메뉴 건너뛰기




Volumn 100, Issue 4, 1997, Pages 839-846

Age-dependent increase in ortho-tyrosine and methionine sulfoxide in human skin collagen is not accelerated in diabetes - Evidence against a generalized increase in oxidative stress in diabetes

Author keywords

Advanced glycation end products; Carboxymethyllysine; Glycation; Oxidation; Pentosidine

Indexed keywords

3 (2 HYDROXYPHENYL)ALANINE; COLLAGEN; GLYCOSYLATED PROTEIN; METHIONINE SULFOXIDE; N (CARBOXYMETHYL)LYSINE; PENTOSIDINE; UNCLASSIFIED DRUG;

EID: 0030866161     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119599     Document Type: Article
Times cited : (137)

References (48)
  • 1
    • 0025732948 scopus 로고
    • The role of oxidative stress in the development of complications in diabetes
    • Baynes, J.W. 1991. The role of oxidative stress in the development of complications in diabetes. Diabetes. 40:405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 2
    • 0028272883 scopus 로고
    • Pathogenic effects of advanced glycosylation: Biochemical, biologic and clinical implications for diabetes and aging
    • Vlassara, H., R. Bucala, and L. Striker. 1994. Pathogenic effects of advanced glycosylation: biochemical, biologic and clinical implications for diabetes and aging. Lab. Invest. 70:138-151.
    • (1994) Lab. Invest. , vol.70 , pp. 138-151
    • Vlassara, H.1    Bucala, R.2    Striker, L.3
  • 3
    • 0026675759 scopus 로고
    • Pentosidine formation in skin correlates with severity of complications 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 complications 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
  • 5
    • 0027169317 scopus 로고
    • Increased collagen-linked pentosidine levels and advanced glycosylation end products in early diabetic nephropathy
    • Beisswenger, P.J., L.L. Moore, T. Brinck-Johnsen, and T.J. Curphey. 1993. Increased collagen-linked pentosidine levels and advanced glycosylation end products 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    Brinck-Johnsen, T.3    Curphey, T.J.4
  • 6
    • 0025174842 scopus 로고
    • End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen
    • Sell, D.R., and V.M. Monnier. 1990. End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen. J. Clin. Invest. 75:380-384.
    • (1990) J. Clin. Invest. , vol.75 , pp. 380-384
    • Sell, D.R.1    Monnier, V.M.2
  • 8
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification: The potential role of autoxidative glycosylation in diabetes
    • Wolff, S.P., and R.T. Dean. 1987. Glucose autoxidation and protein modification: the potential role of autoxidative glycosylation in diabetes. Biochem. J. 245:243-250.
    • (1987) Biochem. J. , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 9
    • 0025853670 scopus 로고
    • Protein glycation and oxidative stress in diabetes mellitus and ageing
    • Wolff, S.P., Z.Y. Jiang, and J.V. Hunt. 1991. Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radical Biol. Med. 10:339-352.
    • (1991) Free Radical Biol. Med. , vol.10 , pp. 339-352
    • Wolff, S.P.1    Jiang, Z.Y.2    Hunt, J.V.3
  • 10
    • 0001836190 scopus 로고    scopus 로고
    • The role of oxidation in the Maillard reaction in vivo
    • R. Ikan, editor. John Wiley & Sons Inc., New York
    • Baynes, J.W. 1996. The role of oxidation in the Maillard reaction in vivo. In The Maillard Reaction: Consequences for the Chemical and Life Sciences. R. Ikan, editor. John Wiley & Sons Inc., New York. pp. 55-72.
    • (1996) The Maillard Reaction: Consequences for the Chemical and Life Sciences , pp. 55-72
    • Baynes, J.W.1
  • 11
    • 1842423094 scopus 로고    scopus 로고
    • The role of oxidative stress in diabetic complications
    • Baynes, J.W., and S.R. Thorpe. 1996. The role of oxidative stress in diabetic complications. Curr. Opin. Endocrinol. Diabetes. 3:277-284.
