D, Sapp, P, Horvitz, HR, Beal, MF, and Brown, RH: Superoxide dismutase concentration and activity in familial amyotrophic lateral sclerosis. J. Neurochem., 64: 2366–2369, 1995.PubMedCrossRefGoogle Scholar
  163. 163.
    Brown, R: Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell, 80: 687–692, 1995.PubMedCrossRefGoogle Scholar
  164. 164.
    Vyth, A, Timmer, JG, Bossuyt, PMM, Louwerse, ES, and Vianney de Jong, JMB: Suvival in patients with amyotrophic lateral sclerosis, treated with an array of antioxidants. J. Neurol. Sci., 139(Suppl.): 99–103, 1996.PubMedCrossRefGoogle Scholar
  165. 165.
    Louwerse, ES, Weverling, GJ, Bossuyt, PMM, Meyjes, FEP, and Vianney de Jong, JMB: Randomized, double-blind, controlled trial of acetylcysteine in amyotrophic lateral sclerosis. Arch. Neurol., 52: 559–564, 1995.PubMedGoogle Scholar
  166. 166.
    Gurney, ME, Cutting, FB, Zhai, P, Doble, A, Taylor, CP, Andrus, PK, and Hall, ED: Benefit of vitamin E, riluzole and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Neurol., 39: 147–157, 1996.PubMedCrossRefGoogle Scholar
  167. 167.
    Gurney, ME, Pu, H, Chiu, AY, Dal Canto, MC, Polchow, CY, Alexander, DD, Caliendo, J, Hentati, A, Kwon, YW, Deng, H-X, Chen, W, Zhai, P, Sufit, RL, and Siddique, T: Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science, 264: 1772–1775, 1994.PubMedGoogle Scholar
  168. 168.
    Ripps, ME, Huntley, GW, Hoff, PR, Morrison, JH, and Gordon, JW: Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA, 92: 689–693, 1995.PubMedGoogle Scholar
  169. 169.
    Oberley, TD, Schultz, JL, Li, N, and Oberley, LW: Antioxidant enzyme levels as a function of growth state in cell culture. Free Radic. Biol. Med., 19: 53–65, 1995.PubMedCrossRefGoogle Scholar
  170. 170.
    Beckman, JS, Carson, M, Smith, CD, and Koppenol, WH: ALS, SOD and peroxynitrite. Nature, 364: 584, 1993.PubMedCrossRefGoogle Scholar
  171. 171.
    Beckman, JS, Ischiropoulos, H, Zhu, L, van der Woerd, M, Smith, C, Chen, J, Harrison, J, Martin, JC, and Tsai, M: Kinetics of superoxide dismutase-and iron-catalyzed nitration of phenolics by peroxynitrite. Arch. Biochem. Biophys., 298: 438–445, 1992.PubMedCrossRefGoogle Scholar
  172. 172.
    Chou, SM, Wang, HS, and Taniguchi, A: Role of SOD-1 and nitric oxide/cyclic GMP cascade on neurofilament aggregation in ALS/MND. J. Neurol. Sci., 139(Suppl.): 16–26, 1996.PubMedCrossRefGoogle Scholar
  173. 173.
    Chou, SM, Wang, HS, and Komai, K: Colocalization of NOS and SOD1 in nurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: an imm unohistochemical study. J. Chem. Neuroanat., 10: 249–258, 1996.PubMedCrossRefGoogle Scholar
  174. 174.
    Lafon-Cazal, M, Pletri, S, Culcasi, M, and Bockaert, J: NMDA-dependant superoxide production and neurotoxicity. Nature, 364: 535–537, 1983.CrossRefGoogle Scholar
  175. 175.
    Beckamn, JS: Ischaemic injury mediator. Nature, 345: 27–28, 1990.CrossRefGoogle Scholar
  176. 176.
    Rabizadeh, S, Gralla, EB, Borchelt, DR, Gwinn, R, Valentine, JS, Sisodia, S, Wong, P, Lee, M, Hahn, H, and Breedesen, DE: Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA, 92: 3024–3028, 1995.PubMedGoogle Scholar
  177. 177.
    Yim, MB, Chock, PB, and Stadtman, ER: Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J. Biol. Chem., 268: 4099–4105, 1993.PubMedGoogle Scholar
  178. 178.
    Yim, MB, Chock, PB, and Stadtman, ER: Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc. Natl. Acad. Sci. USA, 87: 5006–5010, 1990.PubMedGoogle Scholar
  179. 179.
    Yim, HS, Kang, JH, Chock, PB, Stadtman, ER, and Yim, MB: A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn-superoxide dismutase mutant has a lower KM for hydrogen peroxide. Correlation between clinical severity and the Km value. J. Biol. Chem., 272: 8861–8863, 1997.PubMedCrossRefGoogle Scholar
  180. 180.
    Yim, MB, Kang, JH, Yim, HS, Kwak, HS, Chock, PB, and Stadtman, ER: A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in KM for hydrogen peroxide. Proc. Natl. Acad. Sci. USA, 93: 5709–5714, 1996.PubMedCrossRefGoogle Scholar
  181. 181.
    Child, CM: Axial gradients in the early development of the starfish. Am. J. Physiol., 37: 203–219, 1915.Google Scholar
  182. 182.
    Child, CM: Individuation and reproduction in organisms; Senescence and Rejuvenescence. Chicago, Chicago University Press, 1915,.Google Scholar
  183. 183.
    Child, CM: Axial susceptibility gradients in the early development of the sea urchin. Biol. Bull., 30: 391–405, 1916.Google Scholar
  184. 184.
    Child, CM: Experimental control and modification of larval development in the sea urchin in relation to the axial gradients. J. Morph., 28: 65–131, 1916.CrossRefGoogle Scholar
  185. 185.
    Child, CM: Physiological dominance and physiological isolation in development and reconstitution. Wilhelm Roux. Arch. Entw. Organ., 113: 556–581, 1929.Google Scholar
  186. 186.
    Caplan, AI, and Koutroupus, S: The control of muscle and cartilage development in the chick limb: the role of differential vascularization. J. Embryol. Exp. Morph., 29: 571–583, 1973.PubMedGoogle Scholar
  187. 187.
    Loudon, C: Development of Tenebrio molitor in low oxygen levels. J. Insect Physiol., 34: 97–103, 1988.CrossRefGoogle Scholar
  188. 188.
    Shaw, JL, and Bassett, CA: The effects of varying oxygen concentrations on osteogenesis and embryonic cartilage in vitro. J. Bone. Joint. Surg., 49-A: 73–80, 1967.Google Scholar
  189. 189.
    Erkell, LJ: Differentiation of mouse neuroblastoma under increased oxygen tension. Exp. Cell Biol., 48: 374–380, 1980.PubMedGoogle Scholar
  190. 190.
    Foreman, HJ, and Boveris, A: Superoxide radical and hydrogen peroxide in mitochondria, in Free Radicals in Biology, edited by Pryor, WA, New York, Academic Press, 1982, pp. 65–90.Google Scholar
  191. 191.
    Turrens, JF, Freeman, BA, Levitt, JG, and Crapo, JD: The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch. Biochem. Biophys., 217: 401–410, 1982.PubMedCrossRefGoogle Scholar
  192. 192.
    Sohal, RS, Allen, RG, and Nations, C: Oxygen free radicals play a role in cellular differentiation: an hypothesis. J. Free Rad. Biol. Med., 2: 175–181, 1986.CrossRefGoogle Scholar
  193. 193.
    McElroy, MC, Postle, AD, and Kelly, FJ: Catalase, superoxide dismutase and glutathione peroxidase activities of lung and liver during human development. Biochim. Biophys. Acta., 1117: 153–158, 1992.PubMedGoogle Scholar
  194. 194.
    Aliakbar, S, Brown, PR, Bidwell, D, and Nicolaides, KH: Human erythrocyte superoxide dismutase in adults, neonates, and normal, hypoxaemic, anemic, and chromesomally abnormal fetuses. Clin. Biochem, 26: 109–115, 1993.PubMedCrossRefGoogle Scholar
  195. 195.
    Hien, PV, Kovacs, K, and Matkovics, B: Properties of enzymes. I. Study of superoxide dismutase activity changes in human placenta of different ages. Enzyme, 18: 341–347, 1974.PubMedGoogle Scholar
  196. 196.
    Takehara, Y, Yoshioka, T, and Sasaki, J: Changes in the levels of lipoperoxide and antioxidant factors in human placenta during gestation. Acta Medical Okayama, 44: 103–111, 1990.Google Scholar
  197. 197.
