Morphologic assessment of oxidative damage: A review

Sohal, R.S., and Weindruch, R.: Oxidative stress, caloric restriction, and aging. Science, 273: 59–63, 1996.

Chance, B., Sies, H., and Boveris, A.: Hydroperoxide metabolism is mammalian organs. Physiol. Rev., 59: 527–605, 1979.

Sohal, R.S., Ku, H.H., Agarwal, S., Forster, M.J., and Lal, H.: Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse. Mech. Ageing Dev., 74: 121–133, 1994.

Pansarasa, O., Bertorelli, L., Vecchiet, J., Felzani, G., and Marzatico, F.: Age-dependent changes of antioxidant activities and markers of free radical damage in human skeletal muscle. Free Radic. Biol. Med., 27: 617–622, 1999.

Mecocci, P., Fano, G., Fulle, S., MacGarvey, U., Shinobu, L., Polidori, M.C., Cherubini, A., Vecchiet, J., Senin, U., and Beal, M.F.: Age-dependent increases in oxidative damage to DNA, lipids, and proteins in human skeletal muscle. Free Radic. Biol. Med., 26: 303–308, 1999.

Pugh, T.D., Oberley, T.D., and Weindruch, R.: Dietary intervention at middle age: caloric restriction but not dehydroepiandrosterone sulfate increases life span and lifetime cancer incidence in mice. Cancer Res., 59: 1642–1648, 1999.

Yan, T., Jiang, X., Zhang, H.J., Li, S., and Oberley, L.W.: Use of commercial antibodies for detection of primary antioxidant enzymes. Free Radic. Biol. Med., 25: 688–693, 1998.

Uchida, K., Itakura, K., Kawakishi, S., Hiai, H., Toyokuni, S., and Stadtman, E.R.: Characterization of epitopes recognized by 4-hydroxy-2-nonenal specific antibodies. Arch. Biochem. Biophys., 324: 241–248, 1995.

Uchida, K., Szweda, L.I., Chae, H-Z., and Stadtman, E.R.: Immunochemical detection of 4-hydroxy-2-nonenal protein adducts in oxidized hepatocytes. Proc. Natl. Acad. Sci. USA, 90: 8742–9846, 1993.

Toyokuni, S., Miyake, N., Hiai, H., Hagiwara, M., Kawakishi, S., Osawa, T., and Uchida, K.: The monoclonal antibody specific for the 4-hydroxy-2-nonenal histidine adduct. FEBS Lett., 359: 189–191, 1995.

Toyokuni, S., Tanaka, T., Hattori, Y., Nishiyama, Y., Yoshida, A., Uchida, K., Ochi, H., and Osawa, T.: Quantitative immunohistochemical determination of 8-hydroxy-2′-deoxyguanosine by a monoclonal antibody N45.1: its application to ferric nitrilo-triacetate-induced renal carcinogenesis model. Lab. Invest., 76: 365–374, 1997.

MacMillen-Crow, L.A., Crow, J.P., Kerby, J.D., Beckman, J.S., and Thompson, J.A.: Nitration and inactivation of manganese superoxide dismutase in chronic rejection of renal allograft. Proc. Natl. Acad. Sci. USA, 93: 11853–11858, 1996.

Smith, M.A., Sayre, L.M., Anderson, V.E., Harris, P.L.R., Beal, M.F., Kowall, N., and Perry, G.: Cytochemical determination of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine. J. Histochem. Cytochem., 46: 731–735, 1998.

Toyokuni, S.: Reactive oxygen species-induced molecular damage and its application in pathology. Path. Int., 49: 401–410, 1999.

Kondo, S., Toyokuni, S., Iwasa, Y., Tanake, T., Onodera, H., Hiai, H., and Imamura M.: Persistent oxidative stress in human colorectal carcinoma, but not in adenoma. Free Radic. Biol. Med., 27: 401–410, 1999.

Coursin, D.B., Cihla, H.P., Oberley, T.D., and Oberley, L.W.: Immunolocalization of antioxidant enzymes and isozymes of glutathione S-transferase in normal rat lung. Am. J. Physiol., 263: L679–L691, 1992.

Weisiger, R.A., and Fridovich, I.: Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial location. J. Biol. Chem., 248: 4793–4796, 1973.

McCord, J.M., and Fridovich, I.: Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem., 244: 6049–6055, 1969.

Marklund, S.L., Holme, E., and Hellner, L.: Superoxide dismutase in extracellular fluids. Clin. Chim. Acta, 126: 41–51, 1982.

