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.
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Harman, D: Aging: a theory based on free radical and radiation biology. J. Gerontol., 11: 298–300, 1956.
Harman, D: Free radicals in aging. Mol. Cell. Biol., 84: 155–161, 1984.
Sohal, RS, and Allen, RG: Oxidative stress as a causal factor in differentiation and aging: a unifying hypothesis. Exp. Geront., 25: 499–522, 1990.
Sohal, RS, Svensson, I, and Brunk, UT: Hydrogen peroxide production by liver mitochondria in different species. Mech. Ageing Dev., 53: 209–215, 1990.
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.
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.
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.
Stadtman, ER, Oliver, CN, Starke-Reed, PE, and Rhee, SG: Age-related oxidation reaction in proteins. Toxicology & Industrial Health, 9: 187–196, 1993.
Stadtman, ER: Protein modification in aging. J. Gerontol., 43: B112–B120, 1988.
Stadtman, ER: Covalent modification reactions are marking steps in protein turnover. Biochemistry, 29: 6323–6331, 1990.
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.
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.
Agarwal, S, and Sohal, RS: Relationship between aging and susceptability to protein oxidative damage. Biochem. Biophys. Res. Commun., 194: 1203–1206, 1993.
Brawn, K, and Fridovich, I: Superoxide radical and superoxide dismutases: threat and defense. Acta Physiol. Scand. Suppl., 492: 9–18, 1980.
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.
Agarwal, S, and Sohal, RS: DNA oxidative damage and life expectancy in houseflies. Proc. Natl. Acad. Sci. USA, 91: 12332–12335, 1994.
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.
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.
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.
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.
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.
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.
Rosen, GM, Barber, MJ, and Rauckman, EJ: Disruption of erythrocyte membrane organization by superoxide. J. Biol. Chem., 258: 2225–2228, 1983.
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.
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.
McCord, JM: Oxygen-derived free radicals in postischemic tissue injury. N. Engl. J. Med., 312: 159–163, 1985.
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.
Oberley, LW: Superoxide dismutases in cancer, in Superoxide Dismutase, edited by Oberley, LW, Boca Raton, FL, CRC Press, 1983, pp. 127–165.
Oberley, LW, and Oberley, TD: The role of superoxide dismutase and gene amplification in carcinogenesis. J. Theor. Biol., 106: 403–422, 1984.
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.
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.
McCord, JM, and Fridovich, I: Superoxide dismutase. J. Biol. Chem., 244: 6049–6055, 1969.
Halliwell, B: Free radicals, oxygen toxicity and aging, in Age Pigments, edited by Sohal, RS, Amsterdam, Elsevier/North Holland, 1981, pp. 1–62.
Foreman, HJ, and Fischer, AB: Antioxidant defenses, in Oxygen and Living Processes, edited by Gilbert, DL, New York, Springer-Verlag, 1981, pp. 65–90.
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.
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.
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.
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.
Beyer, W, Imlay, J, and Fridovich, I: Superoxide dismutases. Prog. Nucl. Acid Res. Mol. Biol., 40: 221–253, 1991.
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.
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.
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.
Marklund, SL: Extracellular superoxide dismutase in human tissues and human cell lines. J. Clin. Invest., 74: 1398–1403, 1984.
Sohal, RS: The free radical hypothesis of aging: an appraisal of the current status. Aging, 5: 3–17, 1993.
Mehlhorn, RJ, and Cole, G: The free radical theory of aging: a critical review. Adv. Free Rad. Biol. Med., 1: 165–223, 1985.
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.
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.
McCord, JM: Human disease, free radicals, and the oxidant/antioxidant balance. Clin. Biochem, 26: 351–357, 1993.
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.
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.
Oberley, LW: Free radicals and diabetes. Free Radic. Biol. Med., 5: 113–124, 1988.
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.
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.
Juurlink, BHJ: Response of glial cells to ischemia-roles of reactive oxygen species and glutathione. Neuroscience & Biobehavioral Reviews, 21: 151–166, 1997.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Sohal, RS, Svensson, I, Sohal, BH, and Brunk, UT: Superoxide radical production in different animal species. Mech. Ageing Dev., 49: 129–135, 1989.
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.
Nohl, H, and Hegner, D: Do mitochondria produce oxygen radicals in vivo? Eur. J. Biochem., 82: 563–567, 1978.
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.
Hegner, D: Age-dependence of molecular and functional changes in biological membranes. Mech. Ageing Dev., 14: 101–118, 1980.
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.
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.
Sohal, RS: Aging, cytochrome oxidase activity, and hydrogen peroxide release by mitochondria. Free Radic. Biol. Med., 14: 583–588, 1993.
Sohal, RS, and Sohal, BH: Hydrogen peroxide release by mitochondria increases during aging. Mech. Ageing Dev., 57: 187–202, 1991.
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.
