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Volumn 99, Issue 3, 1997, Pages 457-468

Increased accumulation of the glycoxidation product N(ε)- (carboxymethyl)lysine in human tissues in diabetes and aging

Author keywords

Atherosclerosis; Complications of diabetes; Glycation; N( )(carboxymethyl)lysine; Oxidative stress

Indexed keywords

ALPHA TOCOPHEROL; AMINOGUANIDINE; CATALASE; DEFEROXAMINE; GLYCOSYLATED PROTEIN; LYSINE DERIVATIVE; SUPEROXIDE DISMUTASE; THIOCTIC ACID;

EID: 0030763201     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119180     Document Type: Article
Times cited : (691)

References (45)
  • 1
    • 0021320701 scopus 로고
    • Non-enzymatic glycosylation and the chronic complications of diabetes: An overview
    • Kennedy. L., and J.W. Baynes. 1984. Non-enzymatic glycosylation and the chronic complications of diabetes: an overview. Diabetologia. 26:93-98.
    • (1984) Diabetologia , vol.26 , pp. 93-98
    • Kennedy, L.1    Baynes, J.W.2
  • 2
    • 0021932625 scopus 로고
    • Non-enzymatic glycosylation of skin collagen in patients with limited joint mobility
    • Lyons, T.J., and L. Kennedy. 1985. Non-enzymatic glycosylation of skin collagen in patients with limited joint mobility. Diabetologia. 28:2-5.
    • (1985) Diabetologia , vol.28 , pp. 2-5
    • Lyons, T.J.1    Kennedy, L.2
  • 3
    • 0022523006 scopus 로고
    • Glycation of skin collagen in type 1 diabetes melliltus: Correlation with long-term complications
    • Vishwanatha, V., K.E. Frank, C.A. Elmets, P.J. Dauchot, and V.M. Monnier. 1986. Glycation of skin collagen in type 1 diabetes melliltus: correlation with long-term complications. Diabetes. 35:916-921.
    • (1986) Diabetes , vol.35 , pp. 916-921
    • Vishwanatha, V.1    Frank, K.E.2    Elmets, C.A.3    Dauchot, P.J.4    Monnier, V.M.5
  • 4
    • 0020334349 scopus 로고
    • ∈-Amino-lysine-bound glucose in human tissues obtained at autopsy: Increase in diabetes mellitus
    • Vogt, B., E. Schleicher, and O.H. Wieland. 1982. ∈-Amino-lysine-bound glucose in human tissues obtained at autopsy: increase in diabetes mellitus. Diabetes. 31:1123-1127.
    • (1982) Diabetes , vol.31 , pp. 1123-1127
    • Vogt, B.1    Schleicher, E.2    Wieland, O.H.3
  • 5
    • 0022480624 scopus 로고
    • Kinetic analysis of glycation as a tool for assessing the half-life of proteins
    • Schleicher, E., and O.H. Wieland. 1986. Kinetic analysis of glycation as a tool for assessing the half-life of proteins. Biochim. Biophys. Acta. 884:199-205.
    • (1986) Biochim. Biophys. Acta , vol.884 , pp. 199-205
    • Schleicher, E.1    Wieland, O.H.2
  • 9
    • 0001112738 scopus 로고
    • Aging of proteins: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose
    • Pongor, S., P.C. Ulrich, F.A. Bencsath, and A. Cerami. 1984. Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. Proc. Natl. Acad. Sci. USA. 81:2684-2688.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2684-2688
    • Pongor, S.1    Ulrich, P.C.2    Bencsath, F.A.3    Cerami, A.4
  • 10
    • 33749101557 scopus 로고
    • New aspects of the Maillard reaction in foods and in the human body
    • Ledl, F., and E. Schleicher. 1990. New aspects of the Maillard reaction in foods and in the human body. Angew. Chem. Int. Ed. Engl. 6:565-594.
    • (1990) Angew. Chem. Int. Ed. Engl. , vol.6 , pp. 565-594
    • Ledl, F.1    Schleicher, E.2
  • 11
    • 0022005139 scopus 로고
    • Detection of an advanced glucosylation product bound to protein in situ
    • Chang, J.C.F., P.C. Ulrich, R. Bucala, and A. Cerami. 1985. Detection of an advanced glucosylation product bound to protein in situ. J. Biol. Chem. 260: 7970-7974.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7970-7974
    • Chang, J.C.F.1    Ulrich, P.C.2    Bucala, R.3    Cerami, A.4
  • 12