    • (1996) Curr. Opin. Endocrinol. Diabetes , vol.3 , pp. 277-284
    • Baynes, J.W.1    Thorpe, S.R.2
  • 12
    • 0025948114 scopus 로고
    • Mechanism of formation of the Maillard protein cross-link, pentosidine: Glucose, fructose and ascorbate as pentosidine precursors
    • Grandhee, S.K., and V.M. Monnier. 1991. Mechanism of formation of the Maillard protein cross-link, pentosidine: glucose, fructose and ascorbate as pentosidine precursors. J. Biol. Chem. 266:11649-11653.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11649-11653
    • Grandhee, S.K.1    Monnier, V.M.2
  • 13
    • 0025945553 scopus 로고
    • Formation of pentosidine during nonenzymatic browning of proteins by glucose: Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo
    • Dyer, D.G., J.A. Blackledge, S.R. Thorpe, and J.W. Baynes. 1991. Formation of pentosidine during nonenzymatic browning of proteins by glucose: identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. J. Biol. Chem. 266:11654-11660.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11654-11660
    • Dyer, D.G.1    Blackledge, J.A.2    Thorpe, S.R.3    Baynes, J.W.4
  • 15
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methioninc sulfoxide residues in proteins
    • Brot, N., and H. Weissbach. 1983. Biochemistry and physiological role of methioninc sulfoxide residues in proteins. Arch. Biochem. Biophys. 223:271-281.
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 16
    • 0028852816 scopus 로고
    • Oxidation of methionine residues in proteins: Tools, targets, and reversal
    • Vogt, W. 1995. Oxidation of methionine residues in proteins: tools, targets, and reversal. Free Radical Biol. Med. 18:93-105.
    • (1995) Free Radical Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 17
    • 0027180882 scopus 로고
    • Formation of o-tyrosine and dityrosine in protein during radiolytic and metal-catalyzed oxidation
    • Huggins, T.G., M.C. Wells-Knecht, N.A., Detorie, J.W. Baynes, and S.R. Thorpe. 1993. Formation of o-tyrosine and dityrosine in protein during radiolytic and metal-catalyzed oxidation. J. Biol. Chem. 268:12341-12347.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12341-12347
    • Huggins, T.G.1    Wells-Knecht, M.C.2    Detorie, N.A.3    Baynes, J.W.4    Thorpe, S.R.5
  • 18
    • 0027254198 scopus 로고
    • Oxidized amino acids in lens proteins with age. Measurement of o-tyrosine and dityrosine in the aging human lens
    • Wells-Knecht, M.C., T.G. Huggins, D.G. Dyer, S.R. Thorpe, and J.W. Baynes. 1993. Oxidized amino acids in lens proteins with age. Measurement of o-tyrosine and dityrosine in the aging human lens. J. Biol. Chem. 268:12348-12352.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12348-12352
    • Wells-Knecht, M.C.1    Huggins, T.G.2    Dyer, D.G.3    Thorpe, S.R.4    Baynes, J.W.5
  • 19
    • 0026018991 scopus 로고
    • Oxidative degradation of glycated proteins: Effect of diabetes and aging on carboxymethyllysine levels in human urine
    • Knecht, K.J., J.A. Dunn, K.F. McFarland, S.R. Thorpe, and J.W. Baynes. 1991. Oxidative degradation of glycated proteins: effect of diabetes and aging on carboxymethyllysine levels in human urine. Diabetes. 40:190-196.
    • (1991) Diabetes , vol.40 , pp. 190-196
    • Knecht, K.J.1    Dunn, J.A.2    McFarland, K.F.3    Thorpe, S.R.4    Baynes, J.W.5
  • 20
    • 0026782087 scopus 로고
    • Role of oxygen in the crosslinking and chemical modification of protein by glucose
    • Fu, M.-X., K.J. Knecht, S.R. Thorpe, and J.W. Baynes. 1992. Role of oxygen in the crosslinking and chemical modification of protein by glucose. Diabeles. 41(Suppl. 2):42-48.
