References
The Diabetes Control and Complications Trial Research Group: The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. New Engl. J. Med. 329 (1993), 977–986.
Bucala, R., H. Vlassara, A. Cerami: Advanced glycosylation endproducts. In: Harding, J. J., M. J. C. Crabbe (eds.): Post translational modification of proteins. CRC Press Inc., Boca Raton, FL 1992, vol. 2, p. 53–79.
Vlassara, H., R. Bucala, L. Striker: Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging. J. Lab. Invest. 70 (1994), 138–151.
Dyer, D. G., J. A. Blackledge, B. M. Katz, C. J. Hull, H. D. Adkisson, S. R. Thorpe, T. J. Lyons, J. W. Baynes: The Maillard reaction in vivo. Z. Ernährungswiss. 30 (1991), 29–45.
Bailey, A. J., T. J. Sims, N. C. Avery, C. A. Miles: Chemistry of collagen cross-links — glucose-mediated covalent cross-linking of type-IV collagen in lens capsules. Biochem. J. 296 (1993), 489–496.
Dyer, D. G., J. A. Blackledge, S. R. Thorpe, J. W. Baynes: 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 (1991), 11654–11660.
Fu, M. X., K. J. Well-Knecht, J. A. Blackledge, T. J. Lyons, S. R. Thorpe, J. W. Baynes: Glycation, glycoxidation, and cross-linking of collagen by glucose: kinetics, mechanisms, and inhibition of late stages of the Maillard reaction. Diabetes 43 (1994), 676–683.
Vlassara, H.: Non-enzymatic glycosylation. Diabetes Ann. 18 (1991), 371–389.
Nakamura, K., T. Hasegawa, Y. Fukunaga, K. Lenaga: Crosslines A and B as candidates for the fluorophores in age- and diabetes-related cross-linked proteins, and their diacetates produced by Maillard reaction ofα-N-acetyl-L-lysine with D-glucose. J. chem. Soc. chem. Commun. 14 (1992), 992–994.
Nakayama, H., S. Taneda, S. Kuwajima, S. Aoki, Y. Kuroda, K. Misawa, S. Nakagawa: Production and characterization of antibodies to advanced glycation products on proteins. Biochem. biophys. Res. Comm. 162 (1989), 740–745.
Horiuchi, S., N. Araki, Y. Morino: Immunochemical approach to characterize advanced glycation endproducts of the Maillard Reaction. J. biol. Chem. 266 (1991), 7329–7332.
Makita, Z., H. Vlassara, A. Cerami, R. Bucala: Immunochemical detection of advanced glycosylation endproducts in vivo. J. biol. Chem. 267 (1992), 5133–5138.
Brownlee, M., H. Vlassara, A. Kooney, P. Ulrich, A. Cerami: Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 232 (1986), 1629–1632.
Bucala, R., K. J. Tracey, A. Cerami: Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilatation in experimental diabetes. J. clin. Invest. 87 (1991), 432–438.
De Tejada, I. S., I. Goldstein, K. Azadzoi, R. J. Krane, R. J. R. Cohen: Impaired neurogenic and endothelium-mediated relaxation of penile smooth muscle in diabetic men with impotence. New Engl. J. Med. 320 (1989), 1025–1030.
McVeigh, G. E., G. M. Brennan, G. D. Johnston, B. J. McDermott, L. T. McGrath, W. R. Henry, J. W. Andrews, J. R. Hayes: Impaired endothelium-dependent and independent vasodilation in patients with type 2 (non-insulin-dependent) diabetes mellitus. Diabetologia 35 (1992), 771–776.
Gascho, J. A., C. Fanelli, R. Zelis: Aging reduces venous distensibility and the venodilatory response to nitroglycerin in normal subjects. Am. J. Cardiol. 63 (1989), 1267–1270.
Vlassara, H., H. Fuh, Z. Makita, S. Krungkrai, A. Cerami, R. Bucala: Exogenous advanced glycosylation endproducts induce complex vascular dysfunction in normal animals; a model for diabetic and aging complications. Proc. nat. Acad. Sci. (Wash.) 89 (1992), 12043–12047.
Hogan, M., A. Cerami, R. Bucala: Advanced glycosylation endproducts block the antiproliferative effect of nitric oxide. J. clin. Invest. 90 (1992), 1110–1115.
Bucala, R., Z. Makita, T. Koschinsky, A. Cerami, H. Vlassara: Lipid advanced glycosylation. Pathway for lipid oxidation in vivo. Proc. nat. Acad. Sci. (Wash.) 90 (1993), 6434–6438.
Bucala, R., Z. Makita, G. Vega, S. Grundy, T. Koschinsky, A. Cerami, H. Vlassara: Modification of LDL by advanced glycosylation endproducts contributes to the dyslipidemia of diabetes and renal insufficiency. Proc. nat. Acad. Sci. (Wash.) 91 (1994), 9441–9445.
Nicholls, K., T. E. Mandel: Advanced glycosylation endproducts in experimental murine diabetic nephropathy. Effect of islet isografting and of aminoguanidine. J. Lab. Invest. 60 (1989), 486–491.