    Sekiba, K, and Yoshioka, T: Changes of lipid peroxidation and superoxide dismutase activity in human placenta. Am. J. Obstetr. Gynecol., 135: 368–371, 1979.Google Scholar
  198. 198.
    Nakagawara, A, Nathan, CF, and Cohn, ZA: Hydrogen peroxide metabolism in human monocytes during differentiation in vitro. J. Clin. Invest., 68: 1243–1252, 1981.PubMedGoogle Scholar
  199. 199.
    Gidrol, N, Lin, WS, Degousee, N, Yip, SF, and Kush, A: Accumulation of reactive oxygen species and oxidation of cytokinin in germinating soybean seeds. Eur. J. Biochem., 224: 21–28, 1994.PubMedCrossRefGoogle Scholar
  200. 200.
    Lott, T, Gorman, S, and Clark, J: Superoxide dismutase in Didymium iridis: characterization of changes in activity during senescence and sporulation. Mech. Ageing Dev., 17: 119–130, 1981.PubMedCrossRefGoogle Scholar
  201. 201.
    Allen, RG, Balin, AK, Reimer, RJ, Sohal, RS, and Nations, C: Superoxide dismutase induces differentiation in the slime mold, Physarum polycephalum. Arch. 8iochem. Biophys., 261: 205–211, 1988.CrossRefGoogle Scholar
  202. 202.
    Allen, RG, Newton, RK, Farmer, KJ, and Nations, C: Effect of the free radical generator paraquat on differentiation, superoxide dismutase, glutathione and inorganic peroxides in microplasmodia of Physarum polycephalum. Cell Tissue Kinet., 18: 623–630, 1985.PubMedGoogle Scholar
  203. 203.
    Nations, C, Atlen, RG, Farmer, K, Toy, PL, and Sohal, RS: Superoxide dismutase activity during the plasmodial life cycle of Physarum polycephalum. Experientia, 42: 64–66, 1986.CrossRefGoogle Scholar
  204. 204.
    Smith, J, and Shrift, A: Phylogenetic distribution of glutathione peroxidase. Comp. Biochem. Physiol., 63B: 39–44, 1979.Google Scholar
  205. 205.
    Allen, RG, Newton, RK, Sohal, RS, Shipley, GL, and Nations, C: Atterations in superoxide dismutase, glutathione, and peroxides in the plasmodial slime mold Physarum polycephalum during differentiation. J. Cell. Physiol., 125: 413–419, 1985.PubMedCrossRefGoogle Scholar
  206. 206.
    Anderson, GL: Superoxide dismutase activity in Dauerlarvae of Caenorhabditis elegans (Nematoda: Rhabditidae). Can. J. Zool., 60: 288–291, 1982.CrossRefGoogle Scholar
  207. 207.
    Fernandez-Souza, JM, and Michelson, AM: Variations of the superoxide dismutases during the development of the fruitfly, Ceratitis capitata. Biochem. Biophys. Res. Commun., 73: 217–223, 1976.CrossRefGoogle Scholar
  208. 208.
    Massie, HR, Aiello, VR, and Williams, TR: Changes in superoxide dismutase activity and copper during development and ageing in the fruit fly Drosophila melanogaster. Mech. Ageing Dev., 12: 279–286, 1980.PubMedCrossRefGoogle Scholar
  209. 209.
    Nickla, H, Anderson, J, and Palzkill, T: Enzymes involved in oxygen detoxification during development of Drosophila melanogaster. Experientia, 39: 610–612, 1983.PubMedCrossRefGoogle Scholar
  210. 210.
    Allen, RG, Oberley, LW, Elwell, JH, and Sohal, RS: Developmental patterns in the antioxidant defenses of the housefly, Musca domestica. J. Cell. Physiol., 146: 270–276, 1991.PubMedCrossRefGoogle Scholar
  211. 211.
    Barja de Quiroga, G, and Gutierrez, P: Superoxide dismutase during the development of two amphibian species and its role in hyperoxia tolerance. Mol. Physiol., 6: 221–232, 1984.Google Scholar
  212. 212.
    Montesano, L, Carri, MT, Mariottini, P, Amaldi, F, and Rotilio, G: Developmental expression of Cu,Zn superoxide dismutase in Xenopus. Eur. J. Biochem., 186: 421–426, 1989.PubMedCrossRefGoogle Scholar
  213. 213.
    Wilson, JX, Lui, EMK, and Del Maestro, RF: Developmental profiles of antioxidant enzymes and trace metals in chick embryoes. Mech. Ageing Dev., 65: 51–64, 1992.PubMedCrossRefGoogle Scholar
  214. 214.
    Frank, L, and Groseclose, EE: Preparation for birth into an O2-rich environment: the antioxidant enzymes in developing rabbit lung. Pediatr. Res., 18: 240–244, 1984.PubMedGoogle Scholar
  215. 215.
    Frank, L, and Sosenko, IR: Prenatal development of lung antioxidant enzymes in four species. J. Pediatr., 110: 106–110, 1987.PubMedCrossRefGoogle Scholar
  216. 216.
    Frank, L, Bucher, JR, and Roberts, RJ: Oxygen toxicity in neonatal and adult animals of various species. J. Appl. Physiol. Respirat. Environ. Exercise Physiol., 45: 699–704, 1978.Google Scholar
  217. 217.
    Autor, AP, Frank, L, and Roberts, RJ: Developmental characteristics of pulmonary superoxide dismutase: relationship to idiopathic respiratory disress syndrome. Pediatr. Res., 10: 154–158, 1976.PubMedGoogle Scholar
  218. 218.
    Russanov, EM, Kirkova, MD, Setchenska, MS, and Arnstein, HRV: Enzymes of oxygen metabolism during erythrocyte differentiation. Biosci. Rep., 1: 927–931, 1981.PubMedCrossRefGoogle Scholar
  219. 219.
    Mavelli, I, Mondovi, B, Federico, R, and Rotilio, G: Superoxide dismutase activity in developing rat brain. J. Neurochem., 31: 363–364, 1978.PubMedGoogle Scholar
  220. 220.
    Tanswell, AK, and Freeman, BA: Pulmonary antioxidant enzyme maturation in the fetal and neonatal rat. I. Development profiles. Pediatr. Res., 18: 584–587, 1984.PubMedGoogle Scholar
  221. 221.
    Yam, J, Frank, L, and Roberts, RJ: Age-related development of pulmonary antioxidant enzymes in the rat (40040). Proc. Soc. Exp. Biol. Med., 157: 293–296, 1978.PubMedGoogle Scholar
  222. 222.
    Gerdin, E, Tyden, O, and Eriksson, UJ: The development of antioxidant enzymatic defense in the perinatal rat lung: activities of superoxide dismutase, glutathione peroxidase, and catalase. Pediatr. Res., 19: 687–691, 1985.PubMedGoogle Scholar
  223. 223.
    Clerch, LB, and Massaro, D: Rat lung antioxidant enzymes: differences in perinatal gene expression and regulation. Am. J. Physiol., 263: L446–L470, 1992.Google Scholar
  224. 224.
    Dobashi, K, Asayama, K, Hayashibe, H, Munim, A, Kawaoi, A, Morikawa, M, and Nakazawa, S: Immunohistochemical study of copper-zinc and manganese superoxide dismutases in the lungs of human fetuses and newborn infants: developmental profile and alterations in hyaline membrane disease and bronchopulmonary dysplasia. Virchows Archiv-A, Pathological Anatomy & Histopathology, 423: 177–184, 1993.CrossRefGoogle Scholar
  225. 225.
    Chen, Y, and Frank, L: Differential gene expression of antioxidant enzymes in the perinatal rat lung. Pediatr. Res., 34: 27–31, 1993.PubMedGoogle Scholar
  226. 226.
    Asayama, K, Hayashibe, H, Dobashi, K, Uchida, N, Kobayashi, M, Kawaoi, A, and Kato, K: Immunohistochemical study on perinatal development of rat superoxide dismutases in lungs and kidneys. Pediatr. Res., 29: 487–491, 1991.PubMedGoogle Scholar
  227. 227.
    Yoshioka, T, Shimada, T, and Sekiba, K: Lipid peroxidation and antioxidants in the rat lung during development. Biol. Neonate, 38: 161–168, 1980.PubMedGoogle Scholar
  228. 228.
    Utsumi, K, Yoshioka, T, Yamanaka, N, and Nakazawa, T: Increase in superoxide dismutase activity concomitant with a decrease in lipid peroxidation during post partum development. FEBS Lett., 79: 1–3, 1977.PubMedCrossRefGoogle Scholar
  229. 229.
