메뉴 건너뛰기




Volumn 27, Issue 2, 1997, Pages 97-108

Advanced glycation end products, oxidant stress and vascular lesions

Author keywords

atherosclerosis; endothelial cells; glycation; monocytes; oxidant stress

Indexed keywords

ATHEROSCLEROSIS; DIABETES MELLITUS; DIABETIC NEPHROPATHY; DIABETIC RETINOPATHY; GLYCATION; HUMAN; OXIDATION; PRIORITY JOURNAL; REVIEW; STRESS; VASCULAR LESION;

EID: 0031048334     PISSN: 00142972     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2362.1997.710624.x     Document Type: Review
Times cited : (214)

References (107)
  • 1
    • 0028321899 scopus 로고
    • Cellular and molecular abnormalities in the vascular endothelium of diabetes mellitus
    • King GL, Shiba T, Oliver J, Inoguchi T, Bursell SE. Cellular and molecular abnormalities in the vascular endothelium of diabetes mellitus. Annu Rev Med 1994;45:179-88.
    • (1994) Annu Rev Med , vol.45 , pp. 179-188
    • King, G.L.1    Shiba, T.2    Oliver, J.3    Inoguchi, T.4    Bursell, S.E.5
  • 2
    • 0019796775 scopus 로고
    • Reaction of monosaccharides with proteins: Possible evolutionary significance
    • Bunn HF, Higgins PJ. Reaction of monosaccharides with proteins: possible evolutionary significance. Science 1981;213:222-4.
    • (1981) Science , vol.213 , pp. 222-224
    • Bunn, H.F.1    Higgins, P.J.2
  • 3
    • 0026505107 scopus 로고
    • Detection of 3-deoxyfructose and 3-deoxyglycanosone in human urine and plasma: Evidence for intermediate stages of Maillard reaction in vivo
    • Knecht KG, Feather MS, Baynes JW. Detection of 3-deoxyfructose and 3-deoxyglycanosone in human urine and plasma: evidence for intermediate stages of Maillard reaction in vivo. Arch Biochem Biophys 1992;294:130-1.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 130-131
    • Knecht, K.G.1    Feather, M.S.2    Baynes, J.W.3
  • 4
    • 0026782087 scopus 로고
    • Role of oxygen in cross linking and chemical modification of collagen by glucose
    • Fu MX, Knecht KJ, Thorpe R et al. Role of oxygen in cross linking and chemical modification of collagen by glucose. Diabetes 1992;41:42-8.
    • (1992) Diabetes , vol.41 , pp. 42-48
    • Fu, M.X.1    Knecht, K.J.2    Thorpe, R.3
  • 5
    • 0027255884 scopus 로고
    • Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation
    • Hunt JV, Bottoms MA, Mitchinson MJ. Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Biochem J 1993;291:529-35.
    • (1993) Biochem J , vol.291 , pp. 529-535
    • Hunt, J.V.1    Bottoms, M.A.2    Mitchinson, M.J.3
  • 6
    • 0000916315 scopus 로고
    • Action des acides aminés sur les sucres. Formation des mélanoïds par voie méthodique
    • France
    • Maillard LC. Action des acides aminés sur les sucres. Formation des mélanoïds par voie méthodique. Compte Rendu Acad Sci (France), 1952;154:66-8.
    • (1952) Compte Rendu Acad Sci , vol.154 , pp. 66-68
    • Maillard, L.C.1
  • 7
    • 0023708392 scopus 로고
    • Hydroxy radical production and antioxidative glycosylation: Glucosyl autooxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing
    • Hunt JV, Dean RT, Wolf SP. Hydroxy radical production and antioxidative glycosylation: glucosyl autooxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing. Biochemistry 1988;256:205-12.
    • (1988) Biochemistry , vol.256 , pp. 205-212
    • Hunt, J.V.1    Dean, R.T.2    Wolf, S.P.3
  • 8
    • 0022931516 scopus 로고
    • Identification of W-carboxymethyl-lysine as a degradation product of fructoselysine in glycated protein
    • Ahmed MU, Thorpe SR, Baynes JW. Identification of W-carboxymethyl-lysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 1986;261:4889-94.
    • (1986) J Biol Chem , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 9
    • 0001112738 scopus 로고
    • Aging of proteins: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose
    • Tongor S, Ulrich PC, Bencsath FA, Cerami A. Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. Proc Natl Acad Sci USA 1984;81:2684-8.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2684-2688
    • Tongor, S.1    Ulrich, P.C.2    Bencsath, F.A.3    Cerami, A.4
  • 10
    • 0029066992 scopus 로고
    • Immunological evidence for the presence of advanced glycosylation end products in atherosclerotic lesions of englycemic rabbits
    • Palinski W, Koschinsky T, Butler SW et al. Immunological evidence for the presence of advanced glycosylation end products in atherosclerotic lesions of englycemic rabbits. Arterioscl Thromb Vasc Biol 1995;15:571-82.
    • (1995) Arterioscl Thromb Vasc Biol , vol.15 , pp. 571-582
    • Palinski, W.1    Koschinsky, T.2    Butler, S.W.3
  • 11
    • 0001090605 scopus 로고
    • Novel pyrroles from sulfite-inhibited Maillard reactions: Insight into the mechanism of inhibition
    • Famar J, Ulrich P, Cerami A. Novel pyrroles from sulfite-inhibited Maillard reactions: insight into the mechanism of inhibition. J Org Chem, 1988;53:2346-9.
    • (1988) J Org Chem , vol.53 , pp. 2346-2349
    • Famar, J.1    Ulrich, P.2    Cerami, A.3
  • 12
    • 0023780475 scopus 로고
    • Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furayl)-4(5)-(2-furamyl)-1H-imidazole
    • Nsoroge FG, Fernandes AA, Monnier VM. Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furayl)-4(5)-(2-furamyl)-1H-imidazole. J Biol Chem 1988;263:10646-52.
    • (1988) J Biol Chem , vol.263 , pp. 10646-10652
    • Nsoroge, F.G.1    Fernandes, A.A.2    Monnier, V.M.3
  • 13
    • 0026703158 scopus 로고
    • Immunochemical detection of advanced glycosylation end products in vivo
    • Makita Z, Vlassara H, Cerami A, Bucala R. Immunochemical detection of advanced glycosylation end products in vivo. J Biol Chem 1992;267:5133-8.
