New biomarkers of Maillard reaction damage to proteins

Nephrology Dialysis Transplantation

Volumn 11, Issue SUPPL. 5, 1996, Pages 41-47

  Wells Knecht, Kevin J ^a   Brinkmann, Elisabeth ^a   Wells Knecht, Mary C ^a   Litchfield, John E ^a   Ahmed, Mahtab U ^a   Reddy, Sharanya ^a   Zyzak, David V ^a   Thorpe, Suzanne R ^a   Baynes, John W ^a,b  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

^b UNIVERSITY OF SOUTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

Advanced glycation end product; Glycoxidation product; Glyoxal; Maillard reaction; Methylglyoxal

Indexed keywords

ARGININE; BIOLOGICAL MARKER; GLYOXAL; IMIDAZOLE DERIVATIVE; LYSINE; METHYLGLYOXAL;

CHEMICAL MODIFICATION; CONFERENCE PAPER; CONTROLLED STUDY; CROSS LINKING; DIABETES MELLITUS; GLYCATION; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; TISSUE INJURY;

EID: 0030483803     PISSN: 09310509     EISSN: None     Source Type: Journal    
DOI: 10.1093/ndt/11.supp5.41     Document Type: Conference Paper

References (53)

1. 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. N Engl J Med 1993; 329: 977-986
2. Kennedy L, Baynes JW. Nonenzymatic glycosylation and the chronic complications of diabetes: an overview. Diabetologia 1984; 26: 93-98
3. Baynes JW, Watkins NG, Fisher CI et al. The Amadori product on protein. In: Baynes JW, Monnier VM, eds. The Maillard Reaction in Aging, Diabetes, and Nutrition. Alan R. Liss, New York; 1989: 43-67
4. Bucala R, Cerami A. Advanced glycosylation: chemistry, biology and implications for diabetes and aging. Adv Pharmacol 1992; 23: 1-34
5. Vlassara H, Bucala R, Striker L. Pathogenic effects of advanced glycosylation: biochemical, biologic and clinical implications for diabetes and aging. Lab Invest 1994; 70: 138-151
6. Makita Z, Vlassara H, Cerami A, Bucala R. Immunochemical detection of advanced glycosylation end products in vivo. J Biol Chem 1992; 267: 5133-5138
7. Taneda S, Monnier VM. ELISA of pentosidine, an advanced glycation end product, in biological specimens. Clin Chem 1994; 40: 1766-1773
8. Bucala R, Makita Z, Vega G et al. Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency. Proc Natl Acad Sci USA 1994; 91: 9441-9445
9. Lyons TJ, Li W, Wells-Knecht MC, Jokl R. Toxicity of mildly modified low-density lipoproteins to cultured retinal capillary endothelial cells and pericytes. Diabetes 1994; 43: 1090-1095
10. Giardino I, Edelstein D, Brownlee M. Nonenzymatic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity: a model for intracellular glycosylation in diabetes. J Clin Invest 1994; 94: 110-117
11. Makita Z, Vlassara H, Rayfield E et al. Hemoglobin-AGE: a circulating marker of advanced glycosylation. Science 1992; 258: 651-653
12. ε-(carboxymethyl)lysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 1986; 261: 4889-4994
13. Sell DR, Monnier VM. Structure elucidation of a senescence cross-link from human extracellular matrix: implication of pentoses in the aging process. J Biol Chem 1989; 264: 21597-21602
14. Baynes JW. Role of oxidative stress in development of complications in diabetes. Diabetes 1991; 40:405-412
15. Baynes JW. Role of oxidation chemistry in the Maillard reaction in vivo. In: Ikan R, ed. The Maillard Reaction in Biological Systems. Wiley, New York, in press
16. Wells-Knecht KJ, Zyzak DV, Litchfield JE, Thorpe SR, Baynes JW. Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry 1995; 34: 3702-3709
17. Wolff SP, Jiang ZY, Hunt JV. Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Rad Biol Med 1991; 10: 339-352
18. Wells-Knecht MW, Thorpe SR, Baynes JW. Pathways of formation of glycoxidation products during glycation of collagen. Biochemistry, in press
19. Glomb M, Monnier VM. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates in the Maillard reaction, J Biol Chem 1995; 270: 10017-10026
20. ε-(carboxymethyl)lysine is a dominant advanced glycation end-product (AGE) antigen in tissue proteins. Biochemistry 1995; 34: 10872-10878.
21. Hayase F, Nagaraj RH, Miyata S, Njoroge FG, Monnier VM. Aging of proteins: immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo. J Biol Chem 1989; 263: 3758-3764
22. Portero-Otin M, Nagaraj RH, Monnier VM. Chromatographic evidence for pyrraline formation during protein glycation in vitro and in vivo. Biochim Biophys Acta 1995; 1247: 74-80
23. Smith MA, Taneda S, Richey PL et al. Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proc Nail Acad Sci USA 1994; 91: 5710-5714
24. ε-acetyl-lysine with glucose. J Chem Soc Chem Commun 1992; 992-994
25. Ienaga K., Nakamura K, Hochi T et al. Crosslines. Fluorophores in the AGE-related cross-linked proteins. Contrib Nephrol 1995; 112: 42-51
26. Hodge JE. Chemistry of browning reactions in model systems. Agric Food Chem 1953; 1: 928-943
