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Volumn 19, Issue 6, 2005, Pages 328-334

A copper chelating agent suppresses carbonyl stress in diabetic rat lenses

Author keywords

3 Deoxyglucosone; Carbonyl stress; Copper chelating agents; Lens; Methylglyoxal; Oxidative stress; Semicarbazide sensitive amine oxidase; Trientine

Indexed keywords

3 DEOXYGLUCOSONE; 8 HYDROXYDEOXYGUANOSINE; ADVANCED GLYCATION END PRODUCT; AMINE OXIDASE (COPPER CONTAINING); CHELATING AGENT; METHYLGLYOXAL; POLYOL; PYRIMIDINE DERIVATIVE; STREPTOZOCIN; TRIENTINE;

EID: 27644495699     PISSN: 10568727     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jdiacomp.2005.08.002     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 0030919275 scopus 로고    scopus 로고
    • N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins
    • M.U. Ahmed, E. Brinkmann Frye, T.P. Degenhardt, S.R. Thorpe, and J.W. Baynes N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins Biochemical Journal 324 1997 565 570
    • (1997) Biochemical Journal , vol.324 , pp. 565-570
    • Ahmed, M.U.1    Brinkmann Frye, E.2    Degenhardt, T.P.3    Thorpe, S.R.4    Baynes, J.W.5
  • 2
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications: A new perspective on an old paradigm
    • J.W. Baynes, and S.R. Thorpe Role of oxidative stress in diabetic complications: A new perspective on an old paradigm Diabetes 48 1999 1 9
    • (1999) Diabetes , vol.48 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 4
    • 0000687067 scopus 로고    scopus 로고
    • 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
    • F. Boomsma, A.H. van den Meiracker, S. Winkel, H.J. Aanstoot, M.R. Batstra, A.J. Man in 't Veld, and G.J. Bruining 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 42 1999 233 237
    • (1999) Diabetologia , vol.42 , pp. 233-237
    • Boomsma, F.1    Van Den Meiracker, A.H.2    Winkel, S.3    Aanstoot, H.J.4    Batstra, M.R.5    Man In 'T Veld, A.J.6    Bruining, G.J.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Analytical Biochemistry 72 1976 248 254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0029562807 scopus 로고
    • Some aspects of the pathophysiology of semicarbazide-sensitive amine oxidase enzymes
    • B.A. Callingham, A.E. Crosbie, and B.A. Rous Some aspects of the pathophysiology of semicarbazide-sensitive amine oxidase enzymes Progress in Brain Research 106 1995 305 321
    • (1995) Progress in Brain Research , vol.106 , pp. 305-321
    • Callingham, B.A.1    Crosbie, A.E.2    Rous, B.A.3
  • 8
    • 0029082815 scopus 로고
    • Neurovascular dysfunction in diabetic rats. Potential contribution of autoxidation and free radicals examined using transition metal chelating agents
    • N.E. Cameron, and M.A. Cotter Neurovascular dysfunction in diabetic rats. Potential contribution of autoxidation and free radicals examined using transition metal chelating agents Journal of Clinical Investigation 96 1995 1159 1163
    • (1995) Journal of Clinical Investigation , vol.96 , pp. 1159-1163
    • Cameron, N.E.1    Cotter, M.A.2
  • 9
    • 0030835896 scopus 로고    scopus 로고
    • 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
    • W. Che, M. Asahi, M. Takahashi, H. Kaneto, A. Okado, S. Higashiyama, and N. Taniguchi 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 272 1997 18453 18459
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 18453-18459
    • Che, W.1    Asahi, M.2    Takahashi, M.3    Kaneto, H.4    Okado, A.5    Higashiyama, S.6    Taniguchi, N.7
  • 10
    • 0029162533 scopus 로고
    • Long-term treatment of Wilson's disease with triethylene tetramine dihydrochloride (trientine)
    • T. Dahlman, P. Hartvig, M. Lofholm, H. Nordlinder, L. Loof, and K. Westermark Long-term treatment of Wilson's disease with triethylene tetramine dihydrochloride (trientine) QJM 88 1995 609 616
    • (1995) QJM , vol.88 , pp. 609-616
    • Dahlman, T.1    Hartvig, P.2    Lofholm, M.3    Nordlinder, H.4    Loof, L.5    Westermark, K.6
  • 13
    • 0029923574 scopus 로고    scopus 로고
    • The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions
    • M.X. Fu, J.R. Requena, A.J. Jenkins, T.J. Lyons, J.W. Baynes, and S.R. Thorpe The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions Journal of Biological Chemistry 271 1996 9982 9986
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 9982-9986
    • Fu, M.X.1    Requena, J.R.2    Jenkins, A.J.3    Lyons, T.J.4    Baynes, J.W.5    Thorpe, S.R.6
  • 14
    • 0025948114 scopus 로고
    • Mechanism of formation of Maillard protein cross-link pentosidine