    • (1992) J Biol Chem , vol.267 , pp. 5133-5138
    • Makita, Z.1    Vlassara, H.2    Cerami, A.3    Bucala, R.4
  • 14
    • 0028988415 scopus 로고
    • 2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation end product
    • 2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation end product. Biochemistry 1995;34:648-55.
    • (1995) Biochemistry , vol.34 , pp. 648-655
    • Papoulis, A.1    Youssef, A.A.2    Bucala, R.3
  • 15
    • 0022644227 scopus 로고
    • Aminoguanidine prevents diabetes-induced arterial wall protein cross linking
    • Brownlee M, Vlassara H, Kooney T, Ulrich P, Cerami A. Aminoguanidine prevents diabetes-induced arterial wall protein cross linking. Science 1986;232:1629-32.
    • (1986) Science , vol.232 , pp. 1629-1632
    • Brownlee, M.1    Vlassara, H.2    Kooney, T.3    Ulrich, P.4    Cerami, A.5
  • 16
    • 21144460354 scopus 로고
    • Mechanism of inhibition of advanced glycosylation by aminoguanidine in vitro
    • Chen HJ, Cerami A. Mechanism of inhibition of advanced glycosylation by aminoguanidine in vitro. J Carbohydr Chem 1993;12:731-42.
    • (1993) J Carbohydr Chem , vol.12 , pp. 731-742
    • Chen, H.J.1    Cerami, A.2
  • 17
    • 0026641944 scopus 로고
    • Aminoguanidine, a novel inhibition of nitric oxide formation, prevents diabetic vascular dysfunctions
    • Corbett JA, Tilton RG, Chang K et al. Aminoguanidine, a novel inhibition of nitric oxide formation, prevents diabetic vascular dysfunctions. Diabetes 1992;41:552-6.
    • (1992) Diabetes , vol.41 , pp. 552-556
    • Corbett, J.A.1    Tilton, R.G.2    Chang, K.3
  • 18
    • 0026679217 scopus 로고
    • Polyclonal immunoglobulin M: Location of glycation sites
    • Menni T, Gugliucci A, Stahl AJC. Polyclonal immunoglobulin M: location of glycation sites. Clin Chim Acta 1992;213:23-35.
    • (1992) Clin Chim Acta , vol.213 , pp. 23-35
    • Menni, T.1    Gugliucci, A.2    Stahl, A.J.C.3
  • 19
    • 0023588968 scopus 로고
    • Glycated proteins in serum: Effect of their relative proportions on their alkaline reducing activity in the fructosomine test
    • Zoppe F, Mosca A, Granata S, Montalbetti N. Glycated proteins in serum: effect of their relative proportions on their alkaline reducing activity in the fructosomine test. Clin Chem 1987; 33:1895-7.
    • (1987) Clin Chem , vol.33 , pp. 1895-1897
    • Zoppe, F.1    Mosca, A.2    Granata, S.3    Montalbetti, N.4
  • 20
    • 0023009324 scopus 로고
    • Non enzymatic glycosylation of albumin in vivo
    • Iberg N, Fluciger R. Non enzymatic glycosylation of albumin in vivo. J Biol Chem 1986;261:13542-5.
    • (1986) J Biol Chem , vol.261 , pp. 13542-13545
    • Iberg, N.1    Fluciger, R.2
  • 21
    • 0347756978 scopus 로고
    • Micropinocytic ingestion of glycosylated albumin by isolated microvessels: Possible role in pathogenesis of diabetic microangiopathy
    • Williams SK, Devenny JJ, Bitensky MW. Micropinocytic ingestion of glycosylated albumin by isolated microvessels: possible role in pathogenesis of diabetic microangiopathy. Proc Natl Acad Sci USA 1981;78:2393-9.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2393-2399
    • Williams, S.K.1    Devenny, J.J.2    Bitensky, M.W.3
  • 22
    • 0022021067 scopus 로고
    • Evidence for non-enzymatic glycation of antithrombin III in diabetic patients
    • Ducrocq R, Bachour M, Belkhodja R et al. Evidence for non-enzymatic glycation of antithrombin III in diabetic patients. Clin Chem 1985;31:338-9.
    • (1985) Clin Chem , vol.31 , pp. 338-339
    • Ducrocq, R.1    Bachour, M.2    Belkhodja, R.3
  • 23
    • 0020789178 scopus 로고
    • Non enzymatic glycosylation reduces the susceptibility of fibrine to degradation by plasmin
    • Brownlee M, Vlassara H, Cerami A. Non enzymatic glycosylation reduces the susceptibility of fibrine to degradation by plasmin. Diabetes 1983;32:680-4.
    • (1983) Diabetes , vol.32 , pp. 680-684
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 24
    • 0018701795 scopus 로고
    • Altered metabolism (in vivo and in vitro) of plasma lipoproteins after selective chemical modification of lysine residues of the apoprotein B
    • Mahley RW, Innerarity TL, Weisgraber KH, Oh SY. Altered metabolism (in vivo and in vitro) of plasma lipoproteins after selective chemical modification of lysine residues of the apoprotein B. J Clin Invest 1979;64:743-50.
    • (1979) J Clin Invest , vol.64 , pp. 743-750
    • Mahley, R.W.1    Innerarity, T.L.2    Weisgraber, K.H.3    Oh, S.Y.4
  • 26
    • 0021363569 scopus 로고
    • Glycosylation of low-density lipoproteins on a extent comparable to that seen in diabetes shows their catabolism
    • Steinbrecher U, Witztum JL. Glycosylation of low-density lipoproteins on a extent comparable to that seen in diabetes shows their catabolism. Diabetes 1984;33:130-4.
    • (1984) Diabetes , vol.33 , pp. 130-134
    • Steinbrecher, U.1    Witztum, J.L.2
  • 27
    • 0026602073 scopus 로고
    • Oxidation of low density lipoprotein leads to particle aggregation and altered macrophage recognition
    • Hoff HF, Whitaker TE, O'Neil J. Oxidation of low density lipoprotein leads to particle aggregation and altered macrophage recognition. J Biol Chem 1992;267:602-9.