    Munim, A, Asayama, K, Dobashi, K, Suzuki, K, Kawaoi, A, and Kato, K: Imunohistochemical localization of superoxide dismutases in fetal and neonatal rat tissues. J. Histochem. Cytochem., 40: 1705–1713, 1992.PubMedGoogle Scholar
  230. 230.
    Pittschieler, K, Lebenthal, E, Bujanover, Y, and Petell, JK: Levels of Cu-Zn and Mn superoxide dismutases in rat liver during development. Gastroenterology, 100: 1062–1068, 1991.PubMedGoogle Scholar
  231. 231.
    Shivakumar, BR, Anandatheerthavarada, HK, and Ravindranath, V: Free radical scavenging systems in developing rat brain. Int. J. Devl. Neuroscience, 9: 181–185, 1991.CrossRefGoogle Scholar
  232. 232.
    Mavelli, I, Rigo, A, Federico, R, Ciriolo, MR, and Rotilio, G: Superoxide dismutase, glutathione peroxidase and catalase in developing rat brain. Biochem. J., 204: 535–540, 1982.PubMedGoogle Scholar
  233. 233.
    Petrovic, VM, Spasic, M, Saicic, Z, Milic, B, and Radojicic, R: Increase in superoxide dismutase activity induced by thyroid hormones in the brains of neonate and adult rats. Experientia, 38: 1355–1356, 1982.CrossRefGoogle Scholar
  234. 234.
    Borrello, S, De Leo, ME, and Galeotti, T: Transcriptional regulation of MnSOD by manganese in the liver of manganese-deficient mice and during rat development. Biochem. Int., 28: 595–601, 1992.PubMedGoogle Scholar
  235. 235.
    Mariucci, G, Ambrosini, MV, Colarieti, L, and Bruschelli, G: Differential changes in Cu, Zn and Mn superoxide dismutase activity in developing rat brain and liver. Experientia, 46: 753–755, 1990.PubMedCrossRefGoogle Scholar
  236. 236.
    Yoshioka, T, Utsumi, K, and Sekiba, K: Superoxide dismutase activity and lipid peroxidation of the rat liver during development. Biol. Neonate, 32: 147–153, 1977.PubMedGoogle Scholar
  237. 237.
    Ledig, M, Fried, R, Ziessel, M, and Mandel, P: Regional distribution of superoxide dismutase in rat brain during postnatal development. Dev. Brain Res., 4: 333–337, 1982.CrossRefGoogle Scholar
  238. 238.
    Aspberg, A, and Tottmar, O: Development of antioxidant enzymes in rat brain and in reaggregation culture of fetal brain cells. Dev. Brain Res., 66: 55–58, 1992.CrossRefGoogle Scholar
  239. 239.
    Hayashibe, H, Asayama, K, Dobashi, K, and Kato, K: Prenatal development of antioxidant enzymes in rat lung, kidney, and heart: marked increase in immunoreactive superoxide dismutases, glutathione peroxidase, and catalase in the kidney. Pediatr. Res., 27: 472–475, 1990.PubMedGoogle Scholar
  240. 240.
    Jow, WW, Schlegel, PN, Cichon, Z, Phillips, D, Goldstein, M, and Bardin, CW: Identification and localization of copper-zinc superoxide dismuatse gene. Expression in rat testicular development. J. Androl., 14: 439–447, 1993.PubMedGoogle Scholar
  241. 241.
    Paoletti, F, and Mocali, A: Changes in CuZn-superoxide dismutase during induced differentiation of murine erythroleukemia. Cancer Res., 48: 6674–6677, 1988.PubMedGoogle Scholar
  242. 242.
    El-Hage, S, and Singh, SM: Temporal expression of genes encoding free radical-metabolizing enzymes is associated with higher mRNA levels during In Utero development in mice. Dev. Genet., 11: 149–159, 1990.PubMedCrossRefGoogle Scholar
  243. 243.
    Novak, R, Matkovics, M, Marik, M, and Fachet, J: Changes in mouse liver superoxide dismutase activity and lipid peroxidation during embryonic and postpartum development. Experientia, 34: 1134–1135, 1978.PubMedCrossRefGoogle Scholar
  244. 244.
    Harman, AW, McKenna, M, and Adamson, GM: Postnatal development of enzyme activities associated woth protection against oxidative stress in the mouse. Biol. Neonate, 57: 187–193, 1990.PubMedCrossRefGoogle Scholar
  245. 245.
    Zelck, U, Nowak, R, Karnstedt, U, Koitschev, A, and Käcker, N: Specific activities of antioxidant enzymes in the cochlea of guinea pigs at different stages of development. Eur. Arch. Otorhinolyrngol., 250: 218–219, 1993.Google Scholar
  246. 246.
    Walther, FJ, Wade, AB, Warburton, D, and Foreman, HJ: Ontogeny of antioxidant enzymes in the fetal lamb lung. Exp. Lung Res., 17: 39–45, 1991.PubMedGoogle Scholar
  247. 247.
    Carbone, GMR, St. Clair, DK, Xu, A, and Rose, JC: Expression of manganese superoxide dismutase in ovine kidney cortex during development. Pediatr. Res., 35: 41–44, 1994.PubMedGoogle Scholar
  248. 248.
    Strange, RC, Cotton, W, Fryer, AA, Drew, R, Bradwell, AR, Marshall, T, Collins, MF, Bell, J, and Hume, R: Studies on the expression of Cu,Zn superoxide dismutase in human tissues during development. Biochim. Biophys. Acta., 964: 260–265, 1988.PubMedGoogle Scholar
  249. 249.
    Asayama, K, Janco, RL, and Burr, IM: Selective induction of manganous superoxide dismutase in human monocytes. Am. J. Physiol., 249: C393–C397, 1985.PubMedGoogle Scholar
  250. 250.
    Strange, RC, Cotton, W, Fryer, AA, Jones, P, Bell, J, and Hume, R: Lipid peroxidation and expression of copper-zinc and manganese superoxide dismutase in lungs of premature infants with hyline membrane disease and broncopulmonary dysplasia. J. Clin. Lab. Med., 116: 666–673, 1990.Google Scholar
  251. 251.
    Church, SL, Farmer, DR, and Nelson, DM: Induction of manganese superoxide dismutase in cultured human trophoblast during in vitro differentiation. Dev. Biol., 149: 177–184, 1992.PubMedCrossRefGoogle Scholar
  252. 252.
    Allen, RG, and Balin, AK: Developmental changes in the superoxide dismutase activity of human skin fibroblasts are maintained in vitro and are not caused by oxygen. J. Clin. Invest., 82: 731–734, 1988.PubMedGoogle Scholar
  253. 253.
    Allen, RG, Keogh, BP, Gerhard, G, Pignolo, R, Horton, J, and Cristofalo, VJ: Expression and regulation of SOD activity in human skin fibroblasts from donors of different ages. J. Cell. Physiol., 165: 576–587, 1995.PubMedCrossRefGoogle Scholar
  254. 254.
    Borg, LAH, Cagliero, E, Sandier, S, Welsh, N, and Eizirik, DL: Interleukin-1β increases the activity of superoxide dismutase in rat pancreatic islets. Endocrinology, 130: 2851–2857, 1992.PubMedCrossRefGoogle Scholar
  255. 255.
    Whitsett, JA, Clark, JC, Wispe, JR, and Pryhuber, GS: Effects of TNF-α and phorbol ester on human surfactant protein and MnSOD-gene transcription in vitro. Am. J. Physiol., 262: L688–L693, 1992.PubMedGoogle Scholar
  256. 256.
    Fernandez, A, Marin, MC, McDonnell, T, and Ananthaswamy, HN: Differential sensitivity of normal and Ha-ras-transformed C3H mouse embryo fibroblasts to tumor necrosis factor: induction of bcl-2, c-myc and manganese superoxide dismutase in resistant cells. Oncogene, 9: 2009–2017, 1994.PubMedGoogle Scholar
  257. 257.
    Czaja, MJ, Schilsky, ML, Xu, Y, Schmiedeberg, P, Compton, A, Ridnour, L, and Oberley, LW: Induction of MnSOD gene expression in a hepatic model of TNF-α toxicity does not result in increased protein. Am. J. Physiol., 266: G737–G744, 1994.PubMedGoogle Scholar
  258. 258.
    Hunt, JS: Expression and regulation of the tumour necrosis factor-alpha gene in the female reproductive tract. Repro. Fert. and Dev., 5: 141–153, 1993.CrossRefGoogle Scholar
  259. 259.
    Kumar, S, Vinci, JM, Millis, AJT, and Baglioni, C: Expression of interleukin-lα and β in early passage fibroblasts from aging individuals. Exp. Geront., 28: 505–513, 1993.CrossRefGoogle Scholar
  260. 260.