Rikans, LE, and Moore, DR: Effects of aging on aqueous-phase antioxidants in tissues of male Fischer rats. Biochim. Biophys. Acta., 966: 269, 1988.
Orr, WC, and Sohal, RS: Extension of lifespan by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science, 263: 1128–1130, 1994.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Beal, MF: Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol., 38: 357–366, 1995.
Bowling, AC, and Beal, MF: Bioenergetic and oxidative stress in neurodegenerative disease. Life Sci., 56: 1151–1171, 1995.
Eisen, A: Amyotrophic lateral sclerosis is a multifactorial disease. Muscle and Nerve, 18: 741–752, 1995.
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.
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.
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.
Eisen, AA: Amyotrophic lateral sclerosis: a multifactorial disease. Adv. Neurol., 68: 121–134, 1995.
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.
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.
Mutisya, EM, Bowling, AC, and Beal, MF: Cortical cytochrome oxidase activity is reduced in Alzheimer’s disease. J. Neurochem., 63: 2179–2184, 1994.
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.
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.
Hosler, BA, and Brown, RH: Copper/Zinc superoxide dismutase mutations and free radical damage in amyotrophic lateral sclerosis. Adv. Neurol., 68: 41–46, 1995.
Schapira, AHV: Oxidative stress and mitochondrial dysfunction in neurodegeneration. Curr. Opin. Neurol., 9: 260–264, 1996.
Simonian, NA, and Coyle, JT: Oxidative stress in neurodegenerative disease. Annu. Rev. Pharmacol. Toxicol., 36: 83–106, 1996.
Bergeron, C: Oxidative stress: its role in the pathogenesis of amyotrophic lateral sclerosis. J. Neurol. Sci., 129(Suppl.): 81–84, 1995.
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.
Cudkowicz, ME, and Brown, RH: An update on superoxide dismutase 1 in familial amyotrophic lateral sclerosis. J. Neurol. Sci., 139(Suppl.): 10–15, 1996.
Mulder, DW, Kurland, LT, Offord, KP, and Beard, CM: Familial adult motor neuron disease: amyotrophic lateral sclerosis. Neurol., 36: 511–517, 1986.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Orrell, R, de Belleroche, J, Marklund, S, Bowe, F, and Hallewell, R: A novel SOD mutant and ALS. Nature, 374: 504–505, 1995.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Brown, RH: Superoxide dismutase in familial amyotrophic lateral sclerosis: models for gain of function. Curr. Opin. Neurobiol., 5: 841–846, 1995.
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.
Brown, R: Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell, 80: 687–692, 1995.
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.
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.
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.
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.
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.
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.
Beckman, JS, Carson, M, Smith, CD, and Koppenol, WH: ALS, SOD and peroxynitrite. Nature, 364: 584, 1993.
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.
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.
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.
Lafon-Cazal, M, Pletri, S, Culcasi, M, and Bockaert, J: NMDA-dependant superoxide production and neurotoxicity. Nature, 364: 535–537, 1983.
Beckamn, JS: Ischaemic injury mediator. Nature, 345: 27–28, 1990.
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.
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.
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.
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.
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.
Child, CM: Axial gradients in the early development of the starfish. Am. J. Physiol., 37: 203–219, 1915.
Child, CM: Individuation and reproduction in organisms; Senescence and Rejuvenescence. Chicago, Chicago University Press, 1915,.
Child, CM: Axial susceptibility gradients in the early development of the sea urchin. Biol. Bull., 30: 391–405, 1916.
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.
Child, CM: Physiological dominance and physiological isolation in development and reconstitution. Wilhelm Roux. Arch. Entw. Organ., 113: 556–581, 1929.
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.
Loudon, C: Development of Tenebrio molitor in low oxygen levels. J. Insect Physiol., 34: 97–103, 1988.
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.
Erkell, LJ: Differentiation of mouse neuroblastoma under increased oxygen tension. Exp. Cell Biol., 48: 374–380, 1980.
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.
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.
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.
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.
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.
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.
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.
Sekiba, K, and Yoshioka, T: Changes of lipid peroxidation and superoxide dismutase activity in human placenta. Am. J. Obstetr. Gynecol., 135: 368–371, 1979.
Nakagawara, A, Nathan, CF, and Cohn, ZA: Hydrogen peroxide metabolism in human monocytes during differentiation in vitro. J. Clin. Invest., 68: 1243–1252, 1981.
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.
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.
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.
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.
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.
Smith, J, and Shrift, A: Phylogenetic distribution of glutathione peroxidase. Comp. Biochem. Physiol., 63B: 39–44, 1979.
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.
Anderson, GL: Superoxide dismutase activity in Dauerlarvae of Caenorhabditis elegans (Nematoda: Rhabditidae). Can. J. Zool., 60: 288–291, 1982.
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.
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.
Nickla, H, Anderson, J, and Palzkill, T: Enzymes involved in oxygen detoxification during development of Drosophila melanogaster. Experientia, 39: 610–612, 1983.
