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Volumn 139, Issue 1, 2003, Pages 49-55

Advanced glycation end product and chronic complications of diabetes mellitus;Productos finales de glicación avanzada y complicaciones crónicas de la diabetes mellitus

(1)  Méndez, José D a  

a NONE

Author keywords

Advanced glycation end products; Chronic complications; Diabetes mellitus; Glucose; Glycation

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ADVANCED GLYCATION END PRODUCT RECEPTOR; AMADORINS; PROTEIN; RECEPTOR BLOCKING AGENT; UNCLASSIFIED DRUG;

EID: 0037223526     PISSN: 00163813     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (10)

References (51)
  • 1
    • 0019363254 scopus 로고
    • The biochemistry of the complications of diabetes mellitus
    • Brownlee M, Cerami A. The biochemistry of the complications of diabetes mellitus. Annu Rev Biochem. 1981;50:385-432.
    • (1981) Annu Rev Biochem , vol.50 , pp. 385-432
    • Brownlee, M.1    Cerami, A.2
  • 2
    • 0021231172 scopus 로고
    • Nonenzymatic glycosilation and the pathogenesis of diabetic complications
    • Brownlee M, Vlassara H, Cerami A. Nonenzymatic glycosilation and the pathogenesis of diabetic complications. Ann Int Med. 1984;101(4):527-537.
    • (1984) Ann Int Med , vol.101 , Issue.4 , pp. 527-537
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 3
    • 0020620893 scopus 로고
    • Metabolic abnormalities in diabetic peripheral nerve: Relation to impaired function
    • Green DA. Metabolic abnormalities in diabetic peripheral nerve: relation to impaired function. Metabolism 1983;32: 118-123.
    • (1983) Metabolism , vol.32 , pp. 118-123
    • Green, D.A.1
  • 4
    • 0002568641 scopus 로고
    • The role of abnormal polyol metabolism in diabetic complications
    • Brodoff BN, Bleicher SJ. Baltimore Williams and Wilkins USA
    • Clements RS Jr. The role of abnormal polyol metabolism in diabetic complications. En: Brodoff BN, Bleicher SJ. Diabetes Mellitus and Obesity. Baltimore Williams and Wilkins USA, 1982, pp 117-128.
    • (1982) Diabetes Mellitus and Obesity , pp. 117-128
    • Clements R.S., Jr.1
  • 6
    • 0001954190 scopus 로고
    • Toward a Maillard reaction theory of aging
    • Baynes JW, Monier VM. Eds. Progress in Clinical and Biological Research. Alan R. Liss, Inc. New York
    • Monier VM. Toward a Maillard reaction theory of aging. In: The Maillard reaction in aging, Diabetes, and Nutrition. Baynes JW, Monier VM. Eds. Progress in Clinical and Biological Research Vol. 34 Alan R. Liss, Inc. New York. 1989. Pp 1-22.
    • (1989) The Maillard Reaction in Aging, Diabetes, and Nutrition , vol.34 , pp. 1-22
    • Monier, V.M.1
  • 7
    • 0018843839 scopus 로고
    • Nonenzymatic glycosylation of eritrocyte membrane proteins: Relevance to diabetes
    • Miller JA, Gravallese E, Bunn HF. Nonenzymatic glycosylation of eritrocyte membrane proteins: relevance to diabetes. J Clin Invest 1980;65:896-901.
    • (1980) J Clin Invest , vol.65 , pp. 896-901
    • Miller, J.A.1    Gravallese, E.2    Bunn, H.F.3
  • 8
    • 0032197141 scopus 로고    scopus 로고
    • Towards a new age of the chemistry and pathophysiology of the Maillard reaction
    • Munch G, Colaco C. Towards a new age of the chemistry and pathophysiology of the Maillard reaction. Cell Mol Biol. 1998; 44(7):ix-x.
    • (1998) Cell Mol Biol , vol.44 , Issue.7
    • Munch, G.1    Colaco, C.2
  • 11
    • 0032563120 scopus 로고    scopus 로고
    • Role of the Maillard reaction in aging of tissue proteins
    • Frie EB, Dehenhart TP, Thorpe SR, Baynes JW. Role of the Maillard reaction in aging of tissue proteins. J Biol Chem. 1998;273(30):18714-18919.
    • (1998) J Biol Chem , vol.273 , Issue.30 , pp. 18714-18919
    • Frie, E.B.1    Dehenhart, T.P.2    Thorpe, S.R.3    Baynes, J.W.4