    Wan, XS, Devalaraja, MN, and St. Clair, DK: Molecular structure and organization of the human manganese superoxide dismutase gene. DNA Cell Biol., 13: 1127–1136, 1994.PubMedGoogle Scholar
  261. 261.
    Meyrick, B, and Magnuson, MA: Identification and functional characterization of the bovine manganous superoxide dismutase promoter. Am. J. Resp. Cell Mol. Biol., 10: 113–121, 1994.Google Scholar
  262. 262.
    Ho, YS, Howard, AJ, and Crapo, JD: Structure of a rat manganous superoxide dismutase gene. Am. J. Resp. Cell Mol. Biol., 4: 278–286, 1991.Google Scholar
  263. 263.
    Smale, ST, Schmidt, MC, Berk, AJ, and Baltimore, D: Transcriptional activation by Sp1 as directed through TATA or initiator: specific requirement for mammalian transcription factor IID. Proc. Natl. Acad. Sci. USA, 87: 4509–4513, 1990.PubMedGoogle Scholar
  264. 264.
    Saffer, JD, Jackson, SF, and Annarella, MB: Developmental expression of Sp1 in the mouse. Mol. Cell. Biol., 11: 2189–2199, 1991.PubMedGoogle Scholar
  265. 265.
    Robidoux, S, Gosselin, P, Harvey, M, Leclerc, S, and Guerin, SL: Trancription of the mouse secretory protease inhibitor p12 gene is activated by the developmentally regulated positive transcription factor Sp1. Mol. Cell. Biol., 12: 3796–3806, 1992.PubMedGoogle Scholar
  266. 266.
    Innis, JW, Moore, DJ, Kash, SF, Ramamurthy, V, Sawadogo, M, and Kellems, RE: The murine deaminase promoter requires an atypical TATA box which binds transcription factor IID and transcriptional activity is stimulated by multiple upstream Sp1 sites. J. Biol. Chem., 266: 21765–21772, 1991.Google Scholar
  267. 267.
    Li, Y, Huang, T-T, Carlson, EJ, Melov, S, Ursell, PC, Olsen, JL, Noble, LJ, Yoshimura, MP, Berger, C, Chan, PH, Wallace, DC, and Epstein, CJ: Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nature Genetics, 11: 376–381, 1995.PubMedCrossRefGoogle Scholar
  268. 268.
    Beckman, BS, Balin, AK, and Allen, RG: Superoxide dismutase induces differentiation in Friend erythroleukemia cells. J. Cell. Physiol., 139: 370–376, 1989.PubMedCrossRefGoogle Scholar
  269. 269.
    Church, SL, Grant, JW, Ridnour, LA, Oberley, LW, Swanson, PE, Meltzer, PS, and Trent, JM: Increased manganese superoxide dismutase expression supresses the malignant phenotype of human melanoma cells. Proc. Natl. Acad. Sci. USA, 90: 3113–3117, 1993.PubMedGoogle Scholar
  270. 270.
    St. Clair, DK, Oberley, TD, Muse, KE, and St. Clair, WH: Expression of manganese superoxide dismutase promotes cellular differentiation. Free Radic. Biol. Med., 16: 275–282, 1994.PubMedCrossRefGoogle Scholar
  271. 271.
    Chernavskii, DS, Solyanik, GI, and Belousov, LV: Relation of the intensity of metabolism with the process of determination in embryonic cell. Biol. Cybernetics, 37: 9–18, 1980.CrossRefGoogle Scholar
  272. 272.
    Hansberg, W, De Groot, H, and Sies, H: Reactive oxygen species associated with cell differentiation in Neurospora crassa. Free Radic. Biol. Med., 14: 287–293, 1993.PubMedCrossRefGoogle Scholar
  273. 273.
    Frank, L, Price, LT, and Whitney, PL: Possible mechanism for late gestational development of the antioxidant enzymes in the fetal rat lung. Biol. Neonate, 70: 116–127, 1996.PubMedCrossRefGoogle Scholar
  274. 274.
    Nagy, K, Pasti, G, Bene, L, and Zs. Nagy, I: Involvement of Fenton reaction products in differentiation of K562 human leukemia cells. Leuk. Res., 19: 203–212, 1995.PubMedCrossRefGoogle Scholar
  275. 275.
    Nagy, K, Pásti, G, Bene, L, and Zs.-Nagy, I: Induction of granuloytic maturation of HL-60 human leukemia cells by free radicals: a hypothesis of cell differentiation involving hydroxyl radicals. Free Rad. Res. Commun., 19: 1–15, 1993.Google Scholar
  276. 276.
    Speier, C, and Newburger, PE: Changes in superoxide dismutase, catalase, and the glutathione cycle during induced myeloid differentiation. Arch. Biochem. Biophys., 251: 551–557, 1986.PubMedCrossRefGoogle Scholar
  277. 277.
    Suda, N, Morita, I, Kuroda, T, and Murota, S: Participation of oxidative stress in the process of osteoclast differentiation. Biochim. Biophys. Acta., 1157: 318–323, 1993.PubMedGoogle Scholar
  278. 278.
    Zhong, W, Oberley, LW, Oberley, TD, Yan, T, Domann, FE, and St. Clair, DK: Inhibition of cell growth and sensitization to oxidative damage by overexpression of manganese superoxide dismutase in rat glioma cells. Cell Growth Diff., 7: 1175–1186, 1996.PubMedGoogle Scholar
  279. 279.
    Kreiger-Brauer, H, and Kather, H: Antagonistic effects of different members of the fibroblast and platlet derived growth factor families on adipose conversion and NADPH-dependent H2O2 generation in 3T3 L1-cells. Biochem. J., 307: 549–556, 1995.Google Scholar
  280. 280.
    Yang, KD, and Shaio, M-F: Hydroxyl radicals as an early signal involved in phorbol ester-induced monocyte differentiation of HL60 cells. Biochem. Biophys. Res. Commun., 200: 1650–1657, 1994.PubMedCrossRefGoogle Scholar
  281. 281.
    Elroy-Stein, O, Bernstein, Y, and Groner, Y: Over-production of human Cu/Zn superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J., 5: 615–622, 1986.PubMedGoogle Scholar
  282. 282.
    Mirochnitchenko, O, and Inouye, M: Effect of overexpression of human Cu, Zn superoxide dismutase in transgenic mice on macrophage functions. J. Immunol., 156: 1578–1586, 1996.PubMedGoogle Scholar
  283. 283.
    Reveillaud, I, Neidzwiecki, A, Bensch, KG, and Fleming, JE: Expression of bovine superoxide dismutase in Drosophila melanogaster augments resistance to oxidative stress. Mol. Cell. Biol., 11: 632–640, 1991.PubMedGoogle Scholar
  284. 284.
    Norris, KH, and Hornsby, PJ: Cytotoxic effects of expression of human superoxide dismutase in bovine adrenocortical cells. Mut. Res., 237: 95–106, 1990.Google Scholar
  285. 285.
    Teixeira, HD, and Meneghini, R: Chinese hamster fibroblasts overexpressing CuZn-superoxide dismutase undergo a global reduction in antioxidants and an increasing sensitivity of DNA to oxidative damage. Biochem. J., 315: 821–825, 1996.PubMedGoogle Scholar
  286. 286.
    Mao, GD, Thomas, PD, Lopaschuk, GD, and Poznansky, MJ: Superoxide dismutase (SOD)-catalase conjugates. J. Biol. Chem., 268: 416–420, 1993.PubMedGoogle Scholar
  287. 287.
    Hodgson, EK, and Fridovich, I: The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry, 14: 5294–5299, 1975.PubMedCrossRefGoogle Scholar
  288. 288.
    Hodgson, EK, and Fridovich, I: The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry, 14: 5299–5303, 1975.PubMedCrossRefGoogle Scholar
  289. 289.
    Paller, MS, and Eaton, JW: Hazards of antioxidant combinations containing superoxide dismutase. Free Radic. Biol. Med., 18: 883–890, 1995.PubMedCrossRefGoogle Scholar
  290. 290.
    Schreck, R, Rieber, P, and Baeuerle, PA: Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κ-B transcription factor and HIV-I. EMBO J., 10: 2247–2258, 1991.PubMedGoogle Scholar
  291. 291.
    Meyer, M, Caselman, WH, Schlüter, V, Schreck, R, Hofschneider, PH, and Baeuerle, PA: Hepatitis B virus transactivator MHBs1: activation of NF-κB, selective inhibition by antioxidants and integral membrane localization. EMBO J., 11: 2991–3001, 1992.PubMedGoogle Scholar
  292. 292.