    • (1992) J Biol Chem , vol.267 , pp. 602-609
    • Hoff, H.F.1    Whitaker, T.E.2    O'Neil, J.3
  • 28
    • 0020520283 scopus 로고
    • A novel method for generating region specific monoclonal antibodies to modify proteins: Application to the identification of human glycosylated low density lipoproteins
    • Curtiss LK, Witztum JL. A novel method for generating region specific monoclonal antibodies to modify proteins: application to the identification of human glycosylated low density lipoproteins. J Clin Invest 1983;72:1427-38.
    • (1983) J Clin Invest , vol.72 , pp. 1427-1438
    • Curtiss, L.K.1    Witztum, J.L.2
  • 29
    • 1842338516 scopus 로고
    • Autoantibodies to glycosylated proteins in the plasma of patients with diabetes mellitus
    • Witzum JL, Steinbrecher UP, Kesaniemiy A et al. Autoantibodies to glycosylated proteins in the plasma of patients with diabetes mellitus. Proc Natl Acad Sci USA 1984;81:3204-8.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3204-3208
    • Witzum, J.L.1    Steinbrecher, U.P.2    Kesaniemiy, A.3
  • 30
    • 0026013131 scopus 로고
    • Non-enzymatic glycosylation of HDL and impaired HDL-receptor-mediated cholesterol efflux
    • Dueil PB, Oram JF, Bierman EL. Non-enzymatic glycosylation of HDL and impaired HDL-receptor-mediated cholesterol efflux. Diabetes 1991;40:377-84.
    • (1991) Diabetes , vol.40 , pp. 377-384
    • Dueil, P.B.1    Oram, J.F.2    Bierman, E.L.3
  • 31
    • 0022600445 scopus 로고
    • Metabolism of glycosylated very-low-density lipoproteins in human skin tibroblasts
    • Yamamoto M, Ranganathan S, Koitke A. Metabolism of glycosylated very-low-density lipoproteins in human skin tibroblasts. Biochem Biophys Acta 1986;875:410-13.
    • (1986) Biochem Biophys Acta , vol.875 , pp. 410-413
    • Yamamoto, M.1    Ranganathan, S.2    Koitke, A.3
  • 32
    • 0018777393 scopus 로고
    • Activation of lipoprotein lipase hyperactive and acetylated peptide of apo-CII
    • Musliner TA, Herbert PN, Church EC. Activation of lipoprotein lipase hyperactive and acetylated peptide of apo-CII. Biochim Biophys Acta 1979;573:501-9.
    • (1979) Biochim Biophys Acta , vol.573 , pp. 501-509
    • Musliner, T.A.1    Herbert, P.N.2    Church, E.C.3
  • 33
    • 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;82:5588-92.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 5588-5592
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 34
    • 0025313580 scopus 로고
    • Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate
    • Gilcrease MZ, Hoover RL. Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate. Diabetologia 1990;33:329-33.
    • (1990) Diabetologia , vol.33 , pp. 329-333
    • Gilcrease, M.Z.1    Hoover, R.L.2
  • 35
    • 0027420670 scopus 로고
    • Advanced glycosylation end product-specific receptors on human and rat T-lymphocytes mediates synthesis of interferon gamma: Role in tissue remodeling
    • Imani F, Horii Y, Suthanthiran M et al. Advanced glycosylation end product-specific receptors on human and rat T-lymphocytes mediates synthesis of interferon gamma: role in tissue remodeling. J Exp Med 1993;178:2165-72.
    • (1993) J Exp Med , vol.178 , pp. 2165-2172
    • Imani, F.1    Horii, Y.2    Suthanthiran, M.3
  • 36
    • 0023922126 scopus 로고
    • Characterization of a solubilized cell surface binding protein on macrophages specific for proteins modified non-enzymatically by advanced glycosylation endproducts
    • Radoff S, Vlassara H, Cerami A. Characterization of a solubilized cell surface binding protein on macrophages specific for proteins modified non-enzymatically by advanced glycosylation endproducts. Arch Biochem Biophys 1988;263:418-23.
    • (1988) Arch Biochem Biophys , vol.263 , pp. 418-423
    • Radoff, S.1    Vlassara, H.2    Cerami, A.3
  • 37
    • 0025787479 scopus 로고
    • Two novel rat liver membrane proteins that bind advanced glycosylation enproducts: Relationship to macrophage receptor glucose-modified proteins
    • Yang Z, Makita Z, Horii Y et al. Two novel rat liver membrane proteins that bind advanced glycosylation enproducts: relationship to macrophage receptor glucose-modified proteins. J Exp Med 1991;174:515-4.
    • (1991) J Exp Med , vol.174 , pp. 515-524
    • Yang, Z.1    Makita, Z.2    Horii, Y.3
  • 38
    • 0026042328 scopus 로고
    • Human and rat mesangial cell receptors for glucose-modified proteins: Potential role in kidney tissue remodeling and diabetic nephropathy
    • Skolnik EY, Yang Z, Makita Z, Radoff S, Kirstein M, Vlassara H. Human and rat mesangial cell receptors for glucose-modified proteins: potential role in kidney tissue remodeling and diabetic nephropathy. J Exp Med 1991;174:931-9.
    • (1991) J Exp Med , vol.174 , pp. 931-939
    • Skolnik, E.Y.1    Yang, Z.2    Makita, Z.3    Radoff, S.4    Kirstein, M.5    Vlassara, H.6
  • 39
    • 0026650438 scopus 로고
    • Isolation and characterization of binding proteins for advanced glycosylation endproducts from lung tissue which are present on the endothelial cell surface
    • Schmidt AM, Vianna M, Gerlach M et al. Isolation and characterization of binding proteins for advanced glycosylation endproducts from lung tissue which are present on the endothelial cell surface. J Biol Chem 1992;267:14987-97.
