Oxidative Modification of Proteins: Age-Related ChangesChakravarti B. · Chakravarti D.N.
Keck Graduate Institute of Applied Life Sciences, Claremont, Calif., USA
Do you have an account?
- Rent for 48h to view
- Buy Cloud Access for unlimited viewing via different devices
- Synchronizing in the ReadCube Cloud
- Printing and saving restrictions apply
Rental: USD 8.50
Cloud: USD 20.00
Article / Publication Details
Aging is a complex biological phenomenon which involves progressive loss of different physiological functions of various tissues of living organisms. It is the inevitable fate of life and is a major risk factor for death and different pathological disorders. Based on a wide variety of studies performed in humans as well as in various animal models and microbial systems, reactive oxygen species (ROS) are believed to play a key role in the aging process. The production of ROS is influenced by cellular metabolic activities as well as environmental factors. ROS can react with all major biological macromolecules such as carbohydrates, nucleic acids, lipids, and proteins. Since, in general, proteins are the key molecules that play the ultimate role in various structural and functional aspects of living organisms, this review will focus on the age-related oxidative modifications of proteins as well as on mechanism for removal or repair of the oxidized proteins. The topics covered include protein oxidation as a marker of oxidative stress, experimental evidence indicating the role of ROS in protein oxidation, protein carbonyl content, enzymatic degradation of oxidized proteins, and effects of caloric restriction on protein oxidation in the context of aging. Finally, we will discuss different strategies which have been or can be undertaken to slow down the oxidative damage of proteins and the aging process.
© 2007 S. Karger AG, Basel
- Pacifici RE, Davies KJ: Protein, lipid and DNA repair systems in oxidative stress: the free-radical theory of aging revisited. Gerontology 1991;37:166–180.
- Davies KJ: Oxidative stress: the paradox of aerobic life. Biochem Soc Symp 1995;61:1–31.
- Stohs SJ: The role of free radical in toxicity and disease. J Basic Clin Physiol Pharmacol 1995;6:205–228.
- Mezzetti A, Lapenna D, Romano F, Costantini F, Pierdomenico SD, De Cesare D, Cuccurullo F, Riario-Sforza G, Zuliani G, Fellin R: Systemic oxidative stress and its relationship with age and illness. Associazione Medica ‘Sabin’. J Am Geriatr Soc 1996;44:873–875.
- Agarwal S, Sohal RS: Relationship between aging and susceptibility to protein oxidative damage. Biochem Biophys Res Commun 1993;194:1203–1206.
- Sohal RS, Agarwal S, Sohal BH: Oxidative stress and aging in the Mongolian gerbil (Meriones unguiculatus). Mech Ageing Dev 1995;81:15–25.
Harman D: Aging: a theory based on free radical and radiation chemistry. J Gerontol 1956;2:289–300.
- Friguet B, Szweda LI, Stadtman ER: 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 1994;311:168–173.
- Friguet B, Szweda LI: Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett 1997;405:21–25.
- Mattson MP: Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity. Trends Neurosci 1998;21:53–57.
- Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER: Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci USA 2001;98:12920–12925.
- Levine RL, Mosoni L, Berlett BS, Stadtman ER: Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci U S A 1996;93:15036–15040.
- Levine RL, Berlett BS, Moskovitz J, Mosoni L, Stadtman ER: Methionine residues may protect proteins from critical oxidative damage. Mech Ageing Dev 1999;107:323–332.
- Arnér ES, Holmgren A: Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 2000;267:6102–6109.
- Laboissiere MC, Sturley SL, Raines RT: The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 1995;270:28006–28009.
- Stadtman ER: Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic Biol Med 1990;9:315–325.
- Fucci L, Oliver CN, Coon MJ, Stadtman ER: Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing. Proc Natl Acad Sci USA 1983;80:1521–1525.
- Agbas A, Zaidi A, Michaelis EK: Decreased activity and increased aggregation of brain calcineurin during aging. Brain Res 2005;1059:59–71.
- Oliver CN, Levine RL, Stadtman ER: A role of mixed-function oxidation reactions in the accumulation of altered enzyme forms during aging. J Am Geriatr Soc 1987;35:947–956.