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.
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.
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.
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.
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.
Frank, L, and Sosenko, IR: Prenatal development of lung antioxidant enzymes in four species. J. Pediatr., 110: 106–110, 1987.
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.
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.
Russanov, EM, Kirkova, MD, Setchenska, MS, and Arnstein, HRV: Enzymes of oxygen metabolism during erythrocyte differentiation. Biosci. Rep., 1: 927–931, 1981.
Mavelli, I, Mondovi, B, Federico, R, and Rotilio, G: Superoxide dismutase activity in developing rat brain. J. Neurochem., 31: 363–364, 1978.
Tanswell, AK, and Freeman, BA: Pulmonary antioxidant enzyme maturation in the fetal and neonatal rat. I. Development profiles. Pediatr. Res., 18: 584–587, 1984.
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.
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.
Clerch, LB, and Massaro, D: Rat lung antioxidant enzymes: differences in perinatal gene expression and regulation. Am. J. Physiol., 263: L446–L470, 1992.
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.
Chen, Y, and Frank, L: Differential gene expression of antioxidant enzymes in the perinatal rat lung. Pediatr. Res., 34: 27–31, 1993.
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.
Yoshioka, T, Shimada, T, and Sekiba, K: Lipid peroxidation and antioxidants in the rat lung during development. Biol. Neonate, 38: 161–168, 1980.
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.
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.
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.
Shivakumar, BR, Anandatheerthavarada, HK, and Ravindranath, V: Free radical scavenging systems in developing rat brain. Int. J. Devl. Neuroscience, 9: 181–185, 1991.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Paoletti, F, and Mocali, A: Changes in CuZn-superoxide dismutase during induced differentiation of murine erythroleukemia. Cancer Res., 48: 6674–6677, 1988.
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.
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.
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.
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.
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.
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.
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.
Asayama, K, Janco, RL, and Burr, IM: Selective induction of manganous superoxide dismutase in human monocytes. Am. J. Physiol., 249: C393–C397, 1985.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Saffer, JD, Jackson, SF, and Annarella, MB: Developmental expression of Sp1 in the mouse. Mol. Cell. Biol., 11: 2189–2199, 1991.
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.
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.
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.
Beckman, BS, Balin, AK, and Allen, RG: Superoxide dismutase induces differentiation in Friend erythroleukemia cells. J. Cell. Physiol., 139: 370–376, 1989.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Norris, KH, and Hornsby, PJ: Cytotoxic effects of expression of human superoxide dismutase in bovine adrenocortical cells. Mut. Res., 237: 95–106, 1990.
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.
Mao, GD, Thomas, PD, Lopaschuk, GD, and Poznansky, MJ: Superoxide dismutase (SOD)-catalase conjugates. J. Biol. Chem., 268: 416–420, 1993.
Hodgson, EK, and Fridovich, I: The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry, 14: 5294–5299, 1975.
Hodgson, EK, and Fridovich, I: The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry, 14: 5299–5303, 1975.
Paller, MS, and Eaton, JW: Hazards of antioxidant combinations containing superoxide dismutase. Free Radic. Biol. Med., 18: 883–890, 1995.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Keyse, SM, and Emslie, EA: Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase. Nature, 359: 644–647, 1992.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Choi, H-S, and Moore, DD: Induction of c-fos and c-jun gene expression by phenolic antioxidants. Mol. Endocrin., 7: 1596–1602, 1993.
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.
Sen, CK, and Packer, L: Antioxidants and redox regulation of gene transcription. FASEB J., 10: 709–720, 1996.
Sun, Y, and Oberley, LW: Redox regulation of transcriptional activators. Free Radic. Biol. Med., 21: 335–348, 1996.
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.
Monterio, HP, and Stern, A: Redox regulation of tyrosine phosphorylation-dependent signal transduction pathways. Free Radic. Biol. Med., 21: 323–333, 1996.
Bauskin, AR, Alkalay, I, and Ben-Neriah, Y: Redox regulation of protein tyrosine kinase in the endoplasmic reticulum. Cell, 66: 685–696, 1991.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Rao, GN, and Berk, BC: Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression. Circ. Res., 70: 593–599, 1992.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Cerutti, P, Shah, G, Peskin, A, and Amstad, P: Oxidant carcinogenesis and antioxidant defense. Ann. New York Acad. Sci., 663: 158–166, 1992.
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.
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.
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.
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.
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.
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.
Walters, DW, and Gilbert, HF: Thiol/disulfide exchange between rabbit muscle phosphofructokinase and glutathione. J. Biol. Chem., 261: 15372–15377, 1986.
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.
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.
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Allen, R.G. Oxidative stress and superoxide dismutase in development, aging and gene regulation. AGE 21, 47–76 (1998). https://doi.org/10.1007/s11357-998-0007-7
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DOI: https://doi.org/10.1007/s11357-998-0007-7