    • (1992) J Biol Chem , vol.267 , pp. 14987-14997
    • Schmidt, A.M.1    Vianna, M.2    Gerlach, M.3
  • 40
    • 0028233384 scopus 로고
    • The endothelial cell binding site for advanced glycation end products consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide
    • Schmidt AM, Mora R, Cao R et al. The endothelial cell binding site for advanced glycation end products consists of a complex: an integral membrane protein and a lactoferrin-like polypeptide. J Biol Chem 1994;269:9882-8.
    • (1994) J Biol Chem , vol.269 , pp. 9882-9888
    • Schmidt, A.M.1    Mora, R.2    Cao, R.3
  • 41
    • 0026659883 scopus 로고
    • Cloning expression of RAGE: A cell surface receptor for advanced glycosylation endproducts of proteins
    • Neeper M, Schmidt AM, Brett J et al. Cloning expression of RAGE: a cell surface receptor for advanced glycosylation endproducts of proteins. J Biol Chem 1992;267:14998-15004.
    • (1992) J Biol Chem , vol.267 , pp. 14998-15004
    • Neeper, M.1    Schmidt, A.M.2    Brett, J.3
  • 42
    • 0027957087 scopus 로고
    • Three genes in the human MHC class III region near the junction with the class II: Gene for receptor of advanced glycosylation endproducts, BPX2 homeobox gene and a Notch homolog, human counterpart of mouse mammary tumor gene int-3
    • Sugaya K, Fukagawa T, Matsumoto KI et al. Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation endproducts, BPX2 homeobox gene and a Notch homolog, human counterpart of mouse mammary tumor gene int-3. Genomics 1994;23:408-19.
    • (1994) Genomics , vol.23 , pp. 408-419
    • Sugaya, K.1    Fukagawa, T.2    Matsumoto, K.I.3
  • 43
    • 0028851635 scopus 로고
    • The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin
    • Hori O, Brett J, Slattery T et al. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. J Biol Chem 1995;270:25752-61.
    • (1995) J Biol Chem , vol.270 , pp. 25752-25761
    • Hori, O.1    Brett, J.2    Slattery, T.3
  • 44
    • 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 AM, Hori O, Brett J, Yan SD, Wautier JL, Stern D. Cellular receptors for advanced glycation end products. Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions. Arterioscler Thromb 1994; 14:1521-8.
    • (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
  • 45
    • 0028875176 scopus 로고
    • Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycatin-modified proteins to a conserved motif
    • Ming, Li YX, Tan A, Vlassara H. Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycatin-modified proteins to a conserved motif. Nature Med 1995;10:1057-61.
    • (1995) Nature Med , vol.10 , pp. 1057-1061
    • Ming1    Li, Y.X.2    Tan, A.3    Vlassara, H.4
  • 46
    • 0018424962 scopus 로고
    • Structural heterogeneity of human hemoglobin A due to nonenzymatic glycosylation
    • Bunn HF, Shapiro R, McManus M et al. Structural heterogeneity of human hemoglobin A due to nonenzymatic glycosylation. J Biol Chem 1979;254:3892-8.
    • (1979) J Biol Chem , vol.254 , pp. 3892-3898
    • Bunn, H.F.1    Shapiro, R.2    McManus, M.3
  • 47
    • 0018138073 scopus 로고
    • Glycosylated minor components of human adult hemoglobin
    • McDonald MJ, Shapiro R, Bleichman M et al. Glycosylated minor components of human adult hemoglobin. J Biol Chem 1978;253:2327-32.
    • (1978) J Biol Chem , vol.253 , pp. 2327-2332
    • McDonald, M.J.1    Shapiro, R.2    Bleichman, M.3
  • 48
    • 0023591735 scopus 로고
    • Enzymatic glycation may decrease activity of erythrocyte S-aminolevulinate dehydratase in diabetes mellitus
    • Ratnaikes S, Blake D, Shevenan P, Enzymatic glycation may decrease activity of erythrocyte S-aminolevulinate dehydratase in diabetes mellitus. Clin Chem 1987;33:1807-10.
    • (1987) Clin Chem , vol.33 , pp. 1807-1810
    • Ratnaikes, S.1    Blake, D.2    Shevenan, P.3
  • 49
    • 0021916065 scopus 로고
    • Non enzymatic glycosylation of erythrocytic proteins in normal and diabetic subjects, enzyme of nucleoside and nucleotide metabolism
    • Argawak KC, Parks RE, Widenss JA et al. Non enzymatic glycosylation of erythrocytic proteins in normal and diabetic subjects, enzyme of nucleoside and nucleotide metabolism. Diabetes 1985;34:251-5.
    • (1985) Diabetes , vol.34 , pp. 251-255
    • Argawak, K.C.1    Parks, R.E.2    Widenss, J.A.3
  • 50
    • 0018843839 scopus 로고
    • Nonenzymatic glycosylation of erythrocyte membrane proteins: Relevance to diabetes
    • Miller JA, Gravallese E, Bunn HF. Nonenzymatic glycosylation of erythrocyte 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
  • 51
    • 0023835005 scopus 로고
    • Association between glycation of erythrocyte membrane proteins and membrane fluidity
    • Bryszewska M, Szosland K. Association between glycation of erythrocyte membrane proteins and membrane fluidity. Ann Clin Res 1988;21:49-51.
    • (1988) Ann Clin Res , vol.21 , pp. 49-51
    • Bryszewska, M.1    Szosland, K.2
  • 52
    • 0022337950 scopus 로고
    • Nonenzymatic protien glycosylation I. Lowered erythrocyte membrane fluidity in juvenile diabetes
    • Watala C, Zawodniak M, Bryszewska M, Novak S. Nonenzymatic protien glycosylation I. Lowered erythrocyte membrane fluidity in juvenile diabetes. Ann Clin Res 1985;17:327-30.
    • (1985) Ann Clin Res , vol.17 , pp. 327-330
    • Watala, C.1    Zawodniak, M.2    Bryszewska, M.3    Novak, S.4
  • 53
    • 0018160553 scopus 로고
    • Reduced erythrocyte deformability in diabetes
    • McMillan DE, Utterback NG, La Puma J. Reduced erythrocyte deformability in diabetes. Diabetes 1978;27:895-901.