- Oliver CN, Ahn BW, Moerman EJ, Goldstein S, Stadtman ER: Age-related changes in oxidized proteins. J Biol Chem 1987;262:5488–5491.
- Carney JM, Starke-Reed PE, Oliver CN, Landum RW, Cheng MS, Wu JF, Floyd RA: Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-alpha-phenylnitrone. Proc Natl Acad Sci USA 1991;88:3633–3636.
- Yan L, Levine RL, Sohal RS: Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl Acad Sci USA 1997;94:11168–11172.
- Yarian CS, Sohal RS: In the aging housefly aconitase is the only citric acid cycle enzyme to decline significantly. J Bioenerg Biomembr 2005;37:91–96.
- Yan LJ, Sohal RS: Mitochondrial adenine nucleotide translocase is modified oxidatively during aging. Proc Natl Acad Sci USA 1998;95:12896–12901.
- Cabiscol E, Levine RL: Carbonic anhydrase III. Oxidative modification in vivo and loss of phosphatase activity during aging. J Biol Chem 1995;270:14742–14747.
- Shacter E: Quantification and significance of protein oxidation in biological samples. Drug Metab Rev 2000;32:307–326.
- Morrow JD, Chen Y, Brame CJ, Yang J, Sanchez SC, Xu J, Zackert WE, Awad JA, Roberts LJ: The isoprostanes: unique prostaglandin-like products of free-radical-initiated lipid peroxidation. Drug Metab Rev 1999:31:117–139.
- Shigenaga MK, Aboujaoude EN, Chen Q, Ames BN: Assays of oxidative DNA damage biomarkers 8-oxo-2′-deoxyguanosine and 8-oxoguanine in nuclear DNA and biological fluids by high-performance liquid chromatography with electrochemical detection. Methods Enzymol 1994;234:16–33.
- Yarian CS, Rebrin I, Sohal RS: Aconitase and ATP synthase are targets of malondialdehyde modification and undergo an age-related decrease in activity in mouse heart mitochondria. Biochem Biophys Res Commun 2005;330:151–156.
- Levine RL, Stadtman ER: Oxidative modification of proteins during aging. Exp Gerontol 2001;36:1495–1502.
- Stadtman ER, Levine RL: Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 2003;25:207–218.
- Stadtman ER, Moskovitz J, Levine RL: Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 2003;5:577–582.
- Stadtman ER: Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 2001;928:22–38.
- Gitlin G, Tsarbopoulos A, Patel ST, Sydor W, Pramanik BN, Jacobs S, Westreich L, Mittelman S, Bausch JN: Isolation and characterization of a monomethioninesulfoxide variant of interferon alpha-2b. Pharm Res 1996;13:762–769.
- Smeal T, Guarente L: Mechanisms of cellular senescence. Curr Opin Genet Dev 1997;7:281–287.
- Ottinger MA, Mobarak M, Abdelnabi M, Roth G, Proudman J, Ingram DK: Effects of calorie restriction on reproductive and adrenal systems in Japanese quail: are responses similar to mammals, particularly primates? Mech Ageing Dev 2005;126:967–975.
- Koubova J, Guarente L: How does calorie restriction work? Genes Dev 2003;17:313–321.
- Yu BP: Why calorie restriction would work for human longevity. Biogerontology 2006; 7:179–182.
- Sohal RS, Weindruch R: Oxidative stress, caloric restriction, and aging. Science 1996;273:59–63.
- Chakravarti B, Abraham GN: Effect of age and oxidative stress on tyrosine phosphorylation of ZAP-70. Mech Ageing Dev 2002;123:297–311.
- Starke-Reed PE, Oliver CN: Protein oxidation and proteolysis during aging and oxidative stress. Arch Biochem Biophys 1989;275:559–567.
- Starke PE, Oliver CN, Stadtman ER: Modification of hepatic proteins in rats exposed to high oxygen concentration. FASEB J 1987;1:36–39.
- Sohal RS: Role of oxidative stress and protein oxidation in the aging process. Free Radic Biol Med 2002;33:37–44.
- Floyd RA, Hensley K: Nitrone inhibition of age-associated oxidative damage. Ann N Y Acad Sci 2000;899:222–237.
