Journal of Diabetes and Its Complications
Volume 19, Issue 6 , Pages 328-334 , November 2005

A copper chelating agent suppresses carbonyl stress in diabetic rat lenses

  • Yoji Hamada

      Affiliations

    • Division of Metabolic Diseases, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan
    • Corresponding Author InformationCorresponding author. Fax: +52 744 2206
  • ,
  • Eitaro Nakashima

      Affiliations

    • Division of Metabolic Diseases, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan
  • ,
  • Keiko Naruse

      Affiliations

    • Division of Metabolic Diseases, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan
  • ,
  • Mika Nakae

      Affiliations

    • Division of Metabolic Diseases, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan
  • ,
  • Mitsuru Naiki

      Affiliations

    • Institute of Bio-Active Science, Nippon Zoki Pharmaceutical Company, Kinashi, Yashiro-cho, Hyogo 673-1461, Japan
  • ,
  • Hiroki Fujisawa

      Affiliations

    • Institute of Bio-Active Science, Nippon Zoki Pharmaceutical Company, Kinashi, Yashiro-cho, Hyogo 673-1461, Japan
  • ,
  • Yutaka Oiso

      Affiliations

    • Division of Metabolic Diseases, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan
  • ,
  • Nigishi Hotta

      Affiliations

    • Chubu Rosai Hospital, 1-10-6 Kohmei, Minato-ku, Nagoya 455-8530, Japan
  • ,
  • Jiro Nakamura

      Affiliations

    • Division of Metabolic Diseases, Nagoya University Graduate School of Medicine, 65 Tsuruma-cho, Showa-ku, Nagoya 466-8550, Japan

Received 15 June 2005 ,Revised 26 July 2005 ,Accepted 1 August 2005.