    • (1978) Diabetes , vol.27 , pp. 895-901
    • McMillan, D.E.1    Utterback, N.G.2    La Puma, J.3
  • 54
    • 0023681418 scopus 로고
    • Correlation between 4.1a/4.1b ratio and erythrocyte life span
    • Inaba M, Maede Y. Correlation between 4.1a/4.1b ratio and erythrocyte life span. Biochem Biophys Acta 1988;944:256-64.
    • (1988) Biochem Biophys Acta , vol.944 , pp. 256-264
    • Inaba, M.1    Maede, Y.2
  • 55
    • 0019433759 scopus 로고
    • Increased adhesion of erythrocytes to endothelial cells in diabetes mellitus and their relation to the vascular complications
    • Wautier JL, Paton CR, Wautier MP et al. Increased adhesion of erythrocytes to endothelial cells in diabetes mellitus and their relation to the vascular complications. N Engl J Med 1981; 305:237-42.
    • (1981) N Engl J Med , vol.305 , pp. 237-242
    • Wautier, J.L.1    Paton, C.R.2    Wautier, M.P.3
  • 56
    • 0028102075 scopus 로고
    • Advanced glycation end products (AGE) on the surface of diabetic red cells bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: A link between surface-associated AGEs and diabetic complications
    • Wautier JL, Wautier MP, Schmidt AM et al. Advanced glycation end products (AGE) on the surface of diabetic red cells bind to the vessel wall via a specific receptor inducing oxidant stress in the vasculature: a link between surface-associated AGEs and diabetic complications. Proc Natl Acad Sci USA 1994;91:7742-6.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7742-7746
    • Wautier, J.L.1    Wautier, M.P.2    Schmidt, A.M.3
  • 57
    • 0028469809 scopus 로고
    • Recent progress on the biologic and clinical significance of advanced glycation end products
    • Vlassara H. Recent progress on the biologic and clinical significance of advanced glycation end products. J Lab Clin Med 1994;124:19-30.
    • (1994) J Lab Clin Med , vol.124 , pp. 19-30
    • Vlassara, H.1
  • 58
    • 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, Ogana 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; 87:9010-4.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9010-9014
    • Kirstein, M.1    Brett, J.2    Radoff, S.3    Ogana, S.4    Stern, D.5    Vlassara, H.6
  • 59
    • 0027176945 scopus 로고
    • Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products
    • Schmidt AM, Yan SD, Brett J, Mora R, Nowygrod R, Stern D. Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products. J Clin Invest 1993;92:2155-68.
    • (1993) J Clin Invest , vol.92 , pp. 2155-2168
    • Schmidt, A.M.1    Yan, S.D.2    Brett, J.3    Mora, R.4    Nowygrod, R.5    Stern, D.6
  • 60
    • 0027049697 scopus 로고
    • Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: A model for diabetic and aging complications
    • Vlassara H, Fuh H, Makita Z, Krungkari S, Cerami A, Bucala R. Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications. Proc Natl Acad Sci USA 1992; 89: 12043-7.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12043-12047
    • Vlassara, H.1    Fuh, H.2    Makita, Z.3    Krungkari, S.4    Cerami, A.5    Bucala, R.6
  • 61
    • 0023940640 scopus 로고
    • Cachectin/TNF and IL-1 induced by glucose-modified proteins: Role in normal tissue remodeling
    • Vlassara H, Brownlee M, Manogue KR, Dinarello C, Pasagian A. Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science 1988;240:1546-8.
    • (1988) Science , vol.240 , pp. 1546-1548
    • Vlassara, H.1    Brownlee, M.2    Manogue, K.R.3    Dinarello, C.4    Pasagian, A.5
  • 62
    • 0026706273 scopus 로고
    • Receptor specific induction of insulin-like growth factor I (IGF-I) in human monocytes by advanced glycosylation end products-modified proteins
    • Kirstein M, Aston C, Hintz R, Vlassara H. Receptor specific induction of insulin-like growth factor I (IGF-I) in human monocytes by advanced glycosylation end products-modified proteins. J Clin Invest 1992;90:439-46.
    • (1992) J Clin Invest , vol.90 , pp. 439-446
    • Kirstein, M.1    Aston, C.2    Hintz, R.3    Vlassara, H.4
  • 63
    • 0023888611 scopus 로고
    • Specific macrophage receptor activity for advanced glycation end products inversely correlates with insulin levels in vivo
    • Vlassara H, Brownlee M, Cerami A. Specific macrophage receptor activity for advanced glycation end products inversely correlates with insulin levels in vivo. Diabetes 1988;37:456-61.
    • (1988) Diabetes , vol.37 , pp. 456-461
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 64
    • 0024851555 scopus 로고
    • Macrophage/monocyte receptor for non enzymatically glycosylated proteins is up regulated by cachectin/tumor necrosis factor
    • Vlassara H, Moldawer L, Chan B. Macrophage/monocyte receptor for non enzymatically glycosylated proteins is up regulated by cachectin/tumor necrosis factor. J Clin Invest 1989;84:1813-20.
    • (1989) J Clin Invest , vol.84 , pp. 1813-1820
    • Vlassara, H.1    Moldawer, L.2    Chan, B.3
  • 66
    • 0026314785 scopus 로고
    • In vivo platelet activation in diabetes mellitus
    • Strano A, Davi G, Patrono C. In vivo platelet activation in diabetes mellitus. Semin Thromb Hemost 1991;17:422-5.
    • (1991) Semin Thromb Hemost , vol.17 , pp. 422-425
    • Strano, A.1    Davi, G.2    Patrono, C.3
  • 67
    • 0028919426 scopus 로고
    • Expression of receptors for advanced glycation end products in peripheral occlusive vascular disease
    • Ritthaler U, Deng Y, Zhang Y et al. Expression of receptors for advanced glycation end products in peripheral occlusive vascular disease. Am J Pathol 1995;146:688-94.
    • (1995) Am J Pathol , vol.146 , pp. 688-694
    • Ritthaler, U.1    Deng, Y.2    Zhang, Y.3
  • 68
    • 0025966026 scopus 로고
    • Characteristics and mechanisms of high-glucose-induced overexpression of basement membrane components in cultured human endothelial cells
    • Cagliero E, Roth T, Roy S, Lorenzi M. Characteristics and mechanisms of high-glucose-induced overexpression of basement membrane components in cultured human endothelial cells. Diabetes 1991;40:102-10.