- Garland D: Role of site-specific, metal-catalyzed oxidation in lens aging and cataract: a hypothesis. Exp Eye Res 1990;50:677–682.
- Smith CD, Carney JM, Starke-Reed PE, Oliver CN, Stadtman ER, Floyd RA, Markesbery WR: Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci USA 1991;88:10540–10543.
- Sohal RS, Sohal BH, Orr WC: Mitochondrial superoxide and hydrogen peroxide generation, protein oxidative damage, and longevity in different species of flies. Free Radic Biol Med 1995;19:499–504.
- Shringarpure R, Davies KJ: Protein turnover by the proteasome in aging and disease. Free Radic Biol Med 2002;32:1084–1089.
- Stadtman ER: Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 1993;62:797–821.
- Stadtman ER, Levine RL: Protein oxidation. Ann N Y Acad Sci 2000;899:191–208.
- Anderson MM, Requena JR, Crowley JR, Thorpe SR, Heinecke JW: The myeloperoxidase system of human phagocytes generates Nepsilon-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. J Clin Invest 1999;104:103–113.
- Cabiscol E, Piulats E, Echave P, Herrero E, Ros J: Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 2000;275:27393–27398.
- Poon HF, Farr SA, Thongboonkerd V, Lynn BC, Banks WA, Morley JE, Klein JB, Butterfield DA: Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: implications for aging and age-related neurodegenerative disorders. Neurochem Int 2005;46:159–168.
- Poon HF, Vaishnav RA, Getchell TV, Getchell ML, Butterfield DA: Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice. Neurobiol Aging 2006;27:1010–1019.
- Poon HF, Shepherd HM, Reed TT, Calabrese V, Giuffrida Stella AM, Pennisi G, Cai J, Pierce WM, Klein JB, Butterfield DA: Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis. Neurobiol Aging 2006;27:1020–1034.
- Sweda PA, Friguet B, Sweda LI: Proteolysis, free radicals, and aging. Free Radic Biol Med 2002;33:29–36.
- Rivett AJ: Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases. J Biol Chem 1985;260:300–305.
- Rivett AJ: Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase. J Biol Chem 1985;260:12600–12606.
- Pacifici RE, Salo DC, Davies KJ: Macroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Radic Biol Med 1989;7:521–536. Erratum in: Free Radic Biol Med 1990;8:211–212.
- Poppek D, Grune T: Proteasomal defense of oxidative protein modifications. Antioxid Redox Signal 2006;8:173–184.
- Grune T, Reinheckel T, Davies KJ: Degradation of oxidized proteins in mammalian cells. FASEB J 1997;11:526–534.
- Shringarpure R, Grune T, Mehlhase J, Davies KJ: Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 2003;278:311–318.
- Rivett AJ, Hearn AR: Proteasome function in antigen presentation: immunoproteasome complexes, peptide production, and interactions with viral proteins. Curr Protein Pept Sci 2004;5:153–161.
- Keller JN, Gee J, Ding Q: The proteasome in brain aging. Ageing Res Rev 2002;1:279–293.
- Coux O, Tanaka K, Goldberg AL: Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996;65:801–847.
- Rivett AJ: Intracellular distribution of proteasomes. Curr Opin Immunol 1998;10:110–114.
- Davies KJ: Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001;83:301–310.
- Grune T, Jung T, Merker K, Davies KJ: Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and ‘aggresomes’ during oxidative stress, aging, and disease. Int J Biochem Cell Biol 2004;36:2519–2530.
- Yin D: Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores. Free Radic Biol Med 1996;21:871–888.
Brunk UT, Terman A: The mitochondrial-lysosomal axis theory of cellular aging; in Cadenas E, Packer L (eds): Understanding the Process of Aging. New York, Marcel Dekker, 1998, pp 229–250.
- Friguet B: Protein repair and degradation during aging. Sci World J 2002;2:248–254.
- Farout L, Friguet B: Proteasome function in aging and oxidative stress: implications in protein maintenance failure. Antioxid Redox Signal 2006;8:205–216.
