Abstract
A role of protein oxidation in aging is indicated by the following observations: The cellular level of oxidized protein increases with animal age. Age-related changes in enzyme activities can be mimicked by treatment of enzymes from young animals with reactive oxygen species (ROS) in vitro. Exposure of animals to conditions of oxidative stress leads to an increase in the intracellular level of oxidized protein. Factors that increase the life span of animals lead also to a decrease in the level of oxidized protein and vice versa. Many age-related diseases are associated with elevated levels of oxidized proteins. Some age-related changes in enzyme activities and cognitive functions can be reversed by exposing old animals to free radical spin traps. The age-related increase in oxidized proteins is a complex function of the balance between a multiplicity of prooxidants, antioxidants, and the activities of proteases that selectively degrade the oxidized forms of proteins.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Agarwal, S. and Sohal, R. S., 1993, Relationship between aging and susceptibility to protein oxidative damage, Biochem. Biophys. Res. Commun. 194, 1203–1206.
Ames, B. N., Shigenaga, M. K., and Hagen, T. M., 1993, Oxidants, antioxidants, and the degenerative diseases of aging, Proc. Natl. Acad. Sci. USA 90, 7915–7922.
Amici, A., Levine, R. L., Tsai, L., and Stadtman, E. R., 1989, Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed reactions, J. Biol. Chem. 264, 3341–3346.
Amstad, P., Moret, R., and Cerotti, P., 1994, Glutathione peroxidase compensates for the hypersensitivity of Cu,Zn-superoxide dismutase overproducers to oxidant stress, J. Biol. Chem. 269, 1606–1609.
Ando, Y., Nyhlin, N., Suhr, O., Holmgren, G., Uchida, K., Sahly, M. E., Yamashita, T., Terasaki, H., Nakamura, M., Uchino, M., and Ando, M., 1997, Oxidative stress is found in amyloid deposits in systemic amyloidosis, Biochem. Biophys. Res. Commun. 232, 497–502.
Ayene, I. S., Dodia, C., and Fisher, A. B., 1992, Role of oxygen in oxidation of lipid and protein during ischemia/reperfusion in isolated perfused rat lung, Arch. Biochem. Biophys. 296, 183–189.
Bandy, B. and Davison, A. J., 1990, Mitochondrial mutations may increase oxidative stress: Implications for carcinogenesis and aging, Free Rad. Biol. Med. 8, 523–539.
Benzi, G. and Moretti, A., 1995, Age-and peroxidative stress-related modifications of the cerebral enzymatic activities linked to mitochondria and the glutathione system, Free Rad. Biol. Med. 19, 77–101.
Bowling, A. C., Schultz, J. B., Brown, Jr., R. H., and Beal, M. F., 1993, Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism I familial and sporadic amyotrophic lateral sclerosis, J. Neurochem. 61, 2322–2325.
Butterfield, D. A., Howard, B. J., Yatin, S., Allen, K. L., and Carney, J. M., 1997, Free radical oxidation of brain proteins in accelerated senescence and its modulation by N-tert-butyl-a-phenylnitrone, Proc. Natl. Acad. Sci. USA 94, 674–678.
Carney, J. M., Smith, C. D., Carney, A. M., and Butterfield, D. A., 1994, Aging-and oxygen-induced modifications in brain biochemistry and behavior, in: Aging and Cellular Defense Mechanisms, Volume 63 ( Franceschi, C., Crepaldi, G., Cristofalo, V. J., and Vijg, J., eds.), pp. 110–119, New York Academy of Science, New York.
Carney, J. M., Starke-Reed, R E., Oliver, C. N., Landum, R. W., Cheng, M. S., Wu, J. F., and Floyd, R.A., 1991, Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity loss and loss of temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-aphenylnitrone, Proc. Natl. Acad. Sci. USA 88, 3633–3636.
Chao, C.-C., Ma, Y.-S., and Stadtman, E. R., 1997, Modification of protein surface hydrophobicity and methionine oxidation by oxidative stress, Proc. Natl. Acad. Sci. USA 94, 2969–2974.
Chapman, M. L., Rubin, B. R., and Gracy, R. W., 1989, Increased carbonyl content of proteins in synovial fluid from patients with rheumatoid arthritis, J. Rheumatol. 16, 15–18.
Chauhan, A., Chauhan, V. P. S., Brockerhoff, H., and Wisniewski, H. M., 1991, Action of amyloid -protein on protein kinase C activity, Life Sci. 49, 1555–1556.