Peeters-Joris, C., Vandervoorde, A.M., and Bandhuin, P.: Subcellular localization of superoxide dismutase in rat liver. Biochem. J., 150: 31–39, 1975.

Muse, K.E., Oberley, T.D., Sempf, J.M., and Oberley, L.W.: Immunolocalization of antioxidant enzymes in adult hamster kidney. Histochem. J., 26: 734–753, 1994.

Vertechy, M., Cooper, M.B., Ghirardi, O., and Ramacci, M.T.: Antioxidant enzyme activities in heart and skeletal muscle of rats of different ages. Exp. Gerontol., 24:211–218, 1989.

Ji L.L., Dillon, D., and Wu, E.: Alteration of antioxidant enzymes with aging in rat skeletal muscle and liver. Am. J. Physiol., 258: R918–R923, 1990.

Oh-Ishi, S., Kisaki, T., Yamashita, H., Nagata, N., Suzuki, K., Taniguchi, N., and Ohno, H.: Alterations of superoxide dismutase iso-enzyme activity, content, and mRNA expression with aging in skeletal muscle. Mech. Ageing Dev., 84: 65–76, 1995.

Oberley, T.D., Oberley, L.W., Slattery, A.F., Lauchner, L.J., and Elwell, J.H.: Immunohistochemical localization of antioxidant enzymes in adult Syrian hamster tissues and during kidney development. Am. J. Path., 137: 199–214, 1990.

Oberley, T.D., Oberley, L.W., Slattery, A.F., and Elwell, J.H.: Immunohistochemical localization of glutathione S-transferase and glutathione peroxidase in adult hamster tissues and during kidney development. Am. J. Path., 139: 355–369, 1991.

Oberley, T.D., Friedman, A.L., Moser, R., and Siegel, F.L.: Effects of lead administration on developing rat kidney. II. Functional, morphologic, and immunohistochemical studies. Toxicol. and Applied Pharmacol., 131: 94–107, 1995.

Daggett, D.A., Oberley, T.D., Nelson, S.A., Wright, L.S., Kornguth, S.E., and Siegel, F.L.: Effects of lead on rat kidney and liver: GST expression and oxidative stress. Toxicology, 128: 191–206, 1998.

Arai, M., Imai, H., Koumura, T., Yoshida, M., Emoto, K., Umeda, M., Chiba, N., and Nakagawa, Y.: Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells. J. Biol. Chem., 274: 4924–4933, 1999.

Bulitta, C., Ganea, C., Fahimi, H.D., and Volkl, A.: Cytoplasmic and peroxisomal catalases of the guinea pig liver: evidence for two distinct proteins. Biochim. et Biophys. Acta, 1293: 55–62, 1996.

Swaroop, M., Bian, J., Aviram, M., Duan, H., Bisgaier, C.L., Loo, J.A., and Sun, Y.: Expression, purification, and biochemical characterization of SAG, a ring finger redox-sensitive protein. Free Radic. Biol. Med., 27: 193–202, 1999.

Oberley, T.D., and Oberley, L.W.: Antioxidant enzyme levels in cancer. Histol. Histopath., 12: 525–535, 1997.

Tsai, L., Szweda, P.A., Vinogradova, O., and Szweda, L.I.: Structural characterization and immunochemical detection of a fluorophore derived from 4-hydroxy-2-nonenal and lysine. Proc. Natl. Acad. Sci. USA, 95: 7975–7980, 1998.

Zainal, T.A., Weindruch, R., Szweda, L.I., and Oberley, T.D.: Localization of 4-hydroxy-2-nonenal-modified proteins in kidney following iron overload. Free Radic. Biol. Med., 26:1181–1193, 1999.

Brennick, J.B., O’Connell, J.V., Dickerson, G.R., and Young, R.H.: Lipofuscin accumulation (so-called “melanosis”) of the prostate. Am. J. Surg. Path., 18: 446–454, 1994.

Amin, M.B., and Bostwick, D.B.: Pigment in prostatic epithelium and adenocarcinoma: a potential source of diagnostic confusion with seminal vesicle epithelium. Modern Pathol., 9: 791–795, 1996.

Oberley, T.D., Toyokuni, S., and Szweda, L.I.: Localization of hydroxynonenal protein adducts in normal human kidney and selected human kidney cancers. Free Radic. Biol. Med., 27: 693–703, 1999.