- Sitte N, Huber M, Grune T, Ladhoff A, Doecke WD, Von Zglinicki T, Davies KJ: Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts. FASEB J 2000;14:1490–1498.
- Sitte N, Merker K, Von Zglinicki T, Grune T, Davies KJ: Protein oxidation and degradation during cellular senescence of human BJ fibroblasts. I. Effects of proliferative senescence. FASEB J 2000;14:2495–2502.
- Sitte N, Merker K, Von Zglinicki T, Davies KJ, Grune T: Protein oxidation and degradation during cellular senescence of human BJ fibroblasts. II. Aging of nondividing cells. FASEB J 2000;14:2503–2510.
- Grune T, Merker K, Jung T, Sitte N, Davies KJ: Protein oxidation and degradation during postmitotic senescence. Free Radic Biol Med 2005;39:1208–1215.
Merker K, Ullrich O, Schmidt H, Sitte N, Grune T: Stability of the nuclear protein turnover during cellular senescence of human fibroblasts. FASEB J 2003;13:1963–1965.
- Louie JL, Kapphahn RJ, Ferrington DA: Proteasome function and protein oxidation in the aged retina. Exp Eye Res 2002;75:271–284.
- Ferrington DA, Husom AD, Thompson LV: Altered proteasome structure, function, and oxidation in aged muscle. FASEB J 2005;19:644–646.
- Abd El Mohsen MM, Iravani MM, Spencer JP, Rose S, Fahim AT, Motawi TM, Ismail NA, Jenner P: Age-associated changes in protein oxidation and proteasome activities in rat brain: modulation by antioxidants. Biochem Biophys Res Commun 2005;336:386–391.
- Zeng BY, Medhurst AD, Jackson M, Rose S, Jenner P: Proteasomal activity in brain differs between species and brain regions and changes with age. Mech Ageing Dev 2005;126:760–766.
- Viteri G, Carrard G, Birlouez-Aragon I, Silva E, Friguet B: Age-dependent protein modifications and declining proteasome activity in the human lens. Arch Biochem Biophys 2004;427:197–203.
- Chen Q, Thorpe J, Ding Q, El-Amouri IS, Keller JN: Proteasome synthesis and assembly are required for survival during stationary phase. Free Radic Biol Med 2004;37:859–868.
- Yu BP: How diet influences the aging process of the rat. Proc Soc Exp Biol Med 1994;205:97–105.
- Yu BP: Cellular defenses against damage from reactive oxygen species. Physiol Rev 1994;74:139–162.
- Chu YF, Sun J, Wu X, Liu RH: Antioxidant and antiproliferative activities of common vegetables. J Agric Food Chem 2002;50:6910–6916.
- Plumb GW, Lambert N, Chambers SJ, Wanigatunga S, Heaney RK, Plumb JA, Aruoma OI, Halliwell B, Miller NJ, Williamson G: Are whole extracts and purified glucosinolates from cruciferous vegetables antioxidants? Free Radic Res 1996;25:75–86.
- McCay C, Crowell M, Maynard L: The effect of retarded growth upon the length of life and upon ultimate size. J Nutr 1935;10:63–79.
- Lane MA, de Cabo R, Mattison J, Anson RM, Roth GS, Ingram DK: The Roy Walford legacy: diet restriction from molecules to mice to monkeys to man and onto mimetics. Exp Gerontol 2004;39:897–902.
- Dubey A, Forster MJ, Lal H, Sohal RS: Effect of age and caloric intake on protein oxidation in different brain regions and on behavioral functions of the mouse. Arch Biochem Biophys 1996;333:189–197.
- Sohal RS, Agarwal S, Candas M, Forster MJ, Lal H: Effect of age and caloric restriction on DNA oxidative damage in different tissues of C57BL/6 mice. Mech Ageing Dev 1994;76:215–224.
Matsuo M, Gomi F, Kuramoto K, Sagai M: Food restriction suppresses an age-dependent increase in the exhalation rate of pentane from rats: a longitudinal study. J Gerontol 1993;48:B133–B136.
- Aksenova MV, Aksenov MY, Carney JM, Butterfield DA: Protein oxidation and enzyme activity decline in old brown Norway rats are reduced by dietary restriction. Mech Ageing Dev 1998;100:157–168.