Cordillo, E., Ayala, A., F.-Lobato, M., Bautista, J., and Machada, A., 1988, Possible involvement of histidine resi-dues in loss of enzymatic activity of rat liver malic enzyme during aging, J. Biol. Chem. 263, 8053–8057.
Cross, C. E., Reznick, A. Z., Packer, L., Davis, P. A., Suzuki, Y. J., and Halliwell, B., 1992, Oxidative damage to human plasma proteins by ozone, Free Rad. Res. Commun. 15, 347–352.
Davies, K. J. A., 1986, Intracellular proteolytic systems may function as secondary antioxidant defenses: A Hypothesis, J. Free Rad. Biol. Med. 2, 155–173.
Davies, K. J. A., 1986a, The role of intracellular proteolytic systems in antioxidant defense, In: Superoxide and superoxide dismutase in chemistry, biology, and medicine ( Rotilio, G., ed.), pp. 443–450, Elsevier Science Publishing, Amsterdam.
Davies, K. J. A. and Goldberg, A. L., 1987, Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells, J. Biol. Chem. 262, 8227–8234.
Davies, K. J. A. and Lin, S. W., 1988, Degradation of oxidatively denatured proteins in Escherichia coli, Free Rad. Biol. Med. 5, 215–223.
Davies, K. J. A. and Lin, S. W., 1988a, Oxidatively denatured proteins are degraded by an ATP-independent proteolytic pathway in Escherichia coli, Free Rad. Biol. Med. 5, 225–236.
Davies, K. J. A., Delsignore, M. E., and Lin, S. W., 1987, Protein damage by oxygen radicals. II. Modification of amino acids, J. Biol. Chem. 262, 9902–9907.
Dreyfus, J. C., Kahn, A., and Schapira, F., 1978, Post translational modifications of enzymes, Curl: Top. Cell. Regul. 14, 243–297.
Forster, M. J., Dubey, A., Dawson, K. M., Stutts, W. A., Lal, H., and Sohal, R. S., 1996, Age-related losses of cognitive function and motor skills in mice are associated with oxidative protein damage in the brain, Proc. Natl. Acad. Sci. USA 93, 4765–4769.
Friguet, B., Stadtman, E. R., and Szweda, L., 1994, Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal, J. Biol. Chem. 269, 21639–21643.
Friguet, B., Szweda, L., and Stadtman, E. R., 1994, Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease, Arch. Biochem. Biophys. 311, 168–173.
Fucci, L., Oliver, C. N., Coon, M. J., and Stadtman, E. R., 1983, Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implications in protein turnover and aging, Proc. Natl. Acad. Sci. USA 80, 1521–1525.
Fulks, R. M., 1977, Regulation of glutamine synthetase degradation in Klebsiella aerogenes, Fed. Proc. Am. Soc. Exptl. Biol. 36, 919 (abstr.).
Garland, D., Russell, P., and Zigler, J. S., 1988, The oxidative modification of lens protein, In: Oxygen Radicals in Biology and Medicine (Simic, M. G., Taylor, K. S., Ward, J. F., and von Sontag, V., eds.), pp. 347–353, Plenum, New York.
Garrison, W. M., 1987, Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins, Chem. Rev. 87, 381–398.
Gerschman, R., Gilbert, D. I., and Caccamise, D., 1988, Effect of various substances on survival times of mice exposed to different high oxygen tension, Am. J. Physiol. 192, 563–571.
Gladstone, I. M. and Levine, R. L., 1994, Oxidation of proteins in neonatal lungs, Pediatrics 93, 764–768.
Goldstein, I. M., Kaplan, H. B., Edelson, H. S., and Weissmann, G., 1979, Ceruloplasmin. A scavenger of superoxide anion radicals, J. Biol. Chem. 254, 4040–4045.
Grant, A. J., Jessup, W., and Dean, R. J., 1993, Inefficient degradation of oxidized regions of protein molecules, Free Rad. Res. Commun. 18, 259–267.
Grune, T., Reinheckel, T., and Davies, K. J. A., 1996, Degradation of oxidized proteins in K562 human hematopoietic cells by proteosome, J. Biol. Chem. 271, 15504–15509.
Grune, T., Reinheckel, T., Joshi, M., and Davies, K. J. A., 1995, Proteolysis in cultured liver epithelial cells during oxidative stress, J. Biol. Chem. 270, 2344–2351.