References 

  1. Ahmed MU, Brinkmann Frye E, Degenhardt TP, Thorpe SR, Baynes JW. N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochemical Journal. 1997;324:565–570
  2. Baynes JW, Thorpe SR. Role of oxidative stress in diabetic complications: A new perspective on an old paradigm. Diabetes. 1999;48:1–9
  3. Beisswenger PJ, Howell SK, Touchette AD, Lal S, Szwergold BS. Metformin reduces systemic methylglyoxal levels in type 2 diabetes. Diabetes. 1999;48:198–202
  4. Boomsma F, van den Meiracker AH, Winkel S, Aanstoot HJ, Batstra MR, Man in 't Veld AJ, et al. Circulating semicarbazide-sensitive amine oxidase is raised both in type I (insulin-dependent), in type II (non-insulin-dependent) diabetes mellitus and even in childhood type I diabetes at first clinical diagnosis. Diabetologia. 1999;42:233–237
  5. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Analytical Biochemistry. 1976;72:248–254
  6. Brown TR, Su B, Brown KA, Schwartz MA, Tobia AM, Kappler F. Modulation of in vivo 3-deoxyglucosone levels. Biochemical Society Transactions. 2003;31:1433–1437
  7. Callingham BA, Crosbie AE, Rous BA. Some aspects of the pathophysiology of semicarbazide-sensitive amine oxidase enzymes. Progress in Brain Research. 1995;106:305–321
  8. Cameron NE, Cotter MA. Neurovascular dysfunction in diabetic rats. Potential contribution of autoxidation and free radicals examined using transition metal chelating agents. Journal of Clinical Investigation. 1995;96:1159–1163
  9. Che W, Asahi M, Takahashi M, Kaneto H, Okado A, Higashiyama S, et al. Selective induction of heparin-binding epidermal growth factor-like growth factor by methylglyoxal and 3-deoxyglucosone in rat aortic smooth muscle cells. The involvement of reactive oxygen species formation and a possible implication for atherogenesis in diabetes. Journal of Biological Chemistry. 1997;272:18453–18459
  10. Dahlman T, Hartvig P, Lofholm M, Nordlinder H, Loof L, Westermark K. Long-term treatment of Wilson's disease with triethylene tetramine dihydrochloride (trientine). QJM. 1995;88:609–616
  11. Degenhardt TP, Thorpe SR, Baynes JW. Chemical modification of proteins by methylglyoxal. Cellular and Molecular Biology. 1998;44:1139–1145
  12. Fraga CG, Shigenaga MK, Park JW, Degan P, Ames BN. Oxidative damage to DNA during aging: 8-Hydroxy-2′-deoxyguanosine in rat organ DNA and urine. Proceedings of the National Academy of Sciences of the United States of America. 1990;87:4533–4537
  13. Fu MX, Requena JR, Jenkins AJ, Lyons TJ, Baynes JW, Thorpe SR. The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. Journal of Biological Chemistry. 1996;271:9982–9986
  14. Grandhee SK, Monnier VM. Mechanism of formation of Maillard protein cross-link pentosidine. Journal of Biological Chemistry. 1991;266:11649–11653
  15. Hamada Y, Nakamura J, Fujisawa H, Yago H, Nakashima E, Koh N, et al. Effects of glycemic control on plasma 3-deoxyglucosone levels in NIDDM patients. Diabetes Care. 1997;20:1466–1469
  16. Hamada Y, Nakamura J, Naruse K, Komori T, Kato K, Kasuya Y, et al. Epalrestat, an aldose reductase inhibitor, reduces the levels of Nepsilon-(carboxymethyl)lysine protein adducts and their precursors in erythrocytes from diabetic patients. Diabetes Care. 2000;23:1539–1544
  17. Hayase F, Nagaraj RH, Miyata S, Njoroge FG, Monnier VM. Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo. Journal of Biological Chemistry. 1989;263:3758–3764
  18. Hayase F, Shibuya T, Sato J, Yamamoto M. Effects of oxygen and transition metals on the advanced Maillard reaction of proteins with glucose. Bioscience, Biotechnology, and Biochemistry. 1996;60:1820–1825
  19. Hayes BE, Clarke DE. Semicarbazide-sensitive amine oxidase activity in streptozotocin diabetic rats. Research Communications in Chemical Pathology and Pharmacology. 1990;69:71–83
  20. Hiraku Y, Sugimoto J, Yamaguchi T, Kawanishi S. Oxidative DNA damage induced by aminoacetone, an amino acid metabolite. Archives of Biochemistry and Biophysics. 1999;365:62–70
  21. Horiuchi S, Araki N, Morino Y. Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Journal of Biological Chemistry. 1991;266:7329–7332
  22. Jakus V, Hrnciarova M, Carsky J, Krahulec B, Rietbrock N. Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity. Life Sciences. 1999;65:1991–1993
  23. Kador PF, Kinoshita JH. Role of aldose reductase in the development of diabetes-associated complications. American Journal of Medicine. 1995;79(Suppl. 5A):8–12
  24. Kantha SS, Wada S, Tanaka H, Takeuchi M, Watabe S, Ochi H. Carnosine sustains the retention of cell morphology in continuous fibroblast culture subjected to nutritional insult. Biochemical and Biophysical Research Communications. 1996;223:278–282