  • 12
    • 0022868106 scopus 로고
    • Diabetic control and microvascular complications: The near normoglycemic experience
    • Hanssen KF, Dahl-Jorgensen K, Lauritzen T. Diabetic control and microvascular complications: The near normoglycemic experience. Diabetologia 1986;29:677-684.
    • (1986) Diabetologia , vol.29 , pp. 677-684
    • Hanssen, K.F.1    Dahl-Jorgensen, K.2    Lauritzen, T.3
  • 13
    • 0023950461 scopus 로고
    • Advanced glycosylation end-products in tissue and the biochemical basis of diabetic complications
    • Brownlee M, Cerami AJ, Vlassara H. Advanced glycosylation end-products in tissue and the biochemical basis of diabetic complications. N Engl J Med. 1988;318:1315-1321.
    • (1988) N Engl J Med , vol.318 , pp. 1315-1321
    • Brownlee, M.1    Cerami, A.J.2    Vlassara, H.3
  • 14
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • Baynes JW. Role of oxidative stress in development of complications in diabetes. Diabetes. 1991;40:405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 15
    • 0030796507 scopus 로고    scopus 로고
    • Glycaemic control and in vivo non oxidative Maillard reaction: Urinary excretion of pyrraline in diabetes patients
    • Portero-Otin M, Pamplona R, Bellmunt MJ, Bergua M, Prat J. Glycaemic control and in vivo non oxidative Maillard reaction: urinary excretion of pyrraline in diabetes patients. Eur J Clin Invest. 1997;27:767-773.
    • (1997) Eur J Clin Invest , vol.27 , pp. 767-773
    • Portero-Otin, M.1    Pamplona, R.2    Bellmunt, M.J.3    Bergua, M.4    Prat, J.5
  • 16
    • 0028223128 scopus 로고
    • Glycation glycoxidation and crosslinking of collagen by glucose: Kinetics, mechanisms and inhibition of late stages of the Maillard reaction
    • Fu MX, Wells-Knecht KJ, Blackledge JA, Lions TJ, Thorpe SR, Baynes JW. Glycation glycoxidation and crosslinking of collagen by glucose: kinetics, mechanisms and inhibition of late stages of the Maillard reaction. Diabetes 1994;43:676-683.
    • (1994) Diabetes , vol.43 , pp. 676-683
    • Fu, M.X.1    Wells-Knecht, K.J.2    Blackledge, J.A.3    Lions, T.J.4    Thorpe, S.R.5    Baynes, J.W.6
  • 17
    • 0024407936 scopus 로고
    • Oxidation of glycated proteins: Age dependet accumulation of N-(carboximethyl) lysine in lens proteins
    • Dunn JA, Patrick JS, Thorpe SR, Baynes JW. Oxidation of glycated proteins: age dependet accumulation of N-(carboximethyl) lysine in lens proteins. Biochemistry 1990;28:9464-9468.
    • (1990) Biochemistry , vol.28 , pp. 9464-9468
    • Dunn, J.A.1    Patrick, J.S.2    Thorpe, S.R.3    Baynes, J.W.4
  • 18
    • 0025948114 scopus 로고
    • Mechanism of formation of the Maillard protein crosslink pentosidine. Glucose, fructose and ascorbate as pentosidine precursors
    • Grandhee SK, Monnier VM. Mechanism of formation of the Maillard protein crosslink pentosidine. Glucose, fructose and ascorbate as pentosidine precursors. J Biol Chem 1991; 266:11649-11653.
    • (1991) J Biol Chem , vol.266 , pp. 11649-11653
    • Grandhee, S.K.1    Monnier, V.M.2
  • 19
    • 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 DG, Blackledge JA, Thorpe SR, Baynes JW. 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. 1991;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
  • 21
    • 0016181316 scopus 로고
    • Altered rate of DNA replication in aging human fibrolblast cultures
    • Petes TD, Farber RA, Tarrant GM, Holliday R. Altered rate of DNA replication in aging human fibrolblast cultures. Nature 1974;251:434-436.
    • (1974) Nature , vol.251 , pp. 434-436
    • Petes, T.D.1    Farber, R.A.2    Tarrant, G.M.3    Holliday, R.4
  • 22
    • 0002695343 scopus 로고
    • Nonenzymatic glycosylation and browning of proteins in vivo
    • American Chemical Society Symposium Series No.215 Washington DC, The American Chemical Society