Harris, M., Hensley, K., Butterfield, D. A., Leedle, R. A., and Carney, J. M., 1995, Direct evidence of oxidative injury produced by Alzheimer’s -amyloid peptide (1–40) in cultured hippocampal neurons, Exp. Neurol. 131, 193–202.
Krsek-Staples, J. A. and Webster, R. 0., 1993, Ceruloplasmin inhibits carbonyl formation in endogenous cell proteins, Free Rad. Biol. Med. 14, 115–125.
Kelley, F. J. and Birch, S., 1993, Ozone exposure inhibits cardiac protein synthesis in the mouse, Free Rad. Biol. Med. 14, 443–446.
Ku, H.-H. and Sohal, R. S., 1993, Comparison of mitochondrial pro-oxidant generation and antioxidant defenses between rat and pigeon: Possible basis of variation in longevity and metabolic potential, Mech. Ageing Develop. 72, 67–76.
Levine, R. L., 1983, Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue, J. Biol. Chem. 258, 11823–11827.
Levine, R. L., 1983a, Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system, J. Biol. Chem. 258, 11828–11833.
Levine, R. L., Williams, J. A., Stadtman, E. R., and Schacter, E., 1994, Carbonyl assays for determination of oxidatively modified proteins, Methods Enzymol. 233, 346–357.
Levine, R. L., Garland, D., Oliver, C. N., Amici, A., Climent, I., Lenz, A. G., Ahn, B.-W., Shaltiel, S., and Stadt-man, E. R., 1990, Determination of carbonyl groups in oxidatively modified proteins, Methods Enzymol. 186, 464–478.
Levine, R. L., Oliver, C. N., Fulks, R. M., and Stadtman, E. R., 1981, Turnover of bacterial glutamine synthetase: Oxidative inactivation precedes proteolysis, Proc. Natl. Acad. Sci. USA 78, 2120–2124.
Lin, F., Thomas, J. P., and Girotti, A. W., 1993, Hyperexpression of catalase in selenium-deprived murine L1210 cell, Arch. Biochem. Biophys. 305, 176–185.
Liu, Y., Rosenthal, R. E., Starke-Reed, P.E., and Fiskum, G., 1993, Inhibition of postcardiac arrest brain protein oxidation by acetyl-L-carnitine, Free Rad. Biol. Med. 15, 667–670.
Marcillat, O., Zhang, Y., Lin, S. W., and Davies, K. J. A., 1988, Mitochondria contain a proteolytic system which can recognize and degrade oxidatively denatured proteins, Biochem. J. 254, 677–683.
Maria, C. S., Revilla, E., P. de la Cruz, C., and Machado, A., 1995, Cu,Zn-superoxide dismutase during aging, FEBS Lett. 347, 85–88.
Matsuo, M., 1993, Age-related alterations in antioxidant defense, In: Free Radicals in Aging ( Yu, B.P., ed.), pp. 143–181, CRC Press, Ann Arbor.
Mickel, H. S., Oliver, C. N., and Starke-Reed, P. E., 1990, Protein oxidation and myelinolysis occur in brain following rapid correction of hyponatremia, Biochem. Biophys. Res. Commun. 172, 92–97.
Mordente, A., Martorana, G. E., Miggiano, G. A. D., Meucci, E., Santini, S. A., and Castelli, A., 1988, Mixed function oxidation and enzymes: Kinetic and structural properties of oxidatively modified alkaline phosphatase, Arch. Biochem. Biophys. 264, 502–509.
Murakami, K., Jahnegn, J. H., Li, S. W., Davies, K. J. A., and Taylor, A., 1990, Lens proteosome shows enhanced rates of degradation of hydroxyl radical modified alpha-crystallin, Free Rad. Biol. Med. 8, 217–222.
Murphy, M. E. and Kherer, J. P., 1989, Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy, Biochem. J. 260, 359–364.
Muscari, C., Frascaro, M., Guamieri, C., and Calderara, C. M., 1990, Mitochondrial function and superoxide gen-eration from submitochondrial particles of aged rat hearts, Biochem. Biophys. Acta 1015, 200–204.
Musci, G., Bonaccorsi di Patti, M. C., Fagiolo, U., and Calabrese, L., 1993, Age-related changes in human cern-loplasmin, J. Biol. Chem. 268, 13388–13395.