    • (1991) Diabetes , vol.40 , pp. 102-110
    • Cagliero, E.1    Roth, T.2    Roy, S.3    Lorenzi, M.4
  • 69
    • 0023950461 scopus 로고
    • Advanced glycation end products in tissue and the biochemical basis of diabetic complication
    • Brownlee M, Cerami A, Vlassara H. Advanced glycation end products in tissue and the biochemical basis of diabetic complication. N Engl J Med 1988;318:1315-21.
    • (1988) N Engl J Med , vol.318 , pp. 1315-1321
    • Brownlee, M.1    Cerami, A.2    Vlassara, H.3
  • 70
    • 11944272384 scopus 로고
    • Glycation products and the pathogenesis of diabetic complications
    • Brownlee M. Glycation products and the pathogenesis of diabetic complications. Diabetes Care 1992;15:1835-43.
    • (1992) Diabetes Care , vol.15 , pp. 1835-1843
    • Brownlee, M.1
  • 71
    • 0025369394 scopus 로고
    • Laminin alterations after in vitro nonenzymatic glycosylation
    • Charonis AS, Reger LA, Dege JE et al. Laminin alterations after in vitro nonenzymatic glycosylation. Diabetes 1990;39:807-14.
    • (1990) Diabetes , vol.39 , pp. 807-814
    • Charonis, A.S.1    Reger, L.A.2    Dege, J.E.3
  • 72
    • 0024502425 scopus 로고
    • 4 proteoglycan by heparin from glomeruli of streptozotocin-induced diabetic rats
    • 4 proteoglycan by heparin from glomeruli of streptozotocin-induced diabetic rats. Diabetes 1989;38:130-9.
    • (1989) Diabetes , vol.38 , pp. 130-139
    • Klein, D.J.1    Oejema, T.R.2    Brown, D.M.3
  • 73
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Rupslathi E, Yamaguchi Y. Proteoglycans as modulators of growth factor activities. Cell 1991;64:867-9.
    • (1991) Cell , vol.64 , pp. 867-869
    • Rupslathi, E.1    Yamaguchi, Y.2
  • 74
    • 0026696647 scopus 로고
    • Altered cellular interactions between endothelial cells and nonenzymatically glycosylated laminin/type IV collagen
    • Haitoglou CS, Tsilibary EC, Brownlee M, Charonis AS. Altered cellular interactions between endothelial cells and nonenzymatically glycosylated laminin/type IV collagen. J Biol Chem 1992;267:12404-7.
    • (1992) J Biol Chem , vol.267 , pp. 12404-12407
    • Haitoglou, C.S.1    Tsilibary, E.C.2    Brownlee, M.3    Charonis, A.S.4
  • 75
    • 0021886497 scopus 로고
    • Non enzymatic glycosylation products on collagen covalently trap low density lipoprotein
    • Brownlee M, Vlassara H, Cerami A. Non enzymatic glycosylation products on collagen covalently trap low density lipoprotein. Diabetes 1985;34:938-41.
    • (1985) Diabetes , vol.34 , pp. 938-941
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 76
    • 0027291535 scopus 로고
    • Aminoguanidine treatment increases elasticity and decreases fluid filtration of large arteries from diabetic rats
    • Huijberts MSP, Wolfenbutel BHR, Struijker R et al. Aminoguanidine treatment increases elasticity and decreases fluid filtration of large arteries from diabetic rats. J Clin Invest 1993;92:1407-11.
    • (1993) J Clin Invest , vol.92 , pp. 1407-1411
    • Huijberts, M.S.P.1    Wolfenbutel, B.H.R.2    Struijker, R.3
  • 77
    • 0028587238 scopus 로고
    • Receptor for AGEs has a central role in vessel wall interactions and gene activation in response to AGE proteins
    • Schmidt AM, Hasu M, Popov D et al. Receptor for AGEs has a central role in vessel wall interactions and gene activation in response to AGE proteins. Proc Natl Acad Sci USA 1994; 91:8807-11.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8807-8811
    • Schmidt, A.M.1    Hasu, M.2    Popov, D.3
  • 78
    • 0029851005 scopus 로고    scopus 로고
    • Endothelial cell dysfunction secondary to the adhesion of diabetic erythrocytes, modulation by Iloprost
    • Zoukourian C, Wautier MP, Chappey O et al Endothelial cell dysfunction secondary to the adhesion of diabetic erythrocytes, modulation by Iloprost. Int Angiol 1996;15:195-200.
    • (1996) Int Angiol , vol.15 , pp. 195-200
    • Zoukourian, C.1    Wautier, M.P.2    Chappey, O.3
  • 79
    • 0024468052 scopus 로고
    • Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties
    • Esposito C, Gerlach H, Brett J, Stern D, Vlassara H. Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties. J Exp Med 1989;170:1387-407.
    • (1989) J Exp Med , vol.170 , pp. 1387-1407
    • Esposito, C.1    Gerlach, H.2    Brett, J.3    Stern, D.4    Vlassara, H.5
  • 80
    • 0026062122 scopus 로고
    • Advanced glycation end products quench nitric oxide and mediate defective endothelium dependent vasodilatation in experimental diabetes
    • Bucala R, Tracey KJ, Cerami A. Advanced glycation end products quench nitric oxide and mediate defective endothelium dependent vasodilatation in experimental diabetes. J Clin Invest 1991;87: 432-8.
    • (1991) J Clin Invest , vol.87 , pp. 432-438
    • Bucala, R.1    Tracey, K.J.2    Cerami, A.3
  • 81
    • 0026713726 scopus 로고
    • Advanced glycosylation end products block the antiproliferative effect of nitric oxide. Role in the vascular and renal complications of diabetes mellitus
    • Hogan M, Cerami A, Bucala R. Advanced glycosylation end products block the antiproliferative effect of nitric oxide. Role in the vascular and renal complications of diabetes mellitus. J Clin Invest 1992;90:1110-5.