    • Monier VM, Cerami A. Nonenzymatic glycosylation and browning of proteins in vivo. En: Maillard reaction in foods and nutrition. American Chemical Society Symposium Series No.215 Washington DC, The American Chemical Society 1983. pp 431-439.
    • (1983) Maillard Reaction in Foods and Nutrition , pp. 431-439
    • Monier, V.M.1    Cerami, A.2
  • 24
    • 0002695343 scopus 로고
    • Nonenzymatic glycosylation and browning of proteins in vivo
    • Waller GR, Feather MS (Eds.) American Chemical Society Symposium Series No.215. The American Chemical Society. Washington DC
    • Monier VM, Cerami A. Nonenzymatic glycosylation and browning of proteins in vivo. In: The Maillard reaction in foods and nutrition. Waller GR, Feather MS (Eds.) American Chemical Society Symposium Series No.215. The American Chemical Society. Washington DC. 1983, pp 431-439.
    • (1983) The Maillard Reaction in Foods and Nutrition , pp. 431-439
    • Monier, V.M.1    Cerami, A.2
  • 25
    • 0019870473 scopus 로고
    • Kinetic analysis of the nonenzymatic glucosylation of hemoglobin
    • Higgins PJ, Bunn HF. Kinetic analysis of the nonenzymatic glucosylation of hemoglobin. J Biol Chem. 1981;256:5204-5208.
    • (1981) J Biol Chem , vol.256 , pp. 5204-5208
    • Higgins, P.J.1    Bunn, H.F.2
  • 26
    • 84966155688 scopus 로고
    • Nonenzymatic glycation of collagen in aging and diabetes
    • Reser KM. Nonenzymatic glycation of collagen in aging and diabetes. Exp Biol Med. 1991;196(1):17-29.
    • (1991) Exp Biol Med , vol.196 , Issue.1 , pp. 17-29
    • Reser, K.M.1
  • 27
    • 0025174842 scopus 로고
    • End-stage renal disease and diabetes catalyzed deformation of a pentose-derived crosslink from aging human collagen
    • Sell DR, Monier UV. End - stage renal disease and diabetes catalyzed deformation of a pentose-derived crosslink from aging human collagen.J Clin Invest. 1990;75:380-384.
    • (1990) J Clin Invest , vol.75 , pp. 380-384
    • Sell, D.R.1    Monier, U.V.2
  • 28
    • 0028469809 scopus 로고
    • Recent progress on the biologic and clinical significance of advanced glycosylation end products
    • Vlassara H. Recent progress on the biologic and clinical significance of advanced glycosylation end products. J Lab Clin Med. 1994;19-30.
    • (1994) J Lab Clin Med , pp. 19-30
    • Vlassara, H.1
  • 29
    • 0001772040 scopus 로고    scopus 로고
    • Glycation and advanced glycation endproducts
    • Colaco C (Ed.) Landes Bioscience and Chapman & Hall. New York, USA
    • Westwood ME, Thornalley PJ. Glycation and advanced glycation endproducts. In: The Glycation Hypotesis of Atherosclerosis. Colaco C (Ed.) Landes Bioscience and Chapman & Hall. New York, USA 1997, pp 57-87.
    • (1997) The Glycation Hypotesis of Atherosclerosis , pp. 57-87
    • Westwood, M.E.1    Thornalley, P.J.2
  • 30
    • 0032563120 scopus 로고    scopus 로고
    • Role of the Maillard reaction in aging of tissue proteins
    • Brinkmann EB, Dehenhard TP, Thorpe SR, Baynes JW. Role of the Maillard reaction in aging of tissue proteins. J Biol Chem 1998;273(30):18714-18719.
    • (1998) J Biol Chem , vol.273 , Issue.30 , pp. 18714-18719
    • Brinkmann, E.B.1    Dehenhard, T.P.2    Thorpe, S.R.3    Baynes, J.W.4
  • 31
    • 0001112738 scopus 로고
    • Aging of proteins: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose
    • Pongor S, Ulrich PC, Bencsath A, Cerami A. Aging of proteins: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. Biochemistry 1984;81:2684-2688.
    • (1984) Biochemistry , vol.81 , pp. 2684-2688
    • Pongor, S.1    Ulrich, P.C.2    Bencsath, A.3    Cerami, A.4
  • 32
    • 0031577293 scopus 로고    scopus 로고
    • Immunohistochemical localization of advanced glycation end products, pentosidine and carboxymethyllysine in lipofucsin pigments of Alzheimer's disease and aged neurons