    Israël, N, Gougerot-Pocidalo, M-A, Aillet, F, and Virelizier, J-L: Redox status of cells influences constituative or induced NF-κB translocation and HIV long terminal repeat activity in human T and monocyte cell lines. J. Immunol., 149: 3386–3393, 1992.PubMedGoogle Scholar
  293. 293.
    Toledano, MB, and Leonard, WJ: Modulation of transcription factor NF-κB binding activity by oxidation-reduction in vitro. Proc. Natl. Acad. Sci. USA, 88: 4328–4332, 1991.PubMedGoogle Scholar
  294. 294.
    Molitor, JA, Ballard, DW, and Greene, WC: κB-specific DNA binding proteins are differentially inhibited by enhancer mutations and biological oxidation. The New Biologist, 3: 987–996, 1991.PubMedGoogle Scholar
  295. 295.
    Wagner, AM: A role for active oxygen species as second messengers in the induction of alternate oxidase gene expression in Petunia hybrida cells. FEBS Lett., 368: 339–342, 1995.PubMedCrossRefGoogle Scholar
  296. 296.
    Sundaresan, M, Yu, Z, Ferrans, KI, and Finkel, T: Requirement for generation of H2O2 for platlet-derived growth factor signal transduction. Science, 270: 296–299, 1995.PubMedGoogle Scholar
  297. 297.
    Chojkier, M, Houglum, K, Solis-Herruzo, J, and Brenner, DA: Stimulation of collagen gene expression by ascorbic acid in cultured human fibroblasts. J. Biol. Chem., 264: 16957–16962, 1989.Google Scholar
  298. 298.
    Brenneisen, P, Briviba, K, Wlaschek, M, Wenk, J, and Scharffetter-Kochanek, K: Hydrogen peroxide (H2O2) increases the steady-state mRNA level of collagenase/MMP-1 in human dermal fibroblasts. Free Radic. Biol. Med., 22: 515–524, 1997.PubMedCrossRefGoogle Scholar
  299. 299.
    Hentze, MW, Rouault, TA, Harford, JB, and Klausner, RD: Oxidative-reduction and the molecular mechanism of a regulatory RNA-protein interaction. Science, 244: 357–359, 1989.PubMedGoogle Scholar
  300. 300.
    Casey, JL, Hentze, MW, Koeller, DM, Caughman, SW, Rouault, TA, Klausner, RD, and Harford, JB: Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. Science, 240: 924–928, 1988.PubMedGoogle Scholar
  301. 301.
    Myrset, ah, Bostard, A, Jamin, N, Lirsac, PN, Toma, F, and Gabrielsen, OS: DNA and redox state induced conformational changes in the DNA-binding domain of the Myb oncoprotein. EMBO J., 12: 4625–4633, 1993.PubMedGoogle Scholar
  302. 302.
    Huang, R-P, and Adamson, ED: Characterization of the DNA-binding properties of the early growth response-1 (EGR-1) transcription factor: evidence for modulation by a redox mechanism. DNA Cell Biol., 12: 265–273, 1993.PubMedCrossRefGoogle Scholar
  303. 303.
    Abate, C, Patel, L, Rauscher, FJ, and Curran, T: Redox regulation of FOS and JUN DNA-binding activity in vitro. Science, 249: 1157–1161, 1990.PubMedGoogle Scholar
  304. 304.
    Keyse, SM, and Emslie, EA: Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase. Nature, 359: 644–647, 1992.PubMedCrossRefGoogle Scholar
  305. 305.
    Yoshioka, K, Deng, T, Cavigelli, M, and Karin, M: Antitumor promotion by phenolic antioxidants: inhibition of AP-1 activity through induction of Fra expression. Proc. Natl. Acad. Sci. USA, 92: 4972–4976, 1995.PubMedGoogle Scholar
  306. 306.
    Bannister, AJ, Cook, A, and Kouzarides, T: In vitro DNA binding of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes. Oncogene, 6: 1243–1250, 1991.PubMedGoogle Scholar
  307. 307.
    Adler, V, Schaffer, A, Kim, J, Dolan, L, and Ronai, Z: UV irradiation and heat shock mediate JNK activation via alternate pathways. J. Biol. Chem., 270: 26071–26077, 1995.Google Scholar
  308. 308.
    Galang, CK, and Hauser, CA: Cooperative DNA binding of the Human HoxB5 (Hox-2.1) protein is under redox regulation in vitro. Mol. Cell. Biol., 13: 4609–4617, 1993.PubMedGoogle Scholar
  309. 309.
    DeForge, LE, Preston, AM, Takeuchi, E, Boxer, LA, and Remick, DG: Regulation of interleukin 8 gene expression by oxidant stress. J. Biol. Chem., 268: 25568–25576, 1993.Google Scholar
  310. 310.
    Datta, R, Hallahan, DE, Kharbanda, SM, Rubin, E, Sherman, ML, Huberman, E, Weichselbaum, RR, and Kufe, DW: Involvement of reactive oxygen intermediates in the induction of c-jun gene transcription by ionizing radiation. Biochemistry, 31: 8300–8306, 1992.PubMedCrossRefGoogle Scholar
  311. 311.
    Maki, A, Berezesky, IK, Fargnoli, J, Holbrook, NJ, and Trump, BF: Role of [Ca2+]j in induction ofc-fos, c-jun, and c-myc mRNA in rat PTE after oxidative stress. FASEB J., 6: 919–924, 1992.PubMedGoogle Scholar
  312. 312.
    Kurata, SI, Matsumoto, M, Tsuji, Y, and Nakajima, H: Lipopolysaccharide activates transcription of the heme oxygenase gene in mouse M1 cells through oxidative activation of nuclear factor kappa-b. Eur. J. Biochem., 239: 566–571, 1996.PubMedCrossRefGoogle Scholar
  313. 313.
    Kurata, S, Matsumoto, M, and Nakajima, H: Transcriptional control of the heine oxygenase gene in mouse M1 cells during their TPA-induced differentiation into macrophages. J. Cell. Biochem., 62: 314–324, 1996.PubMedCrossRefGoogle Scholar
  314. 314.
    Rao, GN, Glasgow, WC, Eling, TE, and Runge, MS: Role of hydroperoxyeicosatetraenoic acids in oxidative stress-induced activating protein 1 (AP-1) activity. J. Biol. Chem., 271: 27760–27764, 1996.Google Scholar
  315. 315.
    Das, KC, Lewis-Molock, Y, and White, CW: Activation of NF-κB and elevation of MnSOD gene expression by thiol reducing agents in lung adenocarcinoma (A549) cells. Am. J. Physiol., 269: L588–L602, 1995.PubMedGoogle Scholar
  316. 316.
    Stevenson, MA, Pollock, SS, Coleman, CN, and Calderwood, SK: X-irradiation, phorbol esters, and H2O2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates. Cancer Res., 54: 12–15, 1994.PubMedGoogle Scholar
  317. 317.
    Guyton, KZ, Liu, Y, Gorospe, M, Xu, Q, and Holbrook, NJ: Activation of mitogen-activated protein kinase by H2O2. J. Biol. Chem., 271: 4138–4142, 1996.PubMedCrossRefGoogle Scholar
  318. 318.
    Barker, CW, Fagan, JB, and Pasco, DS: Down-regulation of P4501A1 and P4501A2 mRNA expression in isolated hepatocytes by oxidative stress. J. Biol. Chem., 269: 3985–3990, 1994.PubMedGoogle Scholar
  319. 319.
    Miyazaki, Y, Shinomura, Y, Tsutsui, S, Yasunaga, Y, Zushi, S, Higashiyama, S, Taniguchi, N, and Matsuzawa, Y: Oxidative stress increases gene expression of heparin-binding EGF-like growth factor and amphiregulin in cultured rat gastric epithelial cells. Biochem. Biophys. Res. Commun., 226: 542–546, 1996.PubMedCrossRefGoogle Scholar
  320. 320.
    Tate, DJ, Miceli, MV, and Newsome, DA: Phagocytosis and H2O2 induced catalase and metallothionein gene expression in human retinal pigment epithelial cells. Invest. Ophthalmol. Vis. Sci., 36: 1271–1279, 1995.PubMedGoogle Scholar
  321. 321.
    Hecht, D, and Zick, Y: Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate in vitro. Biochem. Biophys. Res. Commun., 188: 773–779, 1992.PubMedCrossRefGoogle Scholar
  322. 322.