Nohl, H., Breuninger, V., and Hegner, D., 1978, Influence of mitochondria) radical formation on energy-linked respiration, Eur. J. Biochem. 90, 385–390.
Oliver, C. N., 1987, Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils, Arch. Biochem. Biophys. 253, 62–72.
Oliver, C. N., Starke-Reed, P. E., Stadtman, E. R., Liu, G. J., Carney, J. M., and Floyd, R. A., 1990, Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia-reperfusion-induced injury to gerbil brain, Pmc. Natl. Acad. Sci. USA 87, 5144–5147.
Oliver, C. N., Ahn, B.-W., Moerman, E. J., Goldstein, S., and Stadtman, E. R., 1987, Age-related changes in oxidized proteins, J. Biol. Chem. 262, 5488–5491.
Oliver, C. N., Ahn, B., Wittenberger, M. E., and Stadtman, E. R., 1985, Oxidative inactivation of enzymes: Implication in protein turnover and aging, In: Cellular Regulation and Malignant Growth ( Ebashi, S., ed.), pp. 320–331, Japan Sci. Soc. Press/Springer-Verlag, Berlin.
Oliver, C. N., Ahn, B., Wittenberger, M. E., Levine, R. L., and Stadtman, E. R., 1985a, Age-related alterations of enzymes may involve mixed-function oxidation reactions, In: Modification of proteins during aging ( Adelman, R. C. and Dekker, E. E., eds.), pp. 39–52, Alan R. Liss, New York.
Oliver, C. N., Fulks, R., Levine, R. L., Fucci, L., Rivett, A. J., Roseman, J. E., and Stadtman, E. R., 1984, Oxida-tive inactivation of key metabolic enzymes during aging, In: Molecular Basis of Aging ( Roy, A. K. and Chattetjee, B., eds.), pp. 235–262, Academic Press, New York.
Oliver, C. N., Fucci, L., Levine, R. L., Wittenberger, M. E., and Stadtman, E. R., 1982, Inactivation of key metabolic enzymes by P450 linked mixed function oxidation systems, In: Cytochrome P-450, Biochemistry, Biophysics, and Environmental Implications ( Heitanen, E., Laitinen, M., and Hanninen, O., eds.), pp. 531–539, Elsevier Biomedical Press, Amsterdam.
Oliver, C. N., Levine, R. L., and Stadtman, E. R., 1982, Regulation of glutamine synthetase degradation, In: Experience in Biochemical Perception ( Ornston, L. N. and Sligar, S. G., eds.), pp. 233–249, Academic Press, New York.
Oliver, C. N., Levine, R. L., and Stadtman, E. R., 1981, Regulation of glutamine synthetase degradation, In: Metabolic interconversion of enzymes ( Holzer, H., ed.), pp. 259–268, Springer-Verlag, Berlin.
Orr, W. C. and Sohal, R. S., 1994, Extension of life-span by over expression of superoxide dismutase and catalase in Drosophila melanogaster, Science 263, 1128–1130.
Osaki, S., 1966, Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin), J. Biol. Chem. 241, 5053–5059.
P. de la Cruz, C.P., Revilla, E., Venero, J. L., Ayala, A., Cano, J., and Machado, A., 1996, Oxidative inactivation of tyrosine hydroxylase in Substantia nigra of aged rat, Free Rad. Biol. Med. 20, 53–61.
Pacifici, R. E., Salo, D. C., and Davies, K. J. A., 1989, Macroproteinase (M.O.P.): A 670 kDA proteinase complex that degrades oxidatively denatured proteins in red blood cells, Free Rad. Biol. Med. 7, 521–536.
Perez, R., Lopez, M., and Barja-De Quiroga, G., 1991, Aging and lung antioxidant enzymes, glutathione and lipid peroxidation in the rat, Free Rad. Biol. Med. 10, 35–39.
Poston, J. M. and Parenteau, G. L., 1992, Biochemical effects of ischemia on isolated perfused rat heart tissues, Arch. Biochem. Biophys. 295, 35–41.
Raddk, Z., Asano, K., Lee, K.-C., Ohno, H., Nakamura, A., Nakamoto, H., and Goto, S., 1997, High altitude training increases reactive carbonyl derivatives but not lipid peroxidation in skeletal muscle of rats, Free Rad. Biol. Med. 22, 1109–1114.
Reznick, A. Z., Cross, C. E., Hu, M.-L., Suzuki, Y. J., Khwaja, S., Safadi, A., Motchnik, P. A., Packer, L., and Halliwell, B., 1992, Modification of plasma proteins by cigarette smoke as measured by protein carbonyl formation, Biochem. J. 286, 607–611.