    • Miyata HK, Yasuda T, Takeda A, Yasuda Y, Maeda K, Sobue G, Kurokawa K. Immunohistochemical localization of advanced glycation end products, pentosidine and carboxymethyllysine in lipofucsin pigments of Alzheimer's disease and aged neurons, Biochem Biophys Res Commun. 1997;236:327-332.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 327-332
    • Miyata, H.K.1    Yasuda, T.2    Takeda, A.3    Yasuda, Y.4    Maeda, K.5    Sobue, G.6    Kurokawa, K.7
  • 33
    • 0027956982 scopus 로고
    • Modification of low density lipoprotein by advanced glycation end products contributes to dyslipidemia of diabetes and renal insufficiency
    • Bucala R, Makita Z, Vega G, Grundy S, Koschinsky T, Cerami A. Vlassara H. Modification of low density lipoprotein by advanced glycation end products contributes to dyslipidemia of diabetes and renal insufficiency. Proc Natl Acad Sci USA 1994;91:9441-9445.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9441-9445
    • Bucala, R.1    Makita, Z.2    Vega, G.3    Grundy, S.4    Koschinsky, T.5    Cerami, A.6    Vlassara, H.7
  • 35
    • 0026625832 scopus 로고
    • Aminoguanidine inhibits oxidative modification of low density lipoprotein and the subsequent increase in uptake by macrophage scavenger receptors
    • Picard S, Parthasathy S, Fruebis J, Witztum JL. Aminoguanidine inhibits oxidative modification of low density lipoprotein and the subsequent increase in uptake by macrophage scavenger receptors. Proc Natl Acad. Sci USA 1991; 89:6876-6880.
    • (1991) Proc Natl Acad Sci USA , vol.89 , pp. 6876-6880
    • Picard, S.1    Parthasathy, S.2    Fruebis, J.3    Witztum, J.L.4
  • 36
    • 0000571086 scopus 로고
    • Modifications of DNA by reducing sugars: A possible mechanism for nucleic acid aging and age-related dysfunction in gene expression
    • Bucala R, Model P, Cerami A. Modifications of DNA by reducing sugars: a possible mechanism for nucleic acid aging and age-related dysfunction in gene expression. Proc Natl Acad Sci USA 1984;81:105-109.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 105-109
    • Bucala, R.1    Model, P.2    Cerami, A.3
  • 37
    • 0015211336 scopus 로고
    • Age-associated changes in the DNA of mouse tissue
    • Price GB, Modak SP, Makinodan T. Age-associated changes in the DNA of mouse tissue. Science 1971;171:917-920.
    • (1971) Science , vol.171 , pp. 917-920
    • Price, G.B.1    Modak, S.P.2    Makinodan, T.3
  • 38
    • 0000746938 scopus 로고    scopus 로고
    • Cell activation by glycated proteins. Age receptors, receptor recognition factors and functional classification of AGEs
    • Thornalley PJ. Cell activation by glycated proteins. Age receptors, receptor recognition factors and functional classification of AGEs. Cell Mol Biol 1998;44(7):1013-1023.
    • (1998) Cell Mol Biol , vol.44 , Issue.7 , pp. 1013-1023
    • Thornalley, P.J.1
  • 39
    • 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, Brownlee M, Cerami A. 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 1985;82:5588-5592.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 5588-5592
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 40
    • 0029088742 scopus 로고
    • Advanced glycation end products interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM) in cultured human endothelial cells in mice
    • Schmidt A-M, Hori M, Chen JX, Li JF Carndall J, Zjang J, Cao R, Yan DS, Brett J, Stern D. Advanced glycation end products interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM) in cultured human endothelial cells in mice. J Clin Invest 1995; 96:1395-1403.
    • (1995) J Clin Invest , vol.96 , pp. 1395-1403
    • Schmidt, A.-M.1    Hori, M.2    Chen, J.X.3    Li, J.F.4    Carndall, J.5    Zjang, J.6    Cao, R.7    Yan, D.S.8    Brett, J.9    Stern, D.10