    • 0023950461 scopus 로고
    • Advanced glycosylation endproducts in tissue and the biochemical basis of diabetic complications
    • Brownlee, M., A. Cerami, and H. Vlassara. 1988. Advanced glycosylation endproducts in tissue and the biochemical basis of diabetic complications. N. Engl. J. Med. 318:1315-1321.
    • (1988) N. Engl. J. Med. , vol.318 , pp. 1315-1321
    • Brownlee, M.1    Cerami, A.2    Vlassara, H.3
  • 13
    • 0026482265 scopus 로고
    • Advanced glycosylation: Chemistry, biology and implications for diabetes in aging
    • Bucala, R., and A. Cerami. 1992. Advanced glycosylation: chemistry, biology and implications for diabetes in aging. Adv. Pharmacol. 23:1-34.
    • (1992) Adv. Pharmacol. , vol.23 , pp. 1-34
    • Bucala, R.1    Cerami, A.2
  • 14
    • 0026703158 scopus 로고
    • Immunochemical detection of advanced glycosylation endproducts in vivo
    • Makila, Z., H. Vlassara, A. Cerami, and R. Bucala. 1992. Immunochemical detection of advanced glycosylation endproducts in vivo. J. Biol. Chem. 267:5133-5138.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5133-5138
    • Makila, Z.1    Vlassara, H.2    Cerami, A.3    Bucala, R.4
  • 15
    • 0001430544 scopus 로고
    • Accelerated age-related browing of human collagen in diabetes mellitus
    • Monnier, V.M., R.R. Kohn, and A. Cerami. 1984. Accelerated age-related browing of human collagen in diabetes mellitus. Proc. Natl. Acad. Sci. USA. 81:583-587.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 583-587
    • Monnier, V.M.1    Kohn, R.R.2    Cerami, A.3
  • 18
    • 0024852380 scopus 로고
    • Structure elucidation of a senescense cross-link from human extracellular matrix: Implication of pentosidine in the aging process
    • Sell, D.R., and V.M. Monnier. 1989. Structure elucidation of a senescense cross-link from human extracellular matrix: implication of pentosidine in the aging process. J. Biol. Chem. 264:21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 19
    • 0023656122 scopus 로고
    • Detection of D-glucose-derived pyrrole compounds during Maillard reaction under physiological conditions
    • Njoroge, F.G., L.M. Sayre, and V.M. Monnier. 1987. Detection of D-glucose-derived pyrrole compounds during Maillard reaction under physiological conditions. Carbohydr. Res. 167:211-220.
    • (1987) Carbohydr. Res. , vol.167 , pp. 211-220
    • Njoroge, F.G.1    Sayre, L.M.2    Monnier, V.M.3
  • 20
    • 0022931516 scopus 로고
    • ∈(carboxymethyl)lysine as a degradation product of fructose lysine in glycated protein
    • ∈(carboxymethyl)lysine as a degradation product of fructose lysine in glycated protein. J. Biol. Chem. 261:4889-4894.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 22
    • 0025732948 scopus 로고
    • Perspectives in diabetes. Role of oxidative stress in development of complications in diabetes
    • Baynes, J.W. 1991. Perspectives in diabetes. Role of oxidative stress in development of complications in diabetes. Diabetes. 40:405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 23
    • 0026782087 scopus 로고
    • Role of oxygen in cross-linking and chemical modifications of collagen by glucose
    • Fu, M.X., K.J. Knecht, S.R. Thorpe, and J.W. Baynes. 1992. Role of oxygen in cross-linking and chemical modifications of collagen by glucose. Diabetes. 41:42-48.
    • (1992) Diabetes , vol.41 , pp. 42-48
    • Fu, M.X.1    Knecht, K.J.2    Thorpe, S.R.3    Baynes, J.W.4
  • 26
    • 0027451507 scopus 로고
    • Differential effects of type 2 (noninsulin-dependent) diabetes mellitus on pentosidine formation in skin and glomerular basement membrane
    • Sell, D.R., E.C. Carlson, and V.M. Monnier. 1993. Differential effects of type 2 (noninsulin-dependent) diabetes mellitus on pentosidine formation in skin and glomerular basement membrane. Diabetologia. 36:936-941.