    • (1992) Diabeles , vol.41 , Issue.2 SUPPL. , pp. 42-48
    • Fu, M.-X.1    Knecht, K.J.2    Thorpe, S.R.3    Baynes, J.W.4
  • 21
    • 0028223128 scopus 로고
    • Glycation, glycoxidation and crosslinking of collagen by glucose: Kinetics, mechanisms and inhibition of 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. Glycation, glycoxidation and crosslinking of collagen by glucose: kinetics, mechanisms and inhibition of 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
  • 22
    • 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
  • 23
    • 0023664488 scopus 로고
    • Effects of phosphate on the kinetics and specificity of glycation of protein
    • Watkins, N.G., C.I. Neglia, D.G. Dyer, S.R. Thorpe, and J.W. Baynes. 1987. Effects of phosphate on the kinetics and specificity of glycation of protein. J. Biol. Chem. 262:7207-7212.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7207-7212
    • Watkins, N.G.1    Neglia, C.I.2    Dyer, D.G.3    Thorpe, S.R.4    Baynes, J.W.5
  • 24
    • 0028798704 scopus 로고
    • Formation of reactive intermediates from Amadori compounds under physiological conditions
    • Zyzak, D.V., J.M. Richardson, S.R. Thorpe, and J.W. Baynes. 1995. Formation of reactive intermediates from Amadori compounds under physiological conditions. Arch. Biochem. Biophys. 316:547-554.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 547-554
    • Zyzak, D.V.1    Richardson, J.M.2    Thorpe, S.R.3    Baynes, J.W.4
  • 25
    • 0008750946 scopus 로고
    • Nephrocytomegaly in rats induced by Maillard reaction products: The involvement of metal ions
    • Finot, P.A., and D.E. Furniss. 1986. Nephrocytomegaly in rats induced by Maillard reaction products: the involvement of metal ions. Dev. Food Sci. 13: 493-502.
    • (1986) Dev. Food Sci. , vol.13 , pp. 493-502
    • Finot, P.A.1    Furniss, D.E.2
  • 26
    • 0025293777 scopus 로고
    • Hydrogen peroxide generation during experimental protein glycation
    • Jiang, Z.Y., A.C.S. Woolard, and S.P. Wolff. 1990. Hydrogen peroxide generation during experimental protein glycation. FEBS Lett. 268:69-71.
    • (1990) FEBS Lett. , vol.268 , pp. 69-71
    • Jiang, Z.Y.1    Woolard, A.C.S.2    Wolff, S.P.3
  • 27
    • 15844366271 scopus 로고    scopus 로고
    • Involvement of hydrogen peroxide in collagen cross-linking by high glucose in vitro and in vivo
    • Elgawish, A., M. Glomb, M. Friedlander, and V.M. Monnier. 1996. Involvement of hydrogen peroxide in collagen cross-linking by high glucose in vitro and in vivo. J. Biol. Chem. 271:12964-12971.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12964-12971
    • Elgawish, A.1    Glomb, M.2    Friedlander, M.3    Monnier, V.M.4
  • 29
    • 0027273039 scopus 로고
    • Potential therapeutic approaches to the treatment or prevention of diabetic neuropathy: Evidence from experimental studies
    • Cameron, N.E., and M.A. Cotter. 1993. Potential therapeutic approaches to the treatment or prevention of diabetic neuropathy: evidence from experimental studies. Diabetic Medicine. 10:593-605.
    • (1993) Diabetic Medicine , vol.10 , pp. 593-605
    • Cameron, N.E.1    Cotter, M.A.2
  • 30
    • 0003229895 scopus 로고
    • Reactive oxygen in the aetiology and complications of diabetes
    • C. Ioannides, editor. Pergamon Press, London
    • Baynes J.W. 1995. Reactive oxygen in the aetiology and complications of diabetes. In Drugs, Diet and Disease. Vol. 2: Mechanistic Approaches to Diabetes. C. Ioannides, editor. Pergamon Press, London. 203-240.