    Choi, H-S, and Moore, DD: Induction of c-fos and c-jun gene expression by phenolic antioxidants. Mol. Endocrin., 7: 1596–1602, 1993.CrossRefGoogle Scholar
  323. 323.
    Flohé, L, Brigelius-Flohe, R, Saliou, C, Traber, MG, and Packer, L: Redox regulation of NF-kappa B activation. Free Radic. Biol. Med., 22: 1115–1126, 1997.PubMedCrossRefGoogle Scholar
  324. 324.
    Sen, CK, and Packer, L: Antioxidants and redox regulation of gene transcription. FASEB J., 10: 709–720, 1996.PubMedGoogle Scholar
  325. 325.
    Sun, Y, and Oberley, LW: Redox regulation of transcriptional activators. Free Radic. Biol. Med., 21: 335–348, 1996.PubMedCrossRefGoogle Scholar
  326. 326.
    Meyer, M, Pahl, HL, and Baeuerle, PA: Regulation of the transcription factors NF-κB and AP-1 by redox changes. Chem.-Biol. Interactions, 91: 91–100, 1994.CrossRefGoogle Scholar
  327. 327.
    Monterio, HP, and Stern, A: Redox regulation of tyrosine phosphorylation-dependent signal transduction pathways. Free Radic. Biol. Med., 21: 323–333, 1996.CrossRefGoogle Scholar
  328. 328.
    Bauskin, AR, Alkalay, I, and Ben-Neriah, Y: Redox regulation of protein tyrosine kinase in the endoplasmic reticulum. Cell, 66: 685–696, 1991.PubMedCrossRefGoogle Scholar
  329. 329.
    Nakamura, K, Hori, T, Sato, N, Sugie, K, Kawakami, T, and Yodoi, J: Redox regulation of a src family protein tyrosine kinase p56lck in T cells. Oncogene, 8: 3133–3139, 1993.PubMedGoogle Scholar
  330. 330.
    Vallé, A, and Kinet, JP: N-acetyl-L-cysteine inhibits antigen-mediated Syk, but not Lyn tyrosine kinase activation in mast cells. FEBS Lett., 357: 41–44, 1995.PubMedCrossRefGoogle Scholar
  331. 331.
    Qin, SF, Minami, Y, Hibi, M, Kurosaki, T, and Yamamura, H: Syk-dependent and-independent signaling cascades in B cells elicited by osmotic and oxidative stress. J. Biol. Chem., 272: 2098–2103, 1997.PubMedCrossRefGoogle Scholar
  332. 332.
    Schieven, GL, Mittler, RS, Nadler, SG, Kirihara, JM, Bolen, JB, Kanner, SB, and Ledbetter, JA: ZAP-70 tyrosine kinase, CD45, and T cell receptor involvement in UV-and H2O2-induced T cell signal transduction. J. Biol. Chem., 269: 20718–20726, 1994.Google Scholar
  333. 333.
    Wang, GL, Jiang, B-H, and Semenza, GL: Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor I. Biochem. Biophys. Res. Commun., 212: 550–556, 1995.Google Scholar
  334. 334.
    Rao, GN: Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases. Oncogene, 13: 713–719, 1996.PubMedGoogle Scholar
  335. 335.
    Knebel, A, Rahmsdorf, HJ, Ullrich, A, and Herrlich, P: Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J., 15: 5314–5325, 1996.PubMedGoogle Scholar
  336. 336.
    Stein, B, Rahmsdorf, HJ, Steffen, A, Litfin, M, and Herrlich, P: UV-induced DNA damage is an intermediate step in UV-induced expression of human immunodeficiency virus type I, collagenase, c-fos, and metallothionine. Mol. Cell. Biol., 9: 5169–5181, 1989.PubMedGoogle Scholar
  337. 337.
    Dalton, TP, Li, Q, Bittle, D, Liang, L, and Andrews, GK: Oxidative stress activates metal-responsive transcription factor-1 binding activity. J. Biol. Chem., 271: 26233–26241, 1996.Google Scholar
  338. 338.
    Arnone, MI, Zannini, M, and Di Lauro, R: The DNA binding activity and dimerization ability of the thyroid transcription factor I are redox regulated. J. Biol. Chem., 270: 12048–12055, 1995.Google Scholar
  339. 339.
    Whisler, RL, Newhouse, YG, Beiqing, L, Karanfilov, BK, Goyette, MA, and Hackshaw, KV: Regulation of protein kinase enzymatic activity in Jurkat T cells during oxidative stress uncoupled from protein tyrosine kinases: role of oxidative changes in protein kinase activation requirements and generation of second messengers. Lymphokine and Cytokine Research, 13: 399–410, 1994.PubMedGoogle Scholar
  340. 340.
    Pombo, CM, Bonverntre, JV, Molnar, A, Kyriakis, J, and Force, T: Activation of human Ste-like kinase by oxidant stress defines novel stress response pathway. EMBO J., 15: 4537–4546, 1996.PubMedGoogle Scholar
  341. 341.
    Ohba, M, Shibanuma, M, Kuroki, T, and Nose, K: Production of hydrogen peroxide by transforming growth factor-β1 and its involvement in induction of erg-1 in mouse osteoblastic cells. J. Cell Biol., 126: 1079–1088, 1994.PubMedCrossRefGoogle Scholar
  342. 342.
    Nose, K, Shibanuma, K, Kikuchi, K, Kageyama, H, Sakiyama, S, and Kuroki, T: Transcriptional activation of early-response genes by hydrogen peroxide in a mouse osteoblastic cell line. Eur. J. Biochem., 201: 99–106, 1991.PubMedCrossRefGoogle Scholar
  343. 343.
    Nose, K, and Ohba, M: Functional activation of the erg-1 (early growth response-1) gene by hydrogen peroxide. Biochem. J., 316: 381–383, 1996.PubMedGoogle Scholar
  344. 344.
    Fraticelli, A, Serrano, CV, Bochner, BS, Capogrossi, MC, and Zweier, JL: Hydrogen peroxide and superoxide modulate leukocyte adhesion molecule expression and leukocyte endothelial adhesion. Biochim. Biophys. Acta., 1310: 251–259, 1996.PubMedCrossRefGoogle Scholar
  345. 345.
    Knoepfel, L, Steinkühler, C, Card, M-T, and Rotilio, G: Role of zinc-coordination and of glutathione redox couple in the redox susceptibility of human transcription factor Sp1. Biochem. Biophys. Res. Commun., 201: 871–877, 1994.PubMedCrossRefGoogle Scholar
  346. 346.
    Crawford, DR, Schools, GP, Salmon, SL, and Davies, KJA: Hydrogen peroxide induces the expression of adapt 15, a novel RNA associated with polysomes in hamster HA-1 cells. Arch. Biochem. Biophys., 325: 256–264, 1996.PubMedCrossRefGoogle Scholar
  347. 347.
    Wang, Y, Crawford, DR, and Davies, KJA: adapt33, a novel oxidant-inducible RNA from hamster HA-1 cells. Arch. Biochem. Biophys., 332: 255–260, 1996.PubMedCrossRefGoogle Scholar
  348. 348.
    Crawford, DR, Leahy, KP, Abramova, N, Lan, L, Wang, Y, and Davies, KJA: Hamster adapt 78 mRNA is a down syndrome critical region homologue that is inducible by oxidative stress. Arch. Biochem. Biophys., 342: 6–12, 1997.PubMedCrossRefGoogle Scholar
  349. 349.
    Crawford, DR, Leahy, KP, Wang, Y, Schools, GP, Kochheiser, JC, and Davies, KJA: Oxidative stress induces the levels of a maf G homolog in hamster HA-1 cells. Free Radic. Biol. Med., 21: 521–525, 1996.PubMedCrossRefGoogle Scholar
  350. 350.
    Ishii, T, Yanagawa, T, Yuki, K, Kawane, T, Yoshida, H, and Bannai, S: Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages. Biochem. Biophys. Res. Commun., 232: 33–37, 1997.PubMedCrossRefGoogle Scholar
  351. 351.
    Shibanuma, M, Arata, S, Murata, M, and Nose, K: Activation of DNA synthesis and expression of the JE gene by catalase in mouse osteoblastic cells: possible involvement of hydrogen peroxide in negative growth regulation. Exp. Cell Res., 218: 132–136, 1995.PubMedCrossRefGoogle Scholar
  352. 352.
    Keyse, SM, and Tyrrell, RM: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA raiation, hydrogen peroxide and sodium arsenite. Proc. Natl. Acad. Sci. USA, 86: 99–103, 1989.PubMedGoogle Scholar
  353. 353.
