L-Arginine inhibits in vitro nonenzymatic glycation and advanced glycosylated end product formation of human serum albumin

Amino Acids

Volumn 11, Issue 1, 1996, Pages 69-81

  Servetnick, D A ^a,e   Bryant, D ^b   Wells Knecht, K J ^c   Wiesenfeld, P L ^d  

^a UNIVERSITY OF MARYLAND   (United States)

^b UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

^c UNIVERSITY OF SOUTH CAROLINA   (United States)

^d CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

^e NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Amino acids; Aminoguanidine; Arginine; Electrospray; Glycation; Human serum albumin; Maillard reaction

Indexed keywords

AMINOGUANIDINE; ARGININE; CARBON 14; GLUCOSE; HUMAN SERUM ALBUMIN; PENTETIC ACID; TRYPSIN;

ARTICLE; CONTROLLED STUDY; FLUORESCENCE; ISOTOPE LABELING; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN GLYCOSYLATION; STRUCTURE ACTIVITY RELATION;

EID: 0029761039     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00805722     Document Type: Article

References (36)

1. Baynes JW, Thorpe SR, Murtiashaw MH (1984) Nonenzymatic glucosylation of lysine residues. Methods Enzymol 106: 88-98
2. Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal Biochem 72: 248-254
3. Brownlee M, Vlassara H, Cerami A (1984) Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann Intern Med 101: 527-537
4. Brownlee M, Vlassara H, Kooney A, Ulrich P, Cerami A (1986) Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 232: 1629-1632
5. Brownlee M, Cerami A, Vlassara H (1988) Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. N Engl J Med 318: 1315-1321
6. Brownlee M, Cerami A, Vlassara H (1988) Advanced products of nonenzymatic-glycosylation and the pathogenesis of diabetic vascular disease. Diab Metab Rev 4: 437-451
7. Dyer DG, Blackledge JA, Katz BM, Hull CJ, Adkisson HD, Thorpe SR, Lyons TJ, Baynes JW (1991) The Maillard reaction in vivo. Z Ernährungswiss 30: 29-45
8. Edelstein D, Brownlee M (1992) Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine. Diabetes 41: 26-29
9. Fu MX, Knecht KJ, Thorpe SR, Baynes JW (1992) Role of oxygen in cross-linking and chemical modification of collagen by glucose. Diabetes 41 [Suppl] 2: 42-48
10. Fu MX, Wells-Knecht KJ, Blackledge JA, Lyons TJ, Thorpe SR, Baynes JW (1994) Glycation, glycoxidation, and cross-linking of collagen by glucose: kinetics, mechanisms, and inhibition of late stages of the Maillard reaction. Diabetes 43: 676-683
11. Hunt JV, Dean RT, Wolff SP (1988) Hydroxyl radical production and autoxidative glycosylation. Biochem J 256: 205-212
12. Hunt JV, Bottoms MA, Mitchinson MJ (1993) Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Biochem J 291: 529-535
13. Igaki N, Sakai M, Hata H, Oimomi M, Baba S, Kato H (1990) Effects of 3-deoxyglucosone on the Maillard reaction. Clin Chem 36: 631-634
14. Kato H, Shin DB, Hayase F (1987) 3-Deoxyglucosone crosslinks proteins under physiological conditions. Agric Biol Chem 51: 2009-2011
15. Laemmli UK (1970) Cleavage of structural protein during assembly of the head of bacteriophage. Nature 227: 680-685
16. Ledl F (1991) Der Abbau von reduzierenden Zuckern und Aminen bei der Maillard-Reaktion. Z Ernährungswiss 30: 4-17
17. Ledl F, Schleicher E (1990) New aspects of the Maillard reaction in foods and in the human body. Angewandte Chemie 29: 565-594
18. Lubec G, Vierhapper H, Bailey AJ, Damjancic P, Fasching P, Sims TJ, Kampel D, Popow C, Bartosch B (1991) Influence of L-arginine on glucose mediated colagen cross link precursors in patients with diabetes mellitus. Amino Acids 1: 73-80
19. Means GE, Feeney RE (eds) (1971) Chemical modification of proteins. Holden-Day, San Francisco, pp 194-211
20. Menzel EJ, Reihsner R (1991) Alterations of biochemical and biomechanical properties of rat tail tendons caused by non-enzymatic glycation and their inhibition by dibasic amino acids arginine and lysine. Diabetologia 34: 12-16
21. Mereish KA, Rosenberg H, Cobby J (1982) Glucosylated albumin and its influence on salicylate binding. J Pharm Sci 71: 235-238
22. Morris MA, Preddy L (1986) Glycosylation accelerates albumin degradation in normal and diabetic dogs. Biochem Med Metab Biol 35: 267-270
23. Ramakrishnan S, Sulochana KN (1993) Decrease in glycation of lens proteins by lysine and glycine by scavenging of glucose and possible mitigation of cataractogenesis. Exp Eye Res 57: 623-628
24. Sensi M, De Rossi MG, Celi FS, Cristina A, Rosati C, Prrett D, Anreani D, Di Mario U (1993) D-Lysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats. Diabetologia 36: 797-801
25. Shin DB, Hayase F, Kato H (1988) Polymerization of proteins caused by reaction with sugars and the formation of 3-deoxyglucosone under physiological conditions. Agric Biol Chem 52: 1451-1458
26. Smith RD, Loo JA, Edmonds CG, Barinaga CJ, Udseth HR (1990) New developments in biochemical mass spectrometry: electrospray ionization. Anal Chem 62: 882-899
27. Smoyer WE, Brouhard BH, Rassin DK, LaGrone L (1991) Enhanced GFR response to oral versus intravenous arginine administration in normal adults. J Lab Clin Med 118: 166-175
28. Sokal RR, Rolf JF (1981) Linear regression. Biometry, 2nd edn. WH Freeman and Co, New York, pp 454-530
29. Soulis-Liparota T, Cooper M, Papazoglou D, Clarke B, Jerums G (1991) Retardation by aminoguanidine of development of albuminuria, mesangial expansion, and tissue fluorescence in streptozocin-induced diabetic rat. Diabetes 40: 1328-1334
30. Van Boekel MAM (1991) The role of glycation in aging and diabetes mellitus. Mol Biol Rep 15: 57-64
31. Vidal P, Nielsen E, Welinder BS (1992) Effect of glycation on the heterogeneity of human serum albumin analysed by reversed-phase high-performance liquid chromatography in a solvent containing formic acid. J Chromatogr 573: 201-206
32. Wells-Knecht KJ, Zyzak DV, Litchfield JE, Thorpe SR, Baynes JW (1995) Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry 34: 3702-3708
33. ε-carboxymethyllysine in the diabetic db/db mouse. Nephron 62: 80-83
34. Wolff SP, Dean RT (1987) Glucose autoxidation and protein modification. Biochem J 245: 243-250
35. Wolff SP, Jiang ZY, Hunt JV (1991) Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radical Biol Med 10: 339-352
36. Zyzak DV, Richardson JM, Thorpe SR, Baynes JW (1995) Formation of reactive intermediates from Amadori compounds under physiological conditions. Arch Biochem Biophys 316: 547-554