    • S.K. Grandhee, and V.M. Monnier Mechanism of formation of Maillard protein cross-link pentosidine Journal of Biological Chemistry 266 1991 11649 11653
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 11649-11653
    • Grandhee, S.K.1    Monnier, V.M.2
  • 16
    • 0033803537 scopus 로고    scopus 로고
    • Epalrestat, an aldose reductase inhibitor, reduces the levels of Nepsilon-(carboxymethyl)lysine protein adducts and their precursors in erythrocytes from diabetic patients
    • Y. Hamada, J. Nakamura, K. Naruse, T. Komori, K. Kato, Y. Kasuya, R. Nagai, S. Horiuchi, and N. Hotta Epalrestat, an aldose reductase inhibitor, reduces the levels of Nepsilon-(carboxymethyl)lysine protein adducts and their precursors in erythrocytes from diabetic patients Diabetes Care 23 2000 1539 1544
    • (2000) Diabetes Care , vol.23 , pp. 1539-1544
    • Hamada, Y.1    Nakamura, J.2    Naruse, K.3    Komori, T.4    Kato, K.5    Kasuya, Y.6    Nagai, R.7    Horiuchi, S.8    Hotta, N.9
  • 17
    • 0024511940 scopus 로고
    • Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo
    • F. Hayase, R.H. Nagaraj, S. Miyata, F.G. Njoroge, and V.M. Monnier Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo Journal of Biological Chemistry 263 1989 3758 3764
    • (1989) Journal of Biological Chemistry , vol.263 , pp. 3758-3764
    • Hayase, F.1    Nagaraj, R.H.2    Miyata, S.3    Njoroge, F.G.4    Monnier, V.M.5
  • 18
    • 0030280345 scopus 로고    scopus 로고
    • Effects of oxygen and transition metals on the advanced Maillard reaction of proteins with glucose
    • F. Hayase, T. Shibuya, J. Sato, and M. Yamamoto Effects of oxygen and transition metals on the advanced Maillard reaction of proteins with glucose Bioscience, Biotechnology, and Biochemistry 60 1996 1820 1825
    • (1996) Bioscience, Biotechnology, and Biochemistry , vol.60 , pp. 1820-1825
    • Hayase, F.1    Shibuya, T.2    Sato, J.3    Yamamoto, M.4
  • 21
    • 0025773632 scopus 로고
    • Immunochemical approach to characterize advanced glycation end products of the Maillard reaction
    • S. Horiuchi, N. Araki, and Y. Morino Immunochemical approach to characterize advanced glycation end products of the Maillard reaction Journal of Biological Chemistry 266 1991 7329 7332
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 7329-7332
    • Horiuchi, S.1    Araki, N.2    Morino, Y.3
  • 22
    • 0033212846 scopus 로고    scopus 로고
    • Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity
    • V. Jakus, M. Hrnciarova, J. Carsky, B. Krahulec, and N. Rietbrock Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity Life Sciences 65 1999 1991 1993
    • (1999) Life Sciences , vol.65 , pp. 1991-1993
    • Jakus, V.1    Hrnciarova, M.2    Carsky, J.3    Krahulec, B.4    Rietbrock, N.5
  • 23
    • 0022374267 scopus 로고
    • Role of aldose reductase in the development of diabetes-associated complications
    • P.F. Kador, and J.H. Kinoshita Role of aldose reductase in the development of diabetes-associated complications American Journal of Medicine 79 Suppl. 5A 1995 8 12
    • (1995) American Journal of Medicine , vol.79 , Issue.SUPPL. 5A , pp. 8-12
    • Kador, P.F.1    Kinoshita, J.H.2
  • 25
    • 0025368418 scopus 로고
    • Metabolism of 3-deoxyglucosone, an intermediate compound in the Maillard reaction, administered orally or intravenously to rats
    • H. Kato, N. van Chuyen, T. Shinoda, F. Sekiya, and F. Hayase Metabolism of 3-deoxyglucosone, an intermediate compound in the Maillard reaction, administered orally or intravenously to rats Biochimica et Biophysica Acta 1035 1990 71 76
    • (1990) Biochimica et Biophysica Acta , vol.1035 , pp. 71-76
    • Kato, H.1    Van Chuyen, N.2    Shinoda, T.3    Sekiya, F.4    Hayase, F.5
  • 26
    • 0027538067 scopus 로고
    • Detection of fructose-3-phosphokinase activity in intact mammalian lenses by 31P NMR spectroscopy
    • S. Lal, B.S. Szwergold, F. Kappler, and T. Brown Detection of fructose-3-phosphokinase activity in intact mammalian lenses by 31P NMR spectroscopy Journal of Biological Chemistry 268 1993 7763 7767
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 7763-7767
    • Lal, S.1    Szwergold, B.S.2    Kappler, F.3    Brown, T.4
  • 28
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • C.P. Lebel, H. Ischiropoulos, and S.C. Bondy Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress Chemical Research in Toxicology 5 1992 227 231
    • (1992) Chemical Research in Toxicology , vol.5 , pp. 227-231
    • Lebel, C.P.1    Ischiropoulos, H.2    Bondy, S.C.3
  • 29
    • 0025892834 scopus 로고
    • Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts
    • T.J. Lyons, G. Silvestri, J.A. Dunn, D.G. Dyer, and J.W. Baynes Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts Diabetes 40 1991 1010 1015
    • (1991) Diabetes , vol.40 , pp. 1010-1015
    • Lyons, T.J.1    Silvestri, G.2    Dunn, J.A.3    Dyer, D.G.4    Baynes, J.W.5
  • 30
    • 0036033536 scopus 로고    scopus 로고
    • Simicarbazide-sensitive amine oxidase in aortic smooth muscle cells mediates synthesis of a methyglyoxal-AGE: Implications for vascular complications in diabetes
    • K.C. Mathys, S.N. Ponnampalam, S. Padival, and R.H. Nagaraj 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 297 2002 863 869
    • (2002) Biochemical and Biophysical Research Communications , vol.297 , pp. 863-869
    • Mathys, K.C.1    Ponnampalam, S.N.2    Padival, S.3    Nagaraj, R.H.4
  • 32
    • 0023688775 scopus 로고
    • Analysis of sorbitol, galactitol, and myo-inositol in lens and sciatic nerve by high-performance liquid chromatography
    • I. Miwa, M. Kanbara, H. Wakazono, and J. Okuda Analysis of sorbitol, galactitol, and myo-inositol in lens and sciatic nerve by high-performance liquid chromatography Analytical Biochemistry 173 1988 39 44
    • (1988) Analytical Biochemistry , vol.173 , pp. 39-44
    • Miwa, I.1    Kanbara, M.2    Wakazono, H.3    Okuda, J.4
  • 33
    • 0028047418 scopus 로고
    • DNA damage by the glycation products of glyceraldehyde 3-phosphate and lysine
    • E.A. Mullokandov, W.A. Franklin, and M. Brownlee DNA damage by the glycation products of glyceraldehyde 3-phosphate and lysine Diabetologia 37 1994 145 149
    • (1994) Diabetologia , vol.37 , pp. 145-149
    • Mullokandov, E.A.1    Franklin, W.A.2    Brownlee, M.3
  • 34
    • 0035881048 scopus 로고    scopus 로고
    • Methylglyoxal, an endogenous aldehyde, crosslinks DNA polymerase and the substrate DNA
    • N. Murata-Kamiya, and H. Kamiya Methylglyoxal, an endogenous aldehyde, crosslinks DNA polymerase and the substrate DNA Nucleic Acids Research 29 2001 3433 3438
    • (2001) Nucleic Acids Research , vol.29 , pp. 3433-3438
    • Murata-Kamiya, N.1    Kamiya, H.2
  • 37
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal
    • S.A. Phillips, and P.J. Thornalley The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal European Journal of Biochemistry 212 1993 101 105
    • (1993) European Journal of Biochemistry , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 40
    • 17444442166 scopus 로고    scopus 로고
    • Oxidative DNA damage induced by high glucose and its suppression in human umbilical vein endothelial cells
    • K. Shimoi, A. Okitsu, M.H. Green, J.E. Lowe, T. Ohta, K. Kaji, H. Terato, H. Ide, and N. Kinae Oxidative DNA damage induced by high glucose and its suppression in human umbilical vein endothelial cells Mutation Research 480-481 2001 371 378
    • (2001) Mutation Research , vol.480-481 , pp. 371-378
    • Shimoi, K.1    Okitsu, A.2    Green, M.H.3    Lowe, J.E.4    Ohta, T.5    Kaji, K.6    Terato, H.7    Ide, H.8    Kinae, N.9
  • 41
    • 0031214523 scopus 로고    scopus 로고
    • Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct
    • I.N. Shipanova, M.A. Glomb, and R.H. Nagaraj Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct Archives of Biochemistry and Biophysics 344 1997 29 36
    • (1997) Archives of Biochemistry and Biophysics , vol.344 , pp. 29-36
    • Shipanova, I.N.1    Glomb, M.A.2    Nagaraj, R.H.3
  • 42
    • 0029442285 scopus 로고
    • The effectiveness of putative anti-cataract agents in the prevention of protein glycation
    • A. Stevens The effectiveness of putative anti-cataract agents in the prevention of protein glycation Journal of the American Optometric Association 66 1995 744 749
    • (1995) Journal of the American Optometric Association , vol.66 , pp. 744-749
    • Stevens, A.1
  • 43
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • P.J. Thornalley, A. Langborg, and H.S. Minhas Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose Biochemical Journal 344 1999 109 116
    • (1999) Biochemical Journal , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 46
    • 0033624640 scopus 로고    scopus 로고
    • Advanced glycation end products in human senile and diabetic cataractous lenses
    • S. Zarina, H.R. Zhao, and E.C. Abraham Advanced glycation end products in human senile and diabetic cataractous lenses Molecular and Cellular Biochemistry 210 2000 29 34
    • (2000) Molecular and Cellular Biochemistry , vol.210 , pp. 29-34
    • Zarina, S.1    Zhao, H.R.2    Abraham, E.C.3


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