- Merker K, Stolzing A, Grune T: Proteolysis, caloric restriction and aging. Mech Ageing Dev 2001;122:595–615.
- Lopez-Lluch G, Hunt N, Jones B, Zhu M, Jamieson H, Hilmer S, Cascajo MV, Allard J, Ingram DK, Navas P, de Cabo R: Calorie restriction induces mitochondrial biogenesis and bioenergetic efficiency. Proc Natl Acad Sci USA 2006;103:1768–1773.
- Ingram DK, Anson RM, de Cabo R, Mamczarz J, Zhu M, Mattison J, Lane MA, Roth GS: Development of calorie restriction mimetics as a prolongevity strategy. Ann N Y Acad Sci 2004;1019:412–423.
- Cho CG, Kim HJ, Chung SW, Jung KJ, Shim KH, Yu BP, Yodoi J, Chung HY: Modulation of glutathione and thioredoxin systems by calorie restriction during the aging process. Exp Gerontol 2003;38:539–548.
Judge S, Judge A, Grune T, Leeuwenburgh C: Short-term CR decreases cardiac mitochondrial oxidant production but increases carbonyl content. Am J Physiol Regul Integr Comp Physiol 2004;286:R254–R259.
- Scrofano MM, Shang F, Nowell TR, Gong X, Smith DE, Kelliher M, Dunning J, Mura CV, Taylor A: Aging, calorie restriction and ubiquitin-dependent proteolysis in the livers of Emory mice. Mech Ageing Dev 1998;101:277–296.
- Rebrin I, Kamzalov S, Sohal RS: Effects of age and caloric restriction on glutathione redox state in mice. Free Radic Biol Med 2003;35:626–635.
- Sell DR, Lane MA, Obrenovich ME, Mattison JA, Handy A, Ingram DK, Cutler RG, Roth GS, Monnier VM: The effect of caloric restriction on glycation and glycoxidation in skin collagen of nonhuman primates. J Gerontol A Biol Sci Med Sci 2003;58:508–516.
Forster MJ, Sohal BH, Sohal RS: Reversible effects of long-term caloric restriction on protein oxidative damage. J Gerontol A Biol Sci Med Sci 2000;55:B522–B529.
- Leeuwenburgh C, Wagner P, Holloszy JO, Sohal RS, Heinecke JW: Caloric restriction attenuates dityrosine cross-linking of cardiac and skeletal muscle proteins in aging mice. Arch Biochem Biophys 1997;346:74–80.
- de Cabo R, Cabello R, Rios M, Lopez-Lluch G, Ingram DK, Lane MA, Navas P: Calorie restriction attenuates age-related alterations in the plasma membrane antioxidant system in rat liver. Exp Gerontol 2004;39:297–304.
- Radak Z, Takahashi R, Kumiyama A, Nakamoto H, Ohno H, Ookawara T, Goto S: Effect of aging and late onset dietary restriction on antioxidant enzymes and proteasome activities, and protein carbonylation of rat skeletal muscle and tendon. Exp Gerontol 2002;37:1423–1430.
- Nagai M, Takahashi R, Goto S: Dietary restriction initiated late in life can reduce mitochondrial protein carbonyls in rat livers: Western blot studies. Biogerontology 2000;1:321–328.
- Kim HJ, Jung KJ, Yu BP, Cho CG, Choi JS, Chung HY: Modulation of redox-sensitive transcription factors by calorie restriction during aging. Mech Ageing Dev 2002;123:1589–1595.
- Chung HY, Sung B, Jung KJ, Zou Y, Yu BP: The molecular inflammatory process in aging. Antioxid Redox Signal 2006;8:572–581.
- Heilbronn LK, de Jonge L, Frisard MI, DeLany JP, Larson-Meyer DE, Rood J, Nguyen T, Martin CK, Volaufova J, Most MM, Greenway FL, Smith SR, Deutsch WA, Williamson DA, Ravussin E; Pennington CALERIE Team: Effect of 6-month calorie restriction on biomarkers of longevity, metabolic adaptation, and oxidative stress in overweight individuals: a randomized controlled trial. JAMA. 2006;295:1539–1548.