  • 41
    • 0030273623 scopus 로고    scopus 로고
    • Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human serum albumin derivatives modified with methyl glyoxal and glucose-derived advanced glucose endproducts
    • Abordo EA, Westwood ME, Thornalley PJ. Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human serum albumin derivatives modified with methyl glyoxal and glucose-derived advanced glucose endproducts. Immunol Lett 1996;53:7-13.
    • (1996) Immunol Lett , vol.53 , pp. 7-13
    • Abordo, E.A.1    Westwood, M.E.2    Thornalley, P.J.3
  • 42
    • 0025203319 scopus 로고
    • Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of PDGF: Role in vascular disease of diabetes and aging
    • Kirstein M, Brett J, Radoff S Ogawa S, Stern D, Vlassara H. Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of PDGF: role in vascular disease of diabetes and aging. Proc Natl Acad Sci USA 1990;87:9010-9014.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9010-9014
    • Kirstein, M.1    Brett, J.2    Radoff, S.3    Ogawa, S.4    Stern, D.5    Vlassara, H.6
  • 44
    • 0025892834 scopus 로고
    • Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts
    • Lyons TJ, Silvestri G, Dunn DG, Baynes JW. Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes 1991;40:1010-105.
    • (1991) Diabetes , vol.40 , pp. 1010-1105
    • Lyons, T.J.1    Silvestri, G.2    Dunn, D.G.3    Baynes, J.W.4
  • 45
    • 0027049697 scopus 로고
    • Exogenous advanced glycosylation endproducts induce complex vascular dysfunction in normal animals: A model for diabetic and aging complications
    • Vlassara H, Fuh H, Makita Z, Krungkrai S, Cerami A, Bucala R. Exogenous advanced glycosylation endproducts induce complex vascular dysfunction in normal animals: A model for diabetic and aging complications. Proc Natl Acad Sci USA 1992;89:12043-12047.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12043-12047
    • Vlassara, H.1    Fuh, H.2    Makita, Z.3    Krungkrai, S.4    Cerami, A.5    Bucala, R.6
  • 46
    • 0027161984 scopus 로고
    • b2-microglobulin modified with advanced glycation endproducts is a major component of haemodialysis-associated amyloidosis
    • Miyata T, Oda O, Inagi R, Lida Y, Araki N, Yamada N, Horiuchi S, Taniguchi N, Maeda K. b2-Microglobulin modified with advanced glycation endproducts is a major component of haemodialysis-associated amyloidosis. J Clin Invest 1993;92:1242-1252.
    • (1993) J Clin Invest , vol.92 , pp. 1242-1252
    • Miyata, T.1    Oda, O.2    Inagi, R.3    Lida, Y.4    Araki, N.5    Yamada, N.6    Horiuchi, S.7    Taniguchi, N.8    Maeda, K.9
  • 47
    • 0028233384 scopus 로고
    • The endothelial binding site for advanced glycation endproducts consist of a complex: An integral membrane protein and a lactoferrin-like polipeptide
    • Schmidt A-M, Mora R, Cao R, Yan S-D Brett J, Ramakrishnan R, Tsang TE, Simonescu M, Stern D. The endothelial binding site for advanced glycation endproducts consist of a complex: An integral membrane protein and a lactoferrin-like polipeptide. J Biol Chem 1994;269:9882-9888.
    • (1994) J Biol Chem , vol.269 , pp. 9882-9888
    • Schmidt, A.-M.1    Mora, R.2    Cao, R.3    Yan, S.-D.4    Brett, J.5    Ramakrishnan, R.6    Tsang, T.E.7    Simonescu, M.8    Stern, D.9
  • 51
    • 0033551042 scopus 로고    scopus 로고
    • Amadorins: Novel post-Amadori inhibitors of advanced glycation reactions
    • Khalifah RG, Baynes JW, Hudson BG. Amadorins: Novel post-Amadori inhibitors of advanced glycation reactions. Biochem Biophys Res Commun 1999;257:251-258.
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 251-258
    • Khalifah, R.G.1    Baynes, J.W.2    Hudson, B.G.3


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