    Vile, GF, Basu-Modak, S, Waltner, C, and Tyrrell, RM: Heme oxygenase I mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc. Natl. Acad. Sci. USA, 91: 2607–2610, 1994.PubMedGoogle Scholar
  354. 354.
    Nascimento, ALTO, Luscher, P, and Tyrrell, RM: Ultraviolet A (320–380 nm) radiation causes an alteration in the binding of a specific protein/protein complex to a short region of the promoter of the human heme oxygenase 1 gene. Nucleic Acids Res., 21: 1103–1109, 1993.PubMedGoogle Scholar
  355. 355.
    Beiqing, L, Chen, M, and Whisler, RL: Sublethal levels of oxidative stress stimulate transcriptional activation of c-jun and suppress IL-2 promoter activation in jurkat T cells. J. Immunol., 157: 160–169, 1996.PubMedGoogle Scholar
  356. 356.
    Estes, SD, Stoler, DL, and Anderson, GR: Normal fibroblasts induce the C/EBPβ and ATF-4 bZIP transcription factors in response to anoxia. Exp. Cell Res., 220: 47–54, 1995.PubMedCrossRefGoogle Scholar
  357. 357.
    Tournier, C, Thomas, G, Pierre, J, Jacquemin, C, Pierre, M, and Saunier, B: Mediation by arachidonic acid metabolites of the H2O2-induced stimulation of mitogen-activated protein kinases (extracellular-signal-regulated kinase and c-Jun NH2-terminal kinase). Eur. J. Biochem., 244: 587–595, 1997.PubMedCrossRefGoogle Scholar
  358. 358.
    Satriano, JA, Shuldiner, M, Hora, K, Xing, Y, Shan, Z, and Schlondorff, D: Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-α and immunogloblin G. J. Clin. Invest., 92: 1564–1571, 1993.PubMedGoogle Scholar
  359. 359.
    Kuroki, M, Voest, EE, Amano, S, Beerepoot, LV, Takashima, S, Tolentino, M, Kim, RY, Rohan, RM, Colby, KA, Yeo, KT, and Adamis, AP: Reactive oxygen intermediates increase vascular endothelial growth factor expression in vitro and in vivo. J. Clin. Invest., 98: 1667–1675, 1996.PubMedGoogle Scholar
  360. 360.
    Herbert, J-M, Bono, F, and Savi, P: The mitogenic effect of H2O2 for the vascular smooth muscle cells is mediated by an increase of the affinity of basic fibroblast growth factor for its receptor. FEBS Lett., 395: 43–47, 1996.PubMedCrossRefGoogle Scholar
  361. 361.
    Taniguchi, Y, Taniguchi-Ueda, Y, Mori, K, and Yodoi, J: A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene. Nucleic Acids Res., 24: 2746–2752, 1996.PubMedCrossRefGoogle Scholar
  362. 362.
    Makino, Y, Okamoto, K, Yoshikawa, N, Aoshima, M, Hirota, K, Yodoi, J, Umesono, K, Makino, I, and Tanaka, H: Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action. J. Clin. Invest., 98: 2469–2477, 1996.PubMedCrossRefGoogle Scholar
  363. 363.
    Papathanasiou, MA, Kerr, NC, Robbons, JH, McBride, OW, Alamo, I, Barret, SF, Hickson, ID, and Forace, AJ: Induction by ionizing radiation of the gadd45 gene in cultured human cells: lack of mediation by protein kinase C. Mol. Cell. Biol., 11: 1009–1016, 1991.PubMedGoogle Scholar
  364. 364.
    Luethy, JD, Fargnoli, J, Park, JS, Fornace, AJ, Jr, and Holbrook, NJ: Isolation and characterization of the hamster gadd153 gene. Activation of promoter activity by agents that damage DNA. J. Biol. Chem., 265: 16521–16526, 1990.Google Scholar
  365. 365.
    Pognonec, P, Kato, H, and Roeder, RG: The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-independent manner. J. Biol. Chem., 267: 24563–24567, 1992.Google Scholar
  366. 366.
    Legrand-Poels, S, Bours, V, Piret, B, Pflaum, M, Epe, B, Rentier, B, and Piette, J: Transcription factor NF-κB is activated by photosensitization generating oxidative DNA damages. J. Biol. Chem., 270: 6925–6934, 1995.PubMedCrossRefGoogle Scholar
  367. 367.
    Li, XH, Song, L, and Jope, RS: Cholinergic stimulation of AP-1 and NF-κB transcription factors is differentially sensitive to oxidative stress in SH-SY5Y neuroblastoma-relationship to phospho-inositide hydrolysis. J. Neurosci., 16: 5914–5922, 1996 Oct 1.PubMedGoogle Scholar
  368. 368.
    Tanaka, C, Kamata, H, Takeshita, H, Yagisawa, H, and Hirata, H: Redox regulation of lipopolysaccharide (LPS)-induced interleukin-8 (IL-8) gene expression mediated by NF-κB and AP-1 in human astrocytoma U373 cells. Biochem. Biophys. Res. Commun., 232: 568–573, 1997.PubMedCrossRefGoogle Scholar
  369. 369.
    Schenk, H, Klein, M, Erdbrügger, W, Dröge, W, and Schulze-Otshoff, K: Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-κB and AP-1. Proc. Natl. Acad. Sci. USA, 91: 1672–1676, 1994.PubMedGoogle Scholar
  370. 370.
    Meyer, M, Schreck, R, and Baeuerle, PA: H2O2 and antioxidants have opposite effects on the activation of NF-κB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J., 12: 2005–2015, 1993.PubMedGoogle Scholar
  371. 371.
    Devary, Y, Rosette, C, DiDonato, JA, and Karin, M: NF-κB activation by ultraviolet light not dependent on a nuclear signal. Science, 261: 1442–1445, 1993.PubMedGoogle Scholar
  372. 372.
    Tong, L, and Perezpolo, JR: Effect of nerve growth factor on AP-1, NF-κB, and Oct DNA binding activity in apoptotic PC12 cells-extrinsic and intrinsic elements. J. Neurosci. Res., 45: 1–12, 1996.PubMedCrossRefGoogle Scholar
  373. 373.
    Garcia-Ruiz, C, Colell, A, Morales, A, Kaplowitz, N, and Fernandez-Checa, JC: Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor Nuclear Factor κB: studies with isolated mitochonria and rat hepatocytes. Mol. Pharmacol., 48: 825–834, 1995.PubMedGoogle Scholar
  374. 374.
    Schmidt, KN, Amstad, P, Cerutti, P, and Baeuerle, PA: The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB. Chem. Biol., 2: 13–22, 1995.PubMedCrossRefGoogle Scholar
  375. 375.
    Suzuki, YJ, Mizuno, M, and Packer, L: Transient overexpression of catalase does not inhibit TNF-or PMA-induced NF-κB activation. Biochem. Biophys. Res. Commun., 210: 537–541, 1995.PubMedCrossRefGoogle Scholar
  376. 376.
    Schreck, R, Grassmann, R, Fleckenstein, B, and Baeuerle, PA: Antioxidants selectively suppress activation of NF-κB by human T-cell leukemia virus type I Tax protein. J. Virol., 66: 6288–6293, 1992.PubMedGoogle Scholar
  377. 377.
    Kamii, H, Kinouchi, H, Sharp, FR, Koistinaho, J, Epstein, CJ, and Chan, PH: Prolonged expression of hsp70 mRNA following transient focal cerebral ischemia in transgenic mice overexpressing CuZn-superoxide dismutase. J. Cereb. Blood Flow Metab., 14: 478–486, 1994.PubMedGoogle Scholar
  378. 378.
    Kamii, H, Kinouchi, H, Sharp, FR, Epstein, CJ, Sagar, SM, and Chan, PH: Expression of c-fos mRNA after a mild focal cerebral ischemia in SOD-1 transgenic mice. Brain Res., 662: 240–244, 1994.PubMedCrossRefGoogle Scholar
  379. 379.
    Kondo, T, Sharp, FR, Honkaniemi, J, Mikawa, S, Epstein, CJ, and Chan, PH: DNA fragmentation and Prolonged expression of c-fos, c-jun, and hsp70 in kainic acid-induced neuronal cell death in transgenic mice overexpressing human CuZn-superoxide dismutase. J. Cereb. Blood Flow Metab., 17: 241–256, 1997.PubMedCrossRefGoogle Scholar
  380. 380.
    Vincent, F, Corral, M, Defer, N, and Adolphe, M: Effects of oxygen free radicals on articular chondrocytes in culture: c-myc and c-Ha-ras messenger RNAs and proliferation kenetics. Exp. Cell Res., 192: 333–339, 1991.PubMedCrossRefGoogle Scholar
  381. 381.