Ellis, E. N., B. H. Good: Prevention of glomerular basement membrane thickening by aminoguanidine in experimental diabetes mellitus. Metabolism 40 (1991), 1016–1019.
Soulis-Liparota, T., M. Cooper, D. Papazoglou, B. Clarke, G. Jerums: Retardation by aminoguanidine of development of albuminuria, mesangial expansion, and tissue fluorescence in streptozotocin-induced diabetic rat. Diabetes 40 (1991), 1328–1334.
Edelstein, D., M. Brownlee: Aminoguanidine ameliorates albuminuria in diabetic hypertensive rats. Diabetologia 35 (1992), 96–97.
Itakura, M., H. Yoshikawa, C. Bannai, M. Kato, K. Kunika, Y. Kawakami, T. Tamaoka, K. Yamashita: Aminoguanidine decreases urinary albumin and high-molecular-weight proteins in diabetic rats. Life Sci. 49 (1991), 889–897.
Cho, H. K., H. Kozu, G. A. Peyman, G. J. Parry, B. Khoobehi: The effect of aminoguanidine on the blood-retinal barrier in streptozotocin-induced diabetic rats. Ophthal. Surg. 22 (1991), 44–47.
Hammes, H. P., S. Martin, K. Federlin, K. Geisen, M. Brownlee: Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy. Proc. nat. Acad. Sci. (Wash.) 88 (1991), 11555–11558.
Hammes, H.-P., M. Brownlee, D. Edelstein, M. Saleck, S. Martin, K. Federlin: Aminoguanidine inhibits the development of accelerated diabetic retinopathy in the spontaneous hypertensive rat. Diabetologia 37 (1994), 32–35.
Huijberts, M. S. P., B. H. R. Wolffenbuttel, H. A. J. Struijker-Boudier, F. R. L. Crijns: Aminoguanidine treatment increases elasticity and decreases fluid filtration of large arteries from diabetic rats. J. clin. Invest. 92 (1993), 1407–1411.
Huijberts, M. S. P., B. H. R. Wolffenbuttel, F. R. L. Crijns, A. C. Nieuwenhuijzen Kruseman, M. H. A. Bemelmans, H. A. J. Struijker Boudier: Aminoguanidine reduces regional albumin clearance but not urinary albumin excretion in streptozotocin-diabetic rats. Diabetologia 37 (1994), 10–14.
Kihara, J., J. D. Schmelzer, J. F. Podusio, G. L. Curran, K. K. Nickander, P. A. Low: Aminoguanidine effects on nerve blood flow, vascular permeability, electrophysiology, and oxygen free radicals. Proc. nat. Acad. Sci. (Wash.) 88 (1991), 6107–6111.
Yagihashi, S., M. Kamijo, M. Baba, N. Yagihashi, K. Nagai: Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats. Diabetes 41 (1992), 47–52.
Cameron, N. E., M. A. Cotter, K. Dines, A. Love: Effects of aminoguanidine on peripheral nerve function and polyol pathway metabolites in streptozotocin-diabetic rats. Diabetologia 35 (1992), 946–950.
Odetti, P. R., A. Borgoglio, A. De Pascale, R. Rolandi, L. Adezati: Prevention of diabetes-increased aging effect on rat collagen-linked fluorescence by aminoguanidine and rutin. Diabetes 39 (1990), 796–801.
Oxlund, H., T. T. Andreassen: Aminoguanidine treatment reduces the increase in collagen stability of rats with experimental diabetes mellitus. Diabetologia 35 (1992), 75–78.
Makita, Z., H. Vlassara, E. Rayfield, K. Cartwright, E. Friedman, R. Rodby, A. Cerami, R. Bucala: Hemoglobin-AGE: A circulating marker of advanced glycosylation. Science 258 (1992), 651–653.
Vlassara, H., M. Brownlee, A. Cerami: High-affinity receptor-mediated uptake and degradation of glucose-modified proteins: A potential mechanism for the removal of senescent macromolecules. Proc. nat. Acad. Sci. (Wash.) 82 (1985), 5588–5592.
Vlassara, H., M. Brownlee, A. Cerami: Novel macrophage receptor for glucose-modified proteins is distinct from previously described scavenger receptors. J. exp. Med. 164 (1986), 1301–1309.
Yang, Z., Z. Makita, Y. Horii, S. Brunelle, A. Cerami, P. Sehajpal, M. Suthanthiran, H. Vlassara: Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: Relationship to macrophage receptor for glucose-modified proteins. J. exp. Med. 174 (1991), 515–524.
Kirstein, M., J. Brett, S. Radoff, D. Stern, H. Vlassara: Advanced Glycosylation Endproducts selectively induce monocyte migration across intact endothelial cell monolayers, and elaboration of growth factors: Role in aging and diabetic vasculopathy. Proc. nat. Acad. Sci. (Wash.) 87 (1990), 9010–9014.
Vlassara, H., M. Brownlee, K. R. Manogue, A. Pasagian, C. A. Dinarello: Cachetin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science 240 (1988), 1546–1548.