    • (1993) Diabetologia , vol.36 , pp. 936-941
    • Sell, D.R.1    Carlson, E.C.2    Monnier, V.M.3
  • 27
    • 0026675759 scopus 로고
    • Pentosidine formation in skin correlates with severity of complication in individuals with long-standing IDDM
    • Sell, D.R., A. Lapolla, P. Odetti, J. Fogarty, and V.M. Monnier. 1992. Pentosidine formation in skin correlates with severity of complication in individuals with long-standing IDDM. Diabetes. 41:1286-1292.
    • (1992) Diabetes , vol.41 , pp. 1286-1292
    • Sell, D.R.1    Lapolla, A.2    Odetti, P.3    Fogarty, J.4    Monnier, V.M.5
  • 28
    • 0027233741 scopus 로고
    • Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus
    • McCance, D.R., D.O. Dyer, J.A. Dunn, K.E. Bailie, S.R. Thorpe, and J.W. Baynes. 1993. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J. Clin. Invest. 91:2470-2478.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2470-2478
    • McCance, D.R.1    Dyer, D.O.2    Dunn, J.A.3    Bailie, K.E.4    Thorpe, S.R.5    Baynes, J.W.6
  • 29
    • 0027169317 scopus 로고
    • Increased collagen-linked pentosidine levels and advanced glucosylation endproducts in early diabetic nephropathy
    • Beisswenger, P.J., L.L. Moore, and T. Brink-Johnsen. 1993. Increased collagen-linked pentosidine levels and advanced glucosylation endproducts in early diabetic nephropathy. J. Clin. Invest. 92:212-217.
    • (1993) J. Clin. Invest. , vol.92 , pp. 212-217
    • Beisswenger, P.J.1    Moore, L.L.2    Brink-Johnsen, T.3
  • 30
    • 84961481757 scopus 로고
    • Specific quantitation by HPLC of protein (lysine) bound glucose in human serum albumin and other glycosylated proteins
    • Schleicher, E., and O.H. Wieland. 1981. Specific quantitation by HPLC of protein (lysine) bound glucose in human serum albumin and other glycosylated proteins. J. Clin. Chem. Clin. Biochem. 19:81-87.
    • (1981) J. Clin. Chem. Clin. Biochem. , vol.19 , pp. 81-87
    • Schleicher, E.1    Wieland, O.H.2
  • 31
    • 0010283436 scopus 로고
    • Characterization of antibodies against carboxymethyllysine-modified proteins
    • T.P. Labuza, G.A. Reineccius, V.M. Monnier, J. O'Brien, and J.W. Baynes, editors. The Royal Society of Chemistry, Cambridge
    • Gempel, K., E. Wagner, and E. Schleicher. 1994. Characterization of antibodies against carboxymethyllysine-modified proteins. In Maillard reactions in chemistry, food and health. T.P. Labuza, G.A. Reineccius, V.M. Monnier, J. O'Brien, and J.W. Baynes, editors. The Royal Society of Chemistry, Cambridge. 392-396.
    • (1994) Maillard Reactions in Chemistry, Food and Health , pp. 392-396
    • Gempel, K.1    Wagner, E.2    Schleicher, E.3
  • 32
    • 0025943567 scopus 로고
    • Immunohistochemical localization of extracellular matrix in human diabetic glomerular lesions
    • Nerlich, A., and E. Schleicher. 1991. Immunohistochemical localization of extracellular matrix in human diabetic glomerular lesions. Am. J. Pathol. 139: 889-899.
    • (1991) Am. J. Pathol. , vol.139 , pp. 889-899
    • Nerlich, A.1    Schleicher, E.2
  • 33
    • 84941840688 scopus 로고
    • Impaired immunoglobulin G Fc fragment function in diabetics is caused by a mechanism different from glycation
    • Dolhofer-Bliesener, R., B. Lechner, and K.-D. Gerbitz. 1994. Impaired immunoglobulin G Fc fragment function in diabetics is caused by a mechanism different from glycation. Eur. J. Clin. Chem. Clin. Biochem. 32:329-336.
    • (1994) Eur. J. Clin. Chem. Clin. Biochem. , vol.32 , pp. 329-336
    • Dolhofer-Bliesener, R.1    Lechner, B.2    Gerbitz, K.-D.3
  • 34
    • 0028826628 scopus 로고
    • Pathways of formation of glycoxidation products during glycation of collagen