    Rao, GN, and Berk, BC: Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression. Circ. Res., 70: 593–599, 1992.PubMedGoogle Scholar
  382. 382.
    Crawford, D, Zbinden, I, Amstad, P, and Cerutti, P: Oxidant stress induces the proto-oncogenes c-fos and c-jun in mouse epidermal cells. Oncogene, 3: 27–32, 1988.Google Scholar
  383. 383.
    Büscher, M, Rahmsdorf, HJ, Litfin, M, Karin, M, and Herrlich, P: Activation of the c-fos gene by UV and phorbol ester: different signal transduction pathways converge to the same enhancer element. Oncogene, 3: 301–311, 1988.PubMedGoogle Scholar
  384. 384.
    Devary, Y, Gottlieb, RA, Lau, L, and Karin, M: Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol. Cell. Biol., 11: 2804–2811, 1991.PubMedGoogle Scholar
  385. 385.
    Müller, JM, Cahill, MA, Rupec, RA, Baeuerle, PA, and Nordheim, A: Antioxidants as well as oxidants activate c-fos via Ras-dependent activation of extracellular-signal-regulated kinase 2 and Elk-l. Eur. J. Biochem., 244: 45–52, 1997.PubMedCrossRefGoogle Scholar
  386. 386.
    Rao, GN, Lasségue, B, Griendling, KK, Alexander, RW, and Berk, BC: Hydrogen peroxide-induced c-fos expression is mediated by arachidonic acid release: role of protein kinase C. Nucleic Acids Res., 21: 1259–1263, 1993.PubMedGoogle Scholar
  387. 387.
    Li, WC, and Spector, A: Lens epithelial cell apoptosis is an early event in the development of UVB-induced cataract. Free Radic. Biol. Med., 20: 301–311, 1996.PubMedCrossRefGoogle Scholar
  388. 388.
    Li, WC, Wang, G-M, Wang, R-R, and Spector, A: The redox active components H2O2 and N-acetyl-L-cysteine regulate expression of c-jun and c-fos in lens system. Exp. Eye Res., 59: 179–190, 1994.PubMedCrossRefGoogle Scholar
  389. 389.
    Lee, SF, Hunag, YT, Wu, WS, and Lin, JK: Induction of c-jun protooncogene expression by hydrogen peroxide through hydroxyl radical generation and p60SRC tyrosine kinase activation. Free Radic. Biol. Med., 21: 437–448, 1996.PubMedCrossRefGoogle Scholar
  390. 390.
    Collart, FR, Horio, M, and Huberman, E: Heterogeneity in c-jun gene expression in normal and malignant cells exposed to either ionizing radiation or hydrogen peroxide. Radiat. Res., 142: 188–196, 1995.PubMedGoogle Scholar
  391. 391.
    Rao, GN, Lasségue, B, Griendling, KK, and Alexander, RW: Hydrogen peroxide stimulates transcription in vascular smooth muscle cells: role of arachidonic acid. Oncogene, 8: 2759–2764, 1993.PubMedGoogle Scholar
  392. 392.
    Manome, Y, Datta, R, Taneja, N, Shafman, T, Bump, E, Hass, R, Weichselbaum, R, and Kufe, D: Coinduction of c-jun gene expression and internucleosomal DNA fragmentation by ionizing radiation. Biochemistry, 32: 10607–10613, 1993.Google Scholar
  393. 393.
    Xanthoudakis, S, and Curran, T: Identification of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J., 11: 653–665, 1992.PubMedGoogle Scholar
  394. 394.
    Xanthoudakis, S, Miao, G, Wang, F, Pan, Y-CE, and Curran, T: Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J., 11: 3323–3335, 1992.PubMedGoogle Scholar
  395. 395.
    Wilmer, WA, Tan, LC, Dickerson, JA, Danne, M, and Rovin, BH: Interleukin-1β induction of mitogen-activated protein kinases in human mesangial cells. Role of oxidation. J. Biol. Chem., 272: 10877–10881, 1997.Google Scholar
  396. 396.
    Rao, GN, Bass, AS, Glasgow, WC, Eling, TE, Runge, MS, and Alaxender, RW: Activation of mitogen-activated protein kinases by arachidonic acid and its metabolites in vascular smooth muscle cells. J. Biol. Chem., 269: 32586–32591, 1994.Google Scholar
  397. 397.
    Abe, J, Kusuhara, M, Ulevitch, RJ, Berk, BC, and Lee, JD: Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase. J. Biol. Chem., 271: 16586–16590, 1996.Google Scholar
  398. 398.
    Cui, XL, and Douglas, JG: Arachidonic acid activates c-jun N-terminal kinase through NADPH oxidase in rabbit proximal tubular epithelial cells. Proc. Natl. Acad. Sci. USA, 94: 3771–3776, 1997.PubMedCrossRefGoogle Scholar
  399. 399.
    Lo, YYC, Wong, JMS, and Cruz, TF: Reactive oxygen species mediate cytokine activation of c-jun NH2-terminal kinases. J. Biol. Chem., 271: 15703–15707, 1996.Google Scholar
  400. 400.
    Dhar, V, Adler, V, Lehmann, A, and Ronai, Z: Impaired jun-NH2-terminal kinase activation by ultraviolet irradiation in fibroblasts of patients with Cockayne syndrome complementation group B. Cell Growth Diff., 7: 841–846, 1996.PubMedGoogle Scholar
  401. 401.
    Wagner, BJ, Hayes, TE, Hoban, CJ, and Cochran, BH: The SIF binding element confers sis/PDGF inducibility onto the c-fos promotor. EMBO J., 9: 4477–4484, 1990.PubMedGoogle Scholar
  402. 402.
    Whitmarsh, AJ, Shore, P, Sharrocks, AD, and Davis, RJ: Integration of MAP kinase signal transduction pathways at the serum responsive element. Science, 269: 403–407, 1995.PubMedGoogle Scholar
  403. 403.
    Cerutti, P, Shah, G, Peskin, A, and Amstad, P: Oxidant carcinogenesis and antioxidant defense. Ann. New York Acad. Sci., 663: 158–166, 1992.Google Scholar
  404. 404.
    Kolch, W, Heldecker, G, Kochs, G, Hummel, R, Vahidl, H, Mischak, H, Finkenzeller, G, Marme, D, and Rapp, UR: Protein kinase C-α activates RAF-1 by direct phosphorylation. Nature, 364: 249–252, 1993.PubMedCrossRefGoogle Scholar
  405. 405.
    Norman, C, Runswick, M, Pollock, R, and Treisman, R: Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum responsive element. Cell, 55: 989–1003, 1988.PubMedCrossRefGoogle Scholar
  406. 406.
    Shaw, PE, Schröter, H, and Nordheim, A: The ability of a ternary complex to form over the serum response element correlates with serum inducibility of the human c-fos promoter. Cell, 56: 563–572, 1989.PubMedCrossRefGoogle Scholar
  407. 407.
    Schröter, H, Mueller, CGF, Meese, K, and Nordheim, A: Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element. EMBO J., 9: 1123–1130, 1990.PubMedGoogle Scholar
  408. 408.
    Hill, CS, Marais, R, John, S, Wynne, J, Dalton, S, and Treisman, R: Functional analysis of a growth factor-responsive transcription factor complex. Cell, 73: 395–406, 1993.PubMedCrossRefGoogle Scholar
  409. 409.
    Okuno, H, Akahori, A, Sato, H, Xanthoudakis, S, Curran, T, and Iba, H: Escape from redox regulation enhances the transforming activity of Fos. Oncogene, 8: 695–701, 1993.PubMedGoogle Scholar
  410. 410.
    Walters, DW, and Gilbert, HF: Thiol/disulfide exchange between rabbit muscle phosphofructokinase and glutathione. J. Biol. Chem., 261: 15372–15377, 1986.Google Scholar
  411. 411.
    Cappel, RE, and Gilbert, HF: Thiol/dissulfide exchange between 3-hydroxy-3-methylglutaryl-CoA reductase and glutathione. A thermodynamically facile dithiol oxidation. J. Biol. Chem., 263: 12204–12212, 1988.Google Scholar
  412. 412.
    Keogh, BP, Tresini, M, Cristofalo, VJ, and Allen, RG: Effects of cellular aging on the induction of c-fos by antioxidant treatments. Mech. Ageing Dev., 86: 151–160, 1995.CrossRefGoogle Scholar

Copyright information

© American Aging Association, Inc. 1998

Authors and Affiliations

  • Robert G. Allen
    • 1
  1. 1.Center for Gerontological ResearchAllegheny UniversityPhiladelphia

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