  25. Kato H, van Chuyen N, Shinoda T, Sekiya F, Hayase F. Metabolism of 3-deoxyglucosone, an intermediate compound in the Maillard reaction, administered orally or intravenously to rats. Biochimica et Biophysica Acta. 1990;1035:71–76
  26. Lal S, Szwergold BS, Kappler F, Brown T. Detection of fructose-3-phosphokinase activity in intact mammalian lenses by 31P NMR spectroscopy. Journal of Biological Chemistry. 1993;268:7763–7767
  27. Lal S, Szwergold BS, Taylor AH, Randall WC, Kappler F, Wells-Knecht K, et al. Metabolism of fructose-3-phosphate in the diabetic rat lens. Archives of Biochemistry and Biophysics. 1995;318:191–199
  28. Lebel CP, Ischiropoulos H, Bondy SC. Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress. Chemical Research in Toxicology. 1992;5:227–231
  29. Lyons TJ, Silvestri G, Dunn JA, Dyer DG, Baynes JW. Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes. 1991;40:1010–1015
  30. Mathys KC, Ponnampalam SN, Padival S, Nagaraj RH. Simicarbazide-sensitive amine oxidase in aortic smooth muscle cells mediates synthesis of a methyglyoxal-AGE: Implications for vascular complications in diabetes. Biochemical and Biophysical Research Communications. 2002;297:863–869
  31. McCance DR, Dyer DG, Dunn JA, Bailie KE, Thorpe SR, Baynes JW, et al. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. Journal of Clinical Investigation. 1993;91:2470–2478
  32. Miwa I, Kanbara M, Wakazono H, Okuda J. Analysis of sorbitol, galactitol, and myo-inositol in lens and sciatic nerve by high-performance liquid chromatography. Analytical Biochemistry. 1988;173:39–44
  33. Mullokandov EA, Franklin WA, Brownlee M. DNA damage by the glycation products of glyceraldehyde 3-phosphate and lysine. Diabetologia. 1994;37:145–149
  34. Murata-Kamiya N, Kamiya H. Methylglyoxal, an endogenous aldehyde, crosslinks DNA polymerase and the substrate DNA. Nucleic Acids Research. 2001;29:3433–3438
  35. Nakamura J, Hamada Y, Chaya S, Nakashima E, Naruse K, Kato K, et al. Transition metals and polyol pathway in the development of diabetic neuropathy in rats. Diabetes/Metabolism Research and Reviews. 2002;18:395–402
  36. Nishikawa T, Edelstein D, Du XL, Yamagishi S, Matsumura T, Kaneda Y, et al. Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature. 2000;404:787–790
  37. Phillips SA, Thornalley PJ. The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal. European Journal of Biochemistry. 1993;212:101–105
  38. Sady C, Jiang CL, Chellan P, Madhun Z, Duve Y, Glomb MA, et al. Maillard reactions by alpha-oxoaldehydes: Detection of glyoxal-modified proteins. Biochimica et Biophysica Acta. 2000;1481:255–264
  39. Shamsi FA, Lin K, Sady C, Nagaraj RH. Methylglyoxal-derived modifications in lens aging and cataract formation. Investigative Ophthalmology & Visual Science. 1998;39:2355–2364
  40. Shimoi K, Okitsu A, Green MH, Lowe JE, Ohta T, Kaji K, et al. Oxidative DNA damage induced by high glucose and its suppression in human umbilical vein endothelial cells. Mutation Research. 2001;480–481:371–378
  41. Shipanova IN, Glomb MA, Nagaraj RH. Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct. Archives of Biochemistry and Biophysics. 1997;344:29–36
  42. Stevens A. The effectiveness of putative anti-cataract agents in the prevention of protein glycation. Journal of the American Optometric Association. 1995;66:744–749
  43. Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochemical Journal. 1999;344:109–116
  44. Van den Enden MK, Nyengaard JR, Ostrow E, Burgan JH, Williamson JR. Elevated glucose levels increase retinal glycolysis and sorbitol pathway metabolism. Implications for diabetic retinopathy. Investigative Ophthalmology & Visual Science. 1995;36:1675–1685
  45. Yamada H, Miyata S, Igaki N, Yatabe H, Miyauchi Y, Ohara T, et al. Increase in 3-deoxyglucosone levels in diabetic rat plasma. Specific in vivo determination of intermediate in advanced Maillard reaction. Journal of Biological Chemistry. 1994;269:20275–20280
  46. Zarina S, Zhao HR, Abraham EC. Advanced glycation end products in human senile and diabetic cataractous lenses. Molecular and Cellular Biochemistry. 2000;210:29–34
  47. Zyzak DV, Richardson JM, Thorpe SR, Baynes JW. Formation of reactive intermediates from Amadori compounds under physiological conditions. Archives of Biochemistry and Biophysics. 1995;316:547–554

PII: S1056-8727(05)00099-1

doi: 10.1016/j.jdiacomp.2005.08.002

Journal of Diabetes and Its Complications
Volume 19, Issue 6 , Pages 328-334 , November 2005