Rivett, A. J., 1986, Regulation of intracellular protein turnover: Covalent modification as a mechanism of marking proteins for degradation, Curr. Top. Cell. Regul. 28, 291–337.
Rivett, A. J., 1985, Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian protease, J. Biol. Chem. 260, 300–305.
Rivett, A. J., 1985a, Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase, J. Biol. Chem. 260, 12600–12606.
Rivett, A. J., Roseman, J. E., Oliver, C. N., Levine, R. L., and Stadtman, E. R., 1985, Covalent modification of proteins by mixed-function oxidation: Recognition by intracellular proteases, In: Intracellular Protein Catabolism ( Khairallan, E. A., Bond, J. S., and Bird, J. W. C., eds.), pp. 317–328, Alan R. Liss, Inc., New York.
Roseman, J. E. and Levine, R. L., 1987, Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase, J. Biol.Chem. 262, 2101–2110.
Rothstein, M., 1977, Recent developments in age-related alteration of enzymes. Mech. Aging and Dev. 6, 241–257.
Salo, D. C., Lin, S. W., Pacifici, R.E., and Davies, K. J. A., 1988, Superoxide dismutase is preferentially degraded by a proteolytic system from red blood cells following oxidative modification by hydrogen peroxide, Free Rad. Biol. Med. 5, 335–339.
Samokyszyn, V. M., Miller, D. M., Reif, D. W., and Aust, S. D., 1989, Inhibition of superoxide and ferritin-dependent lipid peroxidation by ceruloplasmin, J. Biol Chem. 264, 21–36.
Sawada, M. and Carlson, J. C., 1987, Changes in superoxide radical and lipid peroxide formation in brain, heart, and liver during lifetime of the rat, Mech. Aging and Dev. 41, 125–137.
Shacter, E., Williams, J. A., and Levine, R. L., 1995, Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation, Free Rad. Biol. Med. 18, 815–821.
Shacter, E., Williams, J. A., Lim, M., and Levine, R. L., 1994, Differential susceptibility of plasma proteins to oxi- dative modification: Examination by Western blot immunoassay, Free Rad. Biol. Med. 17, 429–437.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., and Floyd, R. A., 1991, Excess brain protein oxidation and enzyme dysfunction in normal and Alzheimer’s disease, Proc. Natl. Acad. Sci. USA 88, 10540–10543.
Smith, M. A., Perry, P. L., Sayre, L. M., Anderson, V. E., Beal, M. F., and Kowall, N., 1996, Oxidative damage in Alzheimer’s disease, Nature 382, 120–121.
Smith, M. A., Rudnicka-Nawrot, M., Richey, R. L., Praprotnik, D., Mulvihill, P., Miller, C. A., Sayre, C. A., and Perry, G., 1995, Carbonyl-related posttranslational modification of neurofilament protein in neurofibrillary pathology of Alzheimer’s disease, J. Neurochem. 64, 2660–2666.
Sohal, R. S., 1993, The free radical hypothesis of aging: An appraisal of the current status, Aging Clin. Exp. Res. 5, 3–17.
Sohal, R. S. and Dubey, A., 1994, Mitochondrial oxidative damage, hydrogen peroxide release, and aging, Free Rad. Biol. Med. 16, 621–626.
Sohal, R. S., Agarwal, S., and Sohal, B. H., 1995, Oxidative stress and aging in the Mongolian gerbil (Meriones unguiculatus), Mech. Aging and Development 81, 15–25.
Sohal, R. S., Ku, H.-H., Agarwal, S., Forster, M. J., and Lal, H., 1994, Mech. Aging and Dis. 79, 121–133.
Sohal, R. S., Agarwal, S., Dubey, A., and Orr, W. C., 1993, Protein oxidative damage is associated with life expectancy of houseflies, Proc. Natl. Acad. Sci. USA 90, 7255–7259.
Sohal, R. S., Ku, H.-H., and Agarwal, S., 1993, Biochemical correlates of longevity in two closely related rodent species, Biochem. Biophys. Res. Commun. 196, 7–11.
Sohal, R. S., Arnold, L. A., and Sohal, B. H., 1990, Age-related changes in antioxidant enzymes and prooxidant generation in tissues of the rat with special reference to parameters in two insect species, Free Rad. Biol. Med. 10, 495–500.