Ahn, B., Han, B.S., Kim, D.J., and Oshima, H.: Immunohistochemical localization of inducible nitric oxide synthase and 3-nitrotyrosine in rat liver tumors induced by N-nitrosodiethylamine. Carcinogenesis, 20: 1337–1344, 1999.

Yoritaka, A., Hattori, N., Uchida, K., Tanaka, M., Stadtman, E.R., and Mizuno, Y.: Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson’s disease. Proc. Natl. Acad. Sci. USA, 93: 2696–2701, 1996.

Montine, K.S., Olson, S.J., Amarnath, V., Whetsell, W. Jr., Graham, D.J., and Montine, T.J.: Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer’s disease is associated with inheritance of APOE4. Am J. Path., 150: 437–443, 1997.

Gurney, M.E., Pu, H., Chiu, A.Y., Dal Canto, M.C., Polchow, C.Y., Alexander, D.D., Caliendo, J., Hentati, A., Kwon, Y.W., Deng, H-X., Chen, W., Zhai, P., Sufit, R.L., and Siddique, T.: Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science, 264: 1772–1775, 1995.

Flood, D.G., Reaume, A.G., Gruner, J.A., Hoffman, E.K., Hirsch, J.D., Lin, Y-G., Dorfman, K.S., and Scott, R.W.: Hindlimb motor neurons require Cu/Zn superoxide dismutase for maintenance of neuromuscular junctions. Am. J. Path., 155: 663–672, 1999.

Anson, R.M., Senturker, S., Dizdaroglu, M., and Bohr, V.: Measurement of oxidatively induced base lesions in liver from Wistar rats of different ages. Free Radic. Biol. Med., 27: 456–452, 1999.

Ando, Y., Nyhlin, N., Suhr, O., Holmgren, G., Uchida, K., Sahly, M.E., Yamashita, T., Terasaki, H., Makamura, M., Uchino, M., and Ando, M.: Oxidative stress is found in amyloid deposits in systemic amyloidosis. Biochem. Biophys. Res. Comm., 232: 497–502, 1997.

Ohhira, M., Ohtake, T., Matsumoto, A., Saito, H., Ikuta, K., Fujimoto, Y., Ono, M., Toyokuni, S., Kohgo, Y.: Immunohistochemical detection of 4-hydroxy-2-nonenal-modified-protein adducts in human alcoholic liver disease. Alcohol Clin. Exp. Res., 22: S145–S149, 1997.

Kageyama, F., Kobayashi, Y., Koide, S.: Enhanced lipid peroxidation in chronic hepatitis C. Jpn. Pharmacol. Ther., 26: S405–S408, 1998.

Lee, C-K., Klopp, R.G., Weindruch, R., and Prolla, T.A.: Gene expression profile of aging and its retardation by caloric restriction. Science, 285: 1390–1393, 1999.

Bates, P.C., and Millward, D.J. Myofibrillar protein turnover. Biochem. J., 214: 587–592, 1983.

Kerver, E.D., Vogels, I.M., Bosch, K.S., Vreeling-Sindelavarova, H., van den Munckhof, R.J.M., and Frederiks, W.M.: In situ detection of spontaneous superoxide anion and singlet oxygen production by mitochondria in rat liver and small intestine. Histochem. J., 29: 229–237, 1997.

Uchida, K., Shiraishi, M., Naito, Y., Torii, Y., Nakamura, Y., and Osawa, T.: Activation of stress signaling pathways by the end product of lipid peroxidation: 4-hydroxy-2-nonenal is a potent inducer of intracellular peroxide production. J. Biol. Chem., 274: 2234–2242, 1999.

Eiserich, J.P., Estevez, A.G., Bamberg, T.V., Ye, Y.Z., Chumley, P.H., Beckman, J.S., and Freeman, B.A.: Microtubule dysfunction by posttranslational nitrotyrosination of a-tubulin: A nitric oxide-dependent mechanism of cellular injury. Proc. Natl. Acad. Sci. USA, 96: 6365–6370, 1999.

Yen, H-C., Oberley, T.D., Vichitbanda, S., Ho, Y-S., and St. Clair, D.K.: The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice. J. Clin. Invest., 98: 1253–1260, 1996.

Yen, H-C., Oberley, T.D., Gairola, C.G., Szweda, L.I., and St. Clair, D.K.: Manganese superoxide dismutase protects mitochondrial complex I against adriamycin-induced cardiomyopathy in transgenic mice. Arch. Biochem. Biophys., 362: 59–66, 1999.