27. Henle T, Walter AW, Haessner R, Klostermeyer H. Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues with methylglyoxal. Z Lebensm Unters Forsch 1994; 199: 55-58
28. Konishi Y, Hayase F, Kato H. Novel imidazolone compound formed by the advanced Maillard reaction of 3-deoxyglucosone and arginine residues in protein. Biosci Biotech Biochem 1994; 58: 1953-1955
29. Zyzak DV. Studies on the Maillard reaction: reaction of 3-deoxyglucosone with arginine residues in protein. Thesis, University of South Carolina, Columbia, SC, 1995
30. Knecht KJ, Feather MS, Baynes JW. Detection of 3-deoxyfructose and 3-deoxyglucosone in human urine and plasma: evidence for intermediate stages of the Maillard reaction in vivo. Arch Biochem Biophys 1992; 294: 130-137
31. Niwa T, Takeda N, Yoshizumi H et al. Presence of 3-deoxyglucosone, a potent protein cross-linking intermediate of Maillard reaction, in diabetic serum. Biochem Biophys Res Commun 1993; 196: 837-843
32. Yamada H, Miyata S, Igaki N et al. Increase in 3-deoxyglucosone levels in diabetic rat plasma.J Biol Chem 1994; 269: 20275-20280
33. Brinkmann E, Wells-Knecht KJ, Thorpe SR, Baynes JW. Characterization of an imidazolium compound formed by reaction of methylglyoxal and N-hippuryllysine. J Chem Soc Perkin Trans, in press
34. Dyer DG, Dunn JA, Thorpe SR et al. Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J Clin Invest 1993; 91: 2463-2469
35. McLellan AC, Phillips SA, Thornalley PJ. The assay of methylglyoxal in biological systems by derivatization with 1,2-diamino-4,5-dimethoxybenzene. Anal Biochem 1992; 206: 17-23
36. Wells-Knecht KJ, Brinkmann E, Baynes JW. Structural characterization of an imidazolium salt formed from glyoxal and N-hippuryllysme. J Org Chem 1995; 6246-6247
37. Dyer DG, Blackledge JA, Katz BM et al. The Maillard reaction in vivo. J Nutr Sci 1990; 30: 29-45
38. Chang JCF, Ulrich PC, Bucala R, Cerami A. Detection of an advanced glycosylation product bound to protein in situ. J Biol Chem 1985; 260: 7970-7974
39. Pongor S, Ulrich PC, Bencsath RA, 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: 2684-2688
40. Njoroge FG, Fernandes AA, Monnier VM. Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole. J Biol Chem 1986; 263: 10646-10652
41. Horiuchi S, Shiga M, Araki N, Takata K, Saitoh M, Morino Y. Evidence against in vivo presence of 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole, a major fluorescent advanced end product generated by nonenzymatic glycosylation. J Biol Chem 1988; 263: 18821-18826
42. Shapiro R, McManus MJ, Zalut C, Bunn HF. Sites of nonenzymatic glycosylation of human hemoglobin A. J Biol Chem 1980; 255: 3120-3127
43. Garlick RL, Mazer JS. The principal site of nonenzymatic glycosylation of human serum albumin in vivo. J Biol Chem 1983; 258: 6142-6146
44. Velícek J, Davidek T, Davidek J, Trska P, Kvasnicka F, Velcová K. New imidazoles formed in nonenzymatic browning reactions. J Food Sci 1989; 54: 1544-1546
45. Sell DR, Lapolla A, Odetti P, Fogarty J, Monnier VM. Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM. Diabetes 1992; 41: 1286-1292
46. McCance DR, Dyer DG, Dunn JA et al. Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J Clin Invest 1993; 91: 2470-2478
47. Beisswenger PJ, Moore LL, Brinck-Johnsen T, Curphey TJ. Increased collagen-linked pentosidine levels and advanced glycosylation end products in early diabetic nephropathy. J Clin Invest 1993; 92: 2212-2217
48. Fu MX, Wells-Knecht KJ, Blackledge JA, Lyons TJ, Thorpe SR, Baynes JW. Glycation, glycoxidation and cross-linking of collagen by glucose: kinetics, mechanisms and inhibition of late stages of the Maillard reaction. Diabetes 1994; 43: 676-683
49. Baynes JW. Reactive oxygen in the aetiology and complications of diabetes. In: Ioannides C, ed. Drugs, Diet and Disease, Vol. 2: Mechanistic Approaches to Diabetes. Pergamon Press, London, in press.
50. Picard S, Parthasarathy S, Fruebis J, Witztum JL. Aminoguanidine inhibits oxidative modification of low density lipoprotein and the subsequent increase in uptake by macrophage scavenger receptor. Proc Natl Acad Sci USA 1992; 89: 6876-6880
51. Tilton RG, Chang K, Hasan KS et al. Prevention of diabetic vascular dysfunction by guanidines. Inhibition of nitric oxide synthase versus advanced glycation end-product formation. Diabetes 1993; 42: 221-232
52. Schmidt AM, Hori O, Brett J, Van SD, Wautier J-L, Stern S. 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: 1521-1528
53. Lyons TJ, Johnson RH. Glycation, oxidation, and glycoxidation of short- and long-lived proteins and the pathogenesis of diabetic complications. In: Labuza TP, Reineccius GA, Monnier VM, O'Brien J, Baynes JW, eds. Maillard Reactions in Chemistry, Food, and Health. Royal Society of Chemistry, London: 1994: 267-273