    • Wells-Knecht, M.C., S.R. Thorpe, and J.W. Baynes. 1995. Pathways of formation of glycoxidation products during glycation of collagen. Biochemistry. 34:15134-15141.
    • (1995) Biochemistry , vol.34 , pp. 15134-15141
    • Wells-Knecht, M.C.1    Thorpe, S.R.2    Baynes, J.W.3
  • 35
    • 0029665694 scopus 로고    scopus 로고
    • ∈-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction
    • ∈-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. Biochemistry. 35:8075-8083.
    • (1996) Biochemistry , vol.35 , pp. 8075-8083
    • Ikeda, K.1    Higashi, T.2    Sano, H.3    Jinnouchi, Y.4    Yoshida, M.5    Araki, T.6    Ueda, S.7    Horiuchi, S.8
  • 36
    • 0025773632 scopus 로고
    • Immunochemical approach to characterize advanced glycation end products of the Maillard reaction
    • Horiuchi, S., N. Araki, and Y. Morino. 1991. Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. J. Biol. Chem. 266:7329-7332.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7329-7332
    • Horiuchi, S.1    Araki, N.2    Morino, Y.3
  • 37
    • 0004818738 scopus 로고
    • High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: A potential mechanism for the removal of senescent macromolecules
    • Vlassara, H., M. Brownlee, and A. Cerami. 1985. High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proc. Natl. Acad. Sci. USA. 82:5588-5592.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5588-5592
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 39
    • 0026629007 scopus 로고
    • Immunohistochemical detection of advanced glycation endproduct in diabetic tissue using monoclonal antibody to pyrraline
    • Miyata, S., and V.M. Monnier. 1992. Immunohistochemical detection of advanced glycation endproduct in diabetic tissue using monoclonal antibody to pyrraline. J. Clin. Invest. 89:1102-1112.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1102-1112
    • Miyata, S.1    Monnier, V.M.2
  • 41
    • 0029121260 scopus 로고
    • Immunohistochemical and ultrastructural detection of advanced glycalion end products in atherosclerotic lesions of human aorta with a novel specific monoclonal antibody
    • Kume, S., M. Takeya, T. Mori. N. Araki. H. Suzuki, S. Horiuchi, T. Kodama, Y. Miyauchi, and K. Takahashi. 1995. Immunohistochemical and ultrastructural detection of advanced glycalion end products in atherosclerotic lesions of human aorta with a novel specific monoclonal antibody. Am. J. Pathol. 147:654-667.
    • (1995) Am. J. Pathol. , vol.147 , pp. 654-667
    • Kume, S.1    Takeya, M.2    Mori, T.3    Araki, N.4    Suzuki, H.5    Horiuchi, S.6    Kodama, T.7    Miyauchi, Y.8    Takahashi, K.9
  • 43
    • 0027162744 scopus 로고
    • Immunochemical detection of advanced glycation endproducts in renal cortex from STZ-induced diabetic rats
    • Mitushashi, T., H. Nakayama, T. Itoh. S. Kuwajima. S. Aoki. T. Atsumi. and T. Koide. 1993. Immunochemical detection of advanced glycation endproducts in renal cortex from STZ-induced diabetic rats. Diabetes. 42:826-832.
    • (1993) Diabetes , vol.42 , pp. 826-832
    • Mitushashi, T.1    Nakayama, H.2    Itoh, T.3    Kuwajima, S.4    Aoki, S.5    Atsumi, T.6    Koide, T.7
  • 44
    • 0028223128 scopus 로고
    • Glycalion. glycosylation. and cross-linking of collagen by glucose. Kinetics, mechanims, and inhibition of the late stages of the Maillard reaction
    • Fu, M.X., K.J. Wells-Knecht, J.A. Blackledge, T.J. Lyons. S.R. Thorpe, and J.W. Baynes. 1994. Glycalion. glycosylation. and cross-linking of collagen by glucose. Kinetics, mechanims, and inhibition of the late stages of the Maillard reaction. Diabetes. 43:676-683.
    • (1994) Diabetes , vol.43 , pp. 676-683
    • Fu, M.X.1    Wells-Knecht, K.J.2    Blackledge, J.A.3    Lyons, T.J.4    Thorpe, S.R.5    Baynes, J.W.6


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