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Original Article

In Vitro Nonenzymatic Glycation Enhances the Role of Myoglobin as a Source of Oxidative Stress

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Pages 139-146 | Received 18 Aug 2003, Published online: 07 Jul 2009

References

  • Schleicher, ED., Olgemoller, B., Wiedenmann, E. and Gerbitz, K.D. (1993) "Specific glycation of albumin depends on its half-life", Clin. Chem. 39, 625–628.
  • Biemel, K.M., Friecll, D.A. and Lederer, M.O. (2002) "Identifica-tion and quantification of major maillard-crosslinks in human serum albumin and lens protein: evidence for glucosepane as the dominant compound", J. Biol. Chem. 277, 24907–24915.
  • Turk, Z., Misur, I., Turk, N. and Benko, B. (1999) "Rat tissue collagen modified by advanced glycation: correlation with duration of diabetes and glycemic control", Clin. Chem. Lab. Med. 37, 813–820.
  • Stewart, J.M., Kilpatric, ES., Cathcart, S., Small, M. and Dominiczac, M.H. (1994) "Low-density lipoprotein particle size in type 2 diabetic patients and age matched controls", Ann. Clin. Biochem. 31, 153–159.
  • De Rosa, MC., Sanna, M.T., Messana, I., Castagnola, M., Galtieri, A., Tellone, E., Scatena, R., Bolta, B., Bolta, M. and Giardina, B. (1998) "Glycated human hemoglobin (HbAic): functional characteristics and molecular modeling studies", Biophys. Chem. 72, 323–335.
  • Cohen, M.P. and Wu, V. (1994) "Purification of glycated hemoglobin", Methods Enzymol. 231, 65–75.
  • Giardino, I., Edelstein, D. and Brownlee, M. (1994) "Non-enzymatic glycosylation in vitro in bovine endothelial cells alters basic fibroblast growth factor", J. Clin. Investig. 94, 110–117.
  • Wolffenbuttel, B.H., Giordano, D., Founds, H.W. and Bucala, R. (1996) "Long-term assessment of glucose control by hemoglobin-AGE measurement", Lancet 347, 513–515.
  • Svacina, S., Hovorka, R. and Skrha, J. (1990) "Computer models of albumin and hemoglobin glycation", Comput. Methods Programs Biomed. 32, 259–263.
  • Watala, C., Gwozdzinski, K. and Malek, M. (1992) "Direct evidence for the alterations in protein structure and conformation upon in vitro nonenzymatic glycosylation", Int. J. Biochem. 24, 1295–1302.
  • Khoo, U.Y., Newman, D.J., Miller, W.K. and Price, C.P. (1994) "The influence of glycation on the peroxidase activity of hemoglobin", Fur. J. Clin. Chem. Clin. Biochem. 32, 435–440.
  • Peterson, K.P., Pavlovich, J.G., Goldstein, D., Little, R., England, J. and Peterson, C.M. (1998) "What is hemoglobin Air? An analysis of glycated hemoglobins by electrospray ionization mass spectrometry", Clin. Chem. 44, 1951–1958.
  • Inouye, M., Mio, T. and Sumino, K. (1999) "Glycated hemoglobin and lipid peroxidation in erythrocytes of diabetic patients", Metabolism 48, 205–209.
  • Kar, M. and Chakraborti, A.S. (1999) "Release of iron from hemoglobin — a possible source of free radicals in diabetes mellitus", Ind. J. Exp. Biol. 37, 190–192.
  • Kar, M. and Chakraborti, A.S. (2001) "Effect of glycosylation on iron-mediated free radical reactions of haemoglobin", Curr. Sci. 80, 770–773.
  • Panter, S.S. (1994) "Release of iron from hemoglobin", Methods Enzymol. 231, 502–514.
  • Gutteridge, J.M.C. (1986) "Iron promoters of the Fenton reaction and lipid peroxidation can be released from hemoglobin by peroxides", FEBS Lett. 201, 291–295.
  • Halliwell, B. and Gutteridge, J.M.C. (1990) "Role of free radicals and catalytic metal ions in human disease", Methods Enzymol. 186, 1–88.
  • Stryer, L. (1995) Biochemistry, 4th ed. (W.H. Freeman, New York), pp 147–178.
  • Halliwell, B. and Gutteridge, J.M.C. (2000) Free Radicals in Biology and Medicine (Oxford University Press, New York), pp 105–245.
  • Cooper, C.E., Vollard, N.B., Choueiri, T. and Wilson, M.T. (2002) "Exercise, free radicals and oxidative stress", Biochem. Soc. Trans. 30, 280–285.
  • Abassi, Z.A., Hoffman, A. and Better, OS. (1998) "Acute renal failure complicating muscle crush injury", Semin. Nephrol. 18, 558–565.
  • Tanabashi, S., Okuno, F., Terakura, T., Tsuji, T., Wakahara, T. and Yamada, S. (1982) "A case of diabetic ketoacidosis with a markedly raised level of serum creatin phosphokinase (CPK) and myoglobin", Nippon Naika Gakki Zasshi. 71, 802–809.
  • Nakano, S., Mugikura, M., Endoh, M., Ogami, Y. and lsuki, M. (1996) "Acute pancreatitis with diabetic ketoacidosis associa-ted with hypermyogloinemia, acute renal failure and DIC", J. Gastroenterol. 31, 623–626.
  • Rumpf, K.W., Kaiser, H., Grone, H.J., Trapp, V.E., Meinck H.M., Goebel, H.H., Kunze, E., Kreuzer, H. and Schler, F. (1981) "Myoglobinuric renal failure in hyperosmolar diabetic coma", Dtsch. Med. Wochenschr. 106, 708–711.