Imani, F., Y. Horii, M. Suthanthiran, E. Y. Skolnik, Z. Makita, V. Sharma, P. Sehajpal, H. Vlassara: Advanced glycosylation endproduct-specific receptors on human and rat T-lymphocytes mediate synthesis of interferon-γ, role in tissue remodeling. J. exp. Med. 178 (1993), 2165–2172.
Libby, P., G. K. Hansson: Involvement of the immune system in human atherogenesis: Current knowledge and unanswered questions. J. Lab. Invest. 64 (1991), 5–15.
Esposito, C., D. Stern, H. Gerlach, H. Vlassara: Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties. J. exp. Med. 170 (1989), 1387–1407.
Schmidt, A. M., M. Vianna, M. Gerlach, J. Brett, J. Ryan, J. Kao: Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface. J. biol. Chem. 256, 21 (1992), 14987–14997.
Neeper, M., A. M. Schmidt, J. Brett, S. D. Yan, F. Wang, Y. C. E. Pan, et al.: Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. J. biol. Chem. 267 (1992), 14998–15004.
Brett, J., A. M. Schmidt, S. D. Yan, Y. S. Zou, E. Weidman, D. Pinsky, R. Nowygrod, M. Neeper, C. Przysiecki, A. Shaw, A. Migheli, D. Stern: Survey of the distribution of a newly characterized receptor for advanced glycation endproducts in tissues. Amer. J. Path. 143 (1993), 1699–1712.
Imani, F., D. Wojciechowicz, M. Creager, J. Greenidge, A. Cerami, H. Vlassara: Serum Mac-2 or carbohydrate binding protein-35 (CBP) binds glycated proteins and is elevated in diabetic sera. Faseb. J. 8 (1994), A1385.
Skolnik, E. Y., Z. Yang, Z. Makita, S. Radoff, M. Kirstein, H. Vlassara: Human and rat mesangial cell receptors for glucose-modified proteins: Potential role in kidney tissue remodelling and diabetic nephropathy. J. exp. Med. 174 (1991), 931–939.
Doi, T., H. Vlassara, M. Kirstein, Y. Yamada, G. E. Striker, L. J. Striker: Receptor-specific increased mesangial cell extracellular matrix production is mediated by PDGF. Proc. nat. Acad. Sci. (Wash.) 89 (1992), 2873–2877.
United States Renal Data System, USRDS 1992 Annual Data Report: The National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Disease. Bethesda, Maryland, August 1992.
Yang, C. W., H. Vlassara, E. P. Peten, C. J. He, G. E. Striker, L. J. Striker: Advanced glycosylation endproducts upregulate gene expression found in diabetic glomerular disease. Proc. nat. Acad. Sci. (Wash.) 91 (1994), 9436–9440.
Miyata, T., O. Oda, R. Inagi, Y. Iida, N. Araki, N. Yamada, S. Horiuchi, N. Taniguchi, K. Maeda, T. Kinoshita: β2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associate amyloidosis. J. clin. Invest. 92 (1993), 1243–1252.
Vlassara, H., L. J. Striker, S. Teichberg, H. Fuh, Y. M. Li, M. Steffes: Advanced glycosylation endproducts induce glomerular sclerosis and albuminuria in normal rats. Proc. nat. Acad. Sci. (Wash.) 91 (1994), 11704–11708.
Makita, Z., S. Radoff, E. J. Rayfield, Z. Yang, E. Skolnik, E. A. Friedman, A. Cerami, H. Vlassara: Advanced glycosylation endproducts in patients with diabetic nephropathy. New Engl. J. Med. 325 (1991), 836–842.
Makita, Z., R. Bucala, E. J. Rayfield, E. A. Friedman, A. M. Kaufman, S. M. Korbet, R. H. Barth, J. A. Winston, H. Fuh, K. R. Manogue, A. Cerami, H. Vlassara: Reactive glycosylation endproducts in diabetic uraemia & treatment of renal failure. Lancet 343 (1994), 1519–1522.
Miyata, T., R. Inagi, Y. Iida, M. Sato, N. Yamada, O. Oda, K. Maeda, H. Seo: Involvement of β2-microglobulin modified with advanced glycation endproducts in the pathogenesis of hemodialysis-associated amyloidosis. J. clin. Invest. 93 (1994), 521–527.
Koschinsky, T., C. He, T. Mitsuhashi, R. Bucala, C. Liu, H. Vlassara: Reactive advanced glycation endproducts (AGEs) from food: A new risk for diabetic complications. Diabetes 45, Suppl. 2 (1996), 127A.
Koschinsky, T., C. He, T. Mitsuhashi, R. Bucala, C. Liu, H. Vlassara: Orally absorbed reactive glycation products — A new risk factor in diabetic nephropathy. (1996) (submitted).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Vlassara, H. Pathogenesis of diabetic nephropathy, advanced glcation and new therapy. Med. Klin. 92 (Suppl 1), 29–34 (1997). https://doi.org/10.1007/BF03041807
Issue Date:
DOI: https://doi.org/10.1007/BF03041807