    • (1992) J Clin Invest , vol.90 , pp. 1110-1115
    • Hogan, M.1    Cerami, A.2    Bucala, R.3
  • 82
    • 0027194349 scopus 로고
    • Angiogenic effects of advanced glycation end products of the Maillard reaction on cultured human umbilical cord vein endothelial cells
    • Tezuka M, Koyama N, Morisaki N et al. Angiogenic effects of advanced glycation end products of the Maillard reaction on cultured human umbilical cord vein endothelial cells. Biochem Biophys Res Commun 1993;193:674-80.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 674-680
    • Tezuka, M.1    Koyama, N.2    Morisaki, N.3
  • 83
    • 0023690359 scopus 로고
    • Increased expression of basement membrane components in human endothelial cells cultured in high glucose
    • Cagliero E, Maiello M, Boeri D, Roy S, Lorenzi M. Increased expression of basement membrane components in human endothelial cells cultured in high glucose. J Clin Invest 1988; 82:735-38.
    • (1988) J Clin Invest , vol.82 , pp. 735-738
    • Cagliero, E.1    Maiello, M.2    Boeri, D.3    Roy, S.4    Lorenzi, M.5
  • 84
    • 0025067393 scopus 로고
    • Overexpression of fibronectin induced by diabetes or high glucose: Phenomenon with a memory
    • Roy S, Sala R, Cagliero E, Lorenzi M. Overexpression of fibronectin induced by diabetes or high glucose: phenomenon with a memory. Proc Natl Acad Sci USA 1990;87:404-8.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 404-408
    • Roy, S.1    Sala, R.2    Cagliero, E.3    Lorenzi, M.4
  • 85
    • 0027171266 scopus 로고
    • Oxidants, antioxidants and the degenerative disease of aging
    • Ames B, Shigenaga MK, Hagen M. Oxidants, antioxidants and the degenerative disease of aging. Proc Natl Acad Sci USA 1993;90: 7915-22.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7915-7922
    • Ames, B.1    Shigenaga, M.K.2    Hagen, M.3
  • 86
    • 0027365599 scopus 로고
    • Vascular cell adhesion molecule (VCAM1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells
    • Marui N, Offermann MK, Swerlick R et al. Vascular cell adhesion molecule (VCAM1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells. J Clin Invest 1993;92:1866-74.
    • (1993) J Clin Invest , vol.92 , pp. 1866-1874
    • Marui, N.1    Offermann, M.K.2    Swerlick, R.3
  • 87
    • 0028304625 scopus 로고
    • Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptor binding proteins
    • Yan SD, Schmidt AM, Anderson GM et al. Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptor binding proteins. J Biol Chem 1994;269:9889-94.
    • (1994) J Biol Chem , vol.269 , pp. 9889-9894
    • Yan, S.D.1    Schmidt, A.M.2    Anderson, G.M.3
  • 88
    • 0028173588 scopus 로고
    • The role of oxidation and glycation in the pathogenesis of diabetic atherosclerosis
    • O'Brien R, Trimmins K. The role of oxidation and glycation in the pathogenesis of diabetic atherosclerosis. Trends Endocrinol Metab 1994;5:329-34.
    • (1994) Trends Endocrinol Metab , vol.5 , pp. 329-334
    • O'Brien, R.1    Trimmins, K.2
  • 89
    • 0027938706 scopus 로고
    • Determination of the mechanism of free radical generation in human aortic endothelial cells exposed to anoxia and reoxygenation
    • Zweier JL, Broderick R, Kuppusamy P, Thompson-Gorman S, Lutty GA. Determination of the mechanism of free radical generation in human aortic endothelial cells exposed to anoxia and reoxygenation. J Biol Chem 1994;269:24156-62.
    • (1994) J Biol Chem , vol.269 , pp. 24156-24162
    • Zweier, J.L.1    Broderick, R.2    Kuppusamy, P.3    Thompson-Gorman, S.4    Lutty, G.A.5
  • 90
    • 0029076397 scopus 로고
    • Non enzymatically glycated tau protein in Alzheimer's disease induce neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide
    • Yan SD, Yan SF, Chen X et al. Non enzymatically glycated tau protein in Alzheimer's disease induce neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide. Nature Med 1995;1:693-9.
    • (1995) Nature Med , vol.1 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3
  • 91
    • 0001430544 scopus 로고
    • Accelerated age-related browning of human colagen in diabetes mellitus
    • Monnier VM, Kohn RR, Cerami A. Accelerated age-related browning of human colagen in diabetes mellitus. Proc Natl Acad Sci USA 1994;81:583-7.
    • (1994) Proc Natl Acad Sci USA , vol.81 , pp. 583-587
    • Monnier, V.M.1    Kohn, R.R.2    Cerami, A.3
  • 92
    • 0027732183 scopus 로고
    • Immunohistochemical localization of AGEs in coronary atheroma and cardiac tissue in diabetes mellitus
    • Nakamura Y, Hori Y, Nishino T et al. Immunohistochemical localization of AGEs in coronary atheroma and cardiac tissue in diabetes mellitus. Am J Pathol 1993;143:1649-56.
    • (1993) Am J Pathol , vol.143 , pp. 1649-1656
    • Nakamura, Y.1    Hori, Y.2    Nishino, T.3
  • 93
    • 0023253280 scopus 로고
    • Increased vascular permeability in spontaneously diabetic BB/W rats and in rats with mild or severous severe streptozocin-induced diabetes. Prevention by aldose reductase inhibitors and castration
    • Williamson JR, Chang K, Tilton RG et al. Increased vascular permeability in spontaneously diabetic BB/W rats and in rats with mild or severous severe streptozocin-induced diabetes. Prevention by aldose reductase inhibitors and castration. Diabetes 1987; 36:813-21.
    • (1987) Diabetes , vol.36 , pp. 813-821
    • Williamson, J.R.1    Chang, K.2    Tilton, R.G.3
  • 94
    • 0030061699 scopus 로고    scopus 로고
    • Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy: Soluble receptor for advanced glycation endproducts blocks hyperpermeability in diabetic rats
    • Wautier JL, Zoukourian C, Chappey O et al. Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy: soluble receptor for advanced glycation endproducts blocks hyperpermeability in diabetic rats. J Clin Invest 1996;97:238-43.