  • Wittenberg, J.B. and Witenberg, B.A. (1981) "Preparation of myoglobin", Methods Enzymol. 76, 29–42.
  • Trinder, P. (1969) "Determination of blood glucose using an oxidase-peroxidase system with a noncarcinogenic chromo-gen", J. Clin. Pat hol. 22, 158–161.
  • Dixon, H.B. and McIntosh, R. (1967) "Reduction of methemoglobin in hemoglobin samples using gel filtration for continuous removal of reaction products", Nature 213, 399–400.
  • Flukinger, R. and Winterhalter, K.H. (1976) "In vitro synthesis of hemoglobin Air", FEBS Lett. 71, 356–360.
  • Sadrzadeh, S.M., Graf, E., Panter, S.S., Hallaway, P.E. and Eaton, J.W. (1984) "Hemoglobin. A biologic Fenton reagents", J. Biol. Chem. 259, 14354–14356.
  • Dixon, W.J., Hayes, J.J., Levin, J.R., Weidner, ME, Dombroski, B.A. and Tullius, T.D. (1991) "Hydroxyl radical footprinting", Methods Enzymol. 208, 380–413.
  • Levine, R.L., Garland, D., Oliver, C.N., Amici, A., Climent, I., Lenz, A., Ahn, B., Shaltiel, S. and Stadtman, KR. (1990) "Determination of carbonyl content in oxidatively modified proteins", Methods Enzymol. 186, 464–478.
  • Winterbourn, C.C. (1990) "Oxidative reactions of hemo-globin", Methods Enzymol. 186, 222–265.
  • Everse, J., Johnson, M.C. and Marini, M.A. (1994) "Peroxi-dative activities of hemoglobin and hemoglobin derivatives", Methods Enzymol. 231, 547–561.
  • Giulivi, C. and Cadenas, E. (1994) "Ferrylmyoglobin: formation and chemical reactivity toward electron-donating compounds", Methods Enzymol. 233, 189–202.
  • Egawa, T., Shimada, H. and Ishimura, Y. (2000) "Formation of compound I in the reaction of native myoglobins with hydrogen peroxide", J. Biol. Chem. 275, 34858–34866.
  • Catalano, CE., Choe, YS. and Ortiz de Montellano, P.R. (1989) "Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link", J. Biol. Chem. 264, 10534–10541.
  • Reeder, B.J., Svistunenko, D.A., Sharpe, MA. and Wilson, M.T. (2002) "Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking to myo-globin", Biochemistry 41, 367–375.
  • Puppo, A. and Halliwell, B. (1988) "Formation of hydroxyl radicals in biological systems. Does myoglobin stimulate hydroxyl radical formation from hydrogen peroxide?", Free Radic. Res. Commun. 4, 415–422.
  • Rice-Evans, C., Okunada, G. and Khan, R. (1989) "The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine", Free Radic. Res. Commun. 7, 45–54.
  • Takasu, N., Komonga, I., Asawa, T. and Nagasawa, Y. (1991) "Streptozotocin and alloxan-induced H202 generation and DNA fragmentation in pancreatic islets, H202 as mediator for DNA fragmentation", Diabetes 40, 1141–1145.
  • Maiorino, M., Ursini, F. and Cadenas, E. (1994) "Reactivity of metmyoglobin towards phospholipid hydroperoxides", Free Radic. Biol. Med. 16, 661–667.
  • Kelman, D.J., Degray, J.A. and Mason, R.P. (1994) "Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical, which oxidizes substrates", J. Biol. Chem. 269, 7458–7463.
  • Cadenas, E. (1989) "Lipid peroxidation during the oxidation of haemoprotein by hydropermddes. Relation to electroni-cally excited state formation", J. Biolumin. Chemilumin. 4, 208–218.
  • Teebor, G.W., Boorstein, R.J. and Cadet, J. (1988) "The repairability of oxidative free radical-mediate damage to DNA: a review", Int. J. Radiat. Biol. 54, 131–150.
  • Wagner, J.R., van Lier, J.E., Decarroz, C., Berger, M. and Cadet, J. (1990) "Photodynamic methods for oxy radical-induced DNA damage", Methods Enzymol. 186, 502–511.
  • Halliwell, B. and Aruoma, 0.1. (1991) "DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems", FEBS Lett. 281, 9–19.
  • Stadtman, ER. (1989) In: Hayaishi, 0., Niki, E., Kondo, M. and Yoshikawa, T., eds, Medical, Biochemical and Chemical Aspects of Free Radicals (Elsevier, Amsterdam), p 11.
  • Davies, K.J. (1986) "Intracellular proteolytic systems may function as secondary antioxidant defenses: an hypothesis", J. Free Radic. Biol. Med. 2, 155–173.
  • Oliver, C.N., Levine, R.L. and Stadtman, E.R. (1987) "A role of mixed-function oxidation reactions in the accumulation of altered enzyme forms during aging", J. Am. Geriatr. Soc. 35, 947–956.
  • Tajima, G. and Shikama, K. (1987) "Autooxidation of myoglobin. An overall stoichiometry including subsequent side reactions", J. Biol. Chem. 262, 12603–12606.
  • Grisham, M.B. and Everse, J. (1991) In: Everse, J., Everse, K.E. and Grisham, M.B., eds, Peroxidase in Chemistry and Biology (CRC Press, Boca Raton, MB) Vol. 1, pp 335–344.

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