    • (1995) Drugs, Diet and Disease. Vol. 2: Mechanistic Approaches to Diabetes , vol.2 , pp. 203-240
    • Baynes, J.W.1
  • 31
    • 0030048496 scopus 로고    scopus 로고
    • Oxidative stress and diabetic vascular complications
    • Giugliano, D., A. Ceriello, and G. Paolisso. 1996. Oxidative stress and diabetic vascular complications. Diabetes Care. 19:257-265.
    • (1996) Diabetes Care , vol.19 , pp. 257-265
    • Giugliano, D.1    Ceriello, A.2    Paolisso, G.3
  • 32
    • 1842347445 scopus 로고    scopus 로고
    • Glycation, oxidation, and lipoxidation in the development of the complications of diabetes mellitus: A carbonyl stress hypothesis
    • In press
    • Lyons, T.J., and A.J. Jenkins. 1996. Glycation, oxidation, and lipoxidation in the development of the complications of diabetes mellitus: a carbonyl stress hypothesis. Diab. Rev. In press.
    • (1996) Diab. Rev.
    • Lyons, T.J.1    Jenkins, A.J.2
  • 35
    • 0028791236 scopus 로고
    • Effects of natural free radical scavengers on peripheral nerve and neurovascular function in diabetic rats
    • Cameron, M.A., A, Love, M.J. Watt, N.F. Cameron, and K.C. Dines. 1995. Effects of natural free radical scavengers on peripheral nerve and neurovascular function in diabetic rats. Diabetologia. 38:1285-1294.
    • (1995) Diabetologia , vol.38 , pp. 1285-1294
    • Cameron, M.A.1    Love, A.2    Watt, M.J.3    Cameron, N.F.4    Dines, K.C.5
  • 36
    • 0030022084 scopus 로고    scopus 로고
    • Inhibition of development of peripheral neuropathy in streptozotocin-induced diabetic rats with N-acetylcysteine
    • Sagara, M., J. Satoh, R. Wada, S. Yagihashi, K. Takahashi, M. Fukuzawa, G. Muto, Y. Muto, and T. Toyota. 1996. Inhibition of development of peripheral neuropathy in streptozotocin-induced diabetic rats with N-acetylcysteine. Diabetologia. 39:263-269.
    • (1996) Diabetologia , vol.39 , pp. 263-269
    • Sagara, M.1    Satoh, J.2    Wada, R.3    Yagihashi, S.4    Takahashi, K.5    Fukuzawa, M.6    Muto, G.7    Muto, Y.8    Toyota, T.9
  • 37
    • 0028790808 scopus 로고
    • Chronic vitamin E treatment prevents defective endothelium-dependent relaxation in diabetic rat aorta
    • Keegan, A., H. Walbank, M.A. Cotter, and N.E. Cameron. 1995. Chronic vitamin E treatment prevents defective endothelium-dependent relaxation in diabetic rat aorta. Diabetologia. 38:1475-1478.
    • (1995) Diabetologia , vol.38 , pp. 1475-1478
    • Keegan, A.1    Walbank, H.2    Cotter, M.A.3    Cameron, N.E.4
  • 38
    • 0344697076 scopus 로고    scopus 로고
    • Studies in animal models on the role of glycation and advanced glycation end-products (AGEs) in the pathogenesis of diabetic complications: Pitfalls and limitations
    • A. Sima, editor. Birkhäuser, Boston. In press
    • Requena, J.R., and J.W. Baynes. 1997. Studies in animal models on the role of glycation and advanced glycation end-products (AGEs) in the pathogenesis of diabetic complications: pitfalls and limitations. In Lessons from Animal Diabetes. Vol. VII. A. Sima, editor. Birkhäuser, Boston. In press.
    • (1997) Lessons from Animal Diabetes , vol.7
    • Requena, J.R.1    Baynes, J.W.2
  • 40
    • 0028310848 scopus 로고
    • Immunological quantification of advanced glycosylation end-products in the serum of patients on hemodialysis or CAPD
    • Papastanasiou, P., L. Grass, H. Rodela, A. Patrikarea, D. Oreopoulos, and E.P. Diamandis. 1994. Immunological quantification of advanced glycosylation end-products in the serum of patients on hemodialysis or CAPD. Kidney Int. 46:216-222.