    • (1996) J Clin Invest , vol.97 , pp. 238-243
    • Wautier, J.L.1    Zoukourian, C.2    Chappey, O.3
  • 95
    • 0027443733 scopus 로고
    • Relationship between markers of endothelial dysfunction, oxidant injury and tubular damage in patients with insulin-dependent diabetes mellitus
    • Yaquob M, Patrick AW, McClelland P et al. Relationship between markers of endothelial dysfunction, oxidant injury and tubular damage in patients with insulin-dependent diabetes mellitus. Clin Sci 1993;85:557-62.
    • (1993) Clin Sci , vol.85 , pp. 557-562
    • Yaquob, M.1    Patrick, A.W.2    McClelland, P.3
  • 96
    • 0027942607 scopus 로고
    • Vascular endothelial growth factor in ocular fluid of patients with diabetic retinopathy and other retinal disorders
    • Aiello LP, Avery RL, Arrigg PG. Vascular endothelial growth factor in ocular fluid of patients with diabetic retinopathy and other retinal disorders. N Engl J Med 1994;331:1480-7.
    • (1994) N Engl J Med , vol.331 , pp. 1480-1487
    • Aiello, L.P.1    Avery, R.L.2    Arrigg, P.G.3
  • 97
    • 0029126212 scopus 로고
    • Receptor-mediated toxicity to pericytes of advanced glycosylation endproducts
    • Yamagishi SI, Hsu Cheng-Chin, Taniguchi M et al. Receptor-mediated toxicity to pericytes of advanced glycosylation endproducts. Biochem Biophys Res Commun 1995;213:681-7.
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 681-687
    • Yamagishi, S.I.1    Cheng-Chin, H.2    Taniguchi, M.3
  • 98
    • 0026465477 scopus 로고
    • Current hypotheses for the biochemical basis of diabetic retinopathy
    • Mandarino LJ. Current hypotheses for the biochemical basis of diabetic retinopathy. Diabetes Care 1992; 15:1892-901.
    • (1992) Diabetes Care , vol.15 , pp. 1892-1901
    • Mandarino, L.J.1
  • 99
    • 0027169317 scopus 로고
    • Increased collagen-liked pentosidine levels and AGEs in early diabetic nephropathy
    • Beisswenger PJ, Morre LL, Brinck-Johnsen T, Curphey TJ. Increased collagen-liked pentosidine levels and AGEs in early diabetic nephropathy. J Clin Invest 1993;92:212-7.
    • (1993) J Clin Invest , vol.92 , pp. 212-217
    • Beisswenger, P.J.1    Morre, L.L.2    Brinck-Johnsen, T.3    Curphey, T.J.4
  • 100
    • 0026323337 scopus 로고
    • Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy
    • Hammes HP, Martin S, Federlin K, Geisen K, Brownlee M. Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy. Proc Natl Acad Sci USA 1991; 88:11555-8.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11555-11558
    • Hammes, H.P.1    Martin, S.2    Federlin, K.3    Geisen, K.4    Brownlee, M.5
  • 101
    • 0020570370 scopus 로고
    • Polyantigenic expansion of basement membrane constituents in diabetic nephropathy
    • Falk RJ, Scheinman JI, Mauer SM, Michael AF. Polyantigenic expansion of basement membrane constituents in diabetic nephropathy. Diabetes 1983;32:34-9.
    • (1983) Diabetes , vol.32 , pp. 34-39
    • Falk, R.J.1    Scheinman, J.I.2    Mauer, S.M.3    Michael, A.F.4
  • 102
    • 0025938891 scopus 로고
    • Advanced glycation end products in patients with diabetic nephropathy
    • Makita Z, Radoff S, Rayfeild EJ et al. Advanced glycation end products in patients with diabetic nephropathy. N Engl J Med 1991;325:836-42.
    • (1991) N Engl J Med , vol.325 , pp. 836-842
    • Makita, Z.1    Radoff, S.2    Rayfeild, E.J.3
  • 104
    • 0026603130 scopus 로고
    • Receptor-specific increase in extracellular matrix production in mouse mesangial cells by advanced glycated end products is mediated via platelet-derived growth factor
    • Doi T, Vlassara H, Kirstein M, Yamada Y, Striker GE, Striker LJ. Receptor-specific increase in extracellular matrix production in mouse mesangial cells by advanced glycated end products is mediated via platelet-derived growth factor. Proc Natl Acad Sci USA 1992;89:2873-7.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2873-2877
    • Doi, T.1    Vlassara, H.2    Kirstein, M.3    Yamada, Y.4    Striker, G.E.5    Striker, L.J.6
  • 105
    • 8044242366 scopus 로고
    • Clinical manifestations and erythrocyte adhesion to endothelium in sickle cell syndrome
    • Wautier JL, Galacteros F, Wautier MP et al. Clinical manifestations and erythrocyte adhesion to endothelium in sickle cell syndrome. Am J Hematol 1985;121:19-26.
    • (1985) Am J Hematol , vol.121 , pp. 19-26
    • Wautier, J.L.1    Galacteros, F.2    Wautier, M.P.3
  • 106
    • 0022363735 scopus 로고
    • Membrane knobs are required for the microcirculatory obstruction induced by plasmodium falciparum-infected erythrocytes
    • Raventos-Suarez C, Kaul DK, Mackuso F, Nagel RL. Membrane knobs are required for the microcirculatory obstruction induced by plasmodium falciparum-infected erythrocytes. Proc Natl Acad Sci USA 1985;82:3829-33.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3829-3833
    • Raventos-Suarez, C.1    Kaul, D.K.2    Mackuso, F.3    Nagel, R.L.4
  • 107
    • 0022620814 scopus 로고
    • Erythrocyte adhesion to cultured endothelium and glycaemic control in type 1 (insulin-dependent) diabetic patients
    • Wautier JL, Leblanc, H, Wautier MP, Abadie E, Passa P, Caen J. Erythrocyte adhesion to cultured endothelium and glycaemic control in type 1 (insulin-dependent) diabetic patients. Diabetologia 1986;29:151-5.
    • (1986) Diabetologia , vol.29 , pp. 151-155
    • Wautier, J.L.1    Leblanc, H.2    Wautier, M.P.3    Abadie, E.4    Passa, P.5    Caen, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.