- Ingram DK, Roth GS, Lane MA, Ottinger MA, Zou S, de Cabo R, Mattison JA: The potential for dietary restriction to increase longevity in humans: extrapolation from monkey studies. Biogerontology 2006;7: 143–148.
- Dirks AJ, Leeuwenburgh C: Caloric restriction in humans: potential pitfalls and health concerns. Mech Ageing Dev 2006;127:1–7.
- Reverter-Branchat G, Cabiscol E, Tamarit J, Ros J: Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. J Biol Chem 2004;279:31983–31989.
- Agarwal S, Sharma S, Agrawal V, Roy N: Caloric restriction augments ROS defense in S. cerevisiae by a Sir2p independent mechanism. Free Radic Res 2005;39:55–62.
- Ingram DK, Zhu M, Mamczarz J, Zou S, Lane MA, Roth GS, de Cabo R: Calorie restriction mimetics: an emerging research field. Aging Cell 2006;5:97–108.
- Juranek I, Bezek S: Controversy of free radical hypothesis: reactive oxygen species – cause or consequence of tissue injury? Gen Physiol Biophys 2005;24:263–278.
- Rivett AJ, Roseman JE, Oliver CN, Levine RL, Stadtman ER: Covalent modification of proteins by mixed-function oxidation: recognition by intracellular proteases. Prog Clin Biol Res 1985;180:317–328.
- Davies KJ: Protein oxidation and proteolytic degradation: general aspects and relationship to cataract formation. Adv Exp Med Biol 1990;264:503–511.
- Martinez-Vicente M, Sovak G, Cuervo AM: Protein degradation and aging. Exp Gerontol 2005;40:622–633.
- Kim CH, Zou Y, Kim DH, Kim ND, Yu BP, Chung HY: Proteomic analysis of nitrated and 4-hydroxy-2-nonenal-modified serum proteins during aging. J Gerontol A Biol Sci Med Sci 2006;61:332–338.
- Rabek JP, Boylston WH, Papaconstantinou J: Carbonylation of ER chaperone proteins in aged mouse liver. Biochem Biophys Res Commun 2003;305:566–572.
- Squier TC: Oxidative stress and protein aggregation during biological aging. Exp Gerontol 2001;36:1539–1550.
- Verzijl N, DeGroot J, Oldehinkel E, Bank RA, Thorpe SR, Baynes JW, Bayliss MT, Bijlsma JW, Lafeber FP, Tekoppele JM: Age-related accumulation of Maillard reaction products in human articular cartilage collagen. Biochem J 2000;350:381–387.
- Verzijl N, DeGroot J, Thorpe SR, Bank RA, Shaw JN, Lyons TJ, Bijlsma JW, Lafeber FP, Baynes JW, Ekpwele JM: Effect of collagen turnover on the accumulation of advanced glycation end products. J Biol Chem 2000;275:39027–39031.
- Baynes JW: The role of AGEs in aging: causation or correlation. Exp Gerontol. 2001;36:1527–1537.
- Srivastava OP, Kirk MC, Srivastava K: Characterization of covalent multimers of crystallins in aging human lenses. J Biol Chem 2004;279:10901–10909.
- Viner RI, Ferrington DA, Williams TD, Bigelow DJ, Schoneich C: Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle. Biochem J 1999;340:657–669.
Sharov VS, Dremina ES, Galeva NA, Williams TD, Schoneich C: Quantitative mapping of oxidation-sensitive cysteine residues in SERCA in vivo and in vitro by HPLC-electrospray-tandem mass spectrometry: selective protein oxidation during biological aging. Biochem J 2005;394:605–615.
- Knyushko TV, Sharov VS, Williams TD, Schoneich C, Bigelow DJ: 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment. Biochemistry 2005;44:13071–13081.
Xu S, Ying J, Jiang B, Guo W, Adachi T, Sharov V, Lazar H, Menzoian J, Knyushko TV, Bigelow DJ, Schoneich C, Cohen RA: Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging. Am J Physiol Heart Circ Physiol 2006;290:H2220–H2227.
Article / Publication Details
Copyright / Drug Dosage / DisclaimerCopyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.