Spoerri, P. E., 1984, Mitochondrial alterations in aging mouse neuroblastoma cells in culture. Monogr. Dev. Biol. 17, 210–220.
Stadtman, E. R., 1992, Protein oxidation and aging, Science 257, 1220–1224.
Stadtman, E. R., 1986, Oxidation of proteins by mixed-function oxidation systems: Implication in protein turnover, aging, and neutrophil function, Trends Biochem. Sci. 11, 11–12.
Stafford, R. E., Mak, T. M., Kramer, J. H., and Weglicki, W. B., 1993, Protein oxidation in magnesium deficient rat brains and kidneys, Biochem. Biophys. Res. Commun. 196, 596–600.
Starke, P. E., Oliver, C. N., and Stadtman, E. R., 1987, Modification of hepatic proteins in rats exposed to high oxygen concentration, FASEB J. 1, 36–39.
Starke-Reed, P. E. and Oliver, C. N., 1989, Protein oxidation and proteolysis during aging and oxidative stress, Arch. Biochem. Biophys. 275, 559–567.
Szweda, L. I. and Stadtman, E. R., 1992, Iron-catalyzed oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc. mesenteroides, J. Biol. Chem. 267, 3096–3100.
Takahashi, R. and Goto, S., 1990, Alteration of aminoacyl-tRNA synthetase with age: Heat labilization of the enzyme by oxidative damage, Arch. Biochem. Biophys. 277, 228–233.
Takahashi, R., and Goto, S., 1987, Influence of dietary restriction on accumulation of heat-labile enzyme molecules in the liver and brain of mice, Arch. Biochem. Biophys. 257, 200–206.
Toyokuni, S. Uchida, K., Okamoto, K., Hattori-Nakakuki, Y., Hiai, H., and Stadtman, E. R., 1994, Formation of 4-hydroxy-2-nonenal-modified proteins in the renal proximal tubules of rats treated with a renal carcinogen ferric nitrilotriacetate, Proc. Natl. Acad. Sci. USA 91, 2616–2620.
Uchida, K. and Stadtman, E. R., 1993, Covalent modification of 4-hydroxynonenal to glyceraldehyde-3-phosphate, J. Biol. Chem. 268, 6388–6393.
Uchida, K., Toyokuni, S., Nishikawa, K., Kawakishi, S., Oda, H., Hiai, H., and Stadtman, E. R., 1994, Michael addition-type 4-hydroxy-2-nonenal adducts in modified low density lipoproteins: Markers for atherosclerosis, Biochemistry 33, 12487–12494.
Wieland, P. and Lauterburg. B. H., 1995, Oxidation of mitochondrial proteins, DNA following administration of ethanol, Biochem. Biophys. Res. Commun. 213, 815–819.
Winter, M. L. and Liehr, J. G., 1991, Free radical-induced carbonyl content in protein of estrogen-treated hamsters assayed by sodium boro[3H]hydride reduction, J. Biol. Chem. 266, 14446–14450.
Witt, E. H., Reznick, A. Z., Viguie, C. A., Starke-Reed, P. E., and Packer, L. (1992) Exercise, oxidative damage, and effects of antioxidant manipulation, J. Nute 122, 766–773.
Wolff, S. R and Dean, R. T., 1987, Glucose autooxidation and protein modification, Biochem. J. 245, 243–250.
Wolff, S. P., Garner, A., and Dean, R. T., 1986, Free radicals, lipids, and protein degradation, Trends Biochem. Sci. 11, 27–31.
Youngman, L. D., Park, J.-Y. K., and Ames, B., 1992, Protein oxidation associated with aging is reduced by dietary restriction of protein calories, Proc. Natl. Acad. Sci. USA 89, 9112–9116.
Zhou, J. Q. and Gafni, A., 1991, Exposure of rat muscle phosphoglycerate kinase to a nonenzymatic MFO system generates the old form of enzyme, J. Gerontol. 46, B217 - B221.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Stadtman, E.R. (1998). The Role of Free Radical Mediation of Protein Oxidation in Aging and Disease. In: Özben, T. (eds) Free Radicals, Oxidative Stress, and Antioxidants. NATO ASI Series, vol 296. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2907-8_13
Download citation
DOI: https://doi.org/10.1007/978-1-4757-2907-8_13
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4419-3292-1
Online ISBN: 978-1-4757-2907-8
eBook Packages: Springer Book Archive