    • (1994) Kidney Int. , vol.46 , pp. 216-222
    • Papastanasiou, P.1    Grass, L.2    Rodela, H.3    Patrikarea, A.4    Oreopoulos, D.5    Diamandis, E.P.6
  • 41
    • 0029875833 scopus 로고    scopus 로고
    • High glucose induces antioxidant enzymes in human endothelial cells in culture: Evidence linking hyperglycemia and oxidative stress
    • Ceriello, A., P. dello Russo, P. Armstad, and P. Cerutti. 1996. High glucose induces antioxidant enzymes in human endothelial cells in culture: evidence linking hyperglycemia and oxidative stress. Diabetes. 45:471-477.
    • (1996) Diabetes , vol.45 , pp. 471-477
    • Ceriello, A.1    Dello Russo, P.2    Armstad, P.3    Cerutti, P.4
  • 42
    • 0028068046 scopus 로고
    • Cellular receptors for advanced glycation end products: Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions
    • Schmidt, A.M., O. Hori, J. Brett, S.-D. Yan, J.L. Wautier, and D. Stern. 1994. Cellular receptors for advanced glycation end products: implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions. Arterioscler. Thromb. 14:1521-1528.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 1521-1528
    • Schmidt, A.M.1    Hori, O.2    Brett, J.3    Yan, S.-D.4    Wautier, J.L.5    Stern, D.6
  • 43
    • 0004931777 scopus 로고
    • Reactive oxygen processes in diabetes
    • P.K. Singal, editor. Kluwer Academic Publishers, Norwell, MA
    • Godin, D.V., and S.A. Wohaieb. 1988. Reactive oxygen processes in diabetes. In Oxygen Radicals in Pathophysiology of Heart Disease. P.K. Singal, editor. Kluwer Academic Publishers, Norwell, MA. pp. 302-322.
    • (1988) Oxygen Radicals in Pathophysiology of Heart Disease , pp. 302-322
    • Godin, D.V.1    Wohaieb, S.A.2
  • 44
    • 0023770113 scopus 로고
    • Free radicals and diabetes
    • Oberley, L.W. 1988. Free radicals and diabetes. Free Radical Biol. Med. 5:113-124.
    • (1988) Free Radical Biol. Med. , vol.5 , pp. 113-124
    • Oberley, L.W.1
  • 45
    • 0029164710 scopus 로고
    • Role of oxidized amino acids in protein breakdown and stability
    • Stadtman, E.R. 1995. Role of oxidized amino acids in protein breakdown and stability. Methods Enzymol. 258:379-393.
    • (1995) Methods Enzymol. , vol.258 , pp. 379-393
    • Stadtman, E.R.1
  • 46
    • 0031051893 scopus 로고    scopus 로고
    • Quantitation of malondialdehyde and 4-hydroxy-nonenal adducts to lysine residues in native and oxidized human low-density lipoprotein
    • Requena, J.R., M.-X. Fu, M.U. Ahmed, A.J. Jenkins, T.J. Lyons, J.W. Baynes, and S.R. Thorpe. 1997. Quantitation of malondialdehyde and 4-hydroxy-nonenal adducts to lysine residues in native and oxidized human low-density lipoprotein. Biochem J. 322:317-325.
    • (1997) Biochem J. , vol.322 , pp. 317-325
    • Requena, J.R.1    Fu, M.-X.2    Ahmed, M.U.3    Jenkins, A.J.4    Lyons, T.J.5    Baynes, J.W.6    Thorpe, S.R.7
  • 47
    • 0027082270 scopus 로고
    • Role of free radicals in aging and disease
    • Harman, D. 1992. Role of free radicals in aging and disease. Ann. NY Acad. Sci. 673:126-141.
    • (1992) Ann. NY Acad. Sci. , vol.673 , pp. 126-141
    • Harman, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.