Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins

The amino acid modification, gel filtration chromatographic, and electrophoretic characteristics of bovine and human serum albumins irreversibly modified by methylglyoxal (MG-SA) and by glucose-derived advanced glycation endproducts (AGE-SA) were investigated. Methylglyoxal selectively modified arginine residues at low concentration (1 mM); at high methylglyoxal concentration (100 mM), the extent of arginine modification increased and lysine residues were also modified. Both arginine and lysine residues were modified in AGE-SA. Analytical gel filtration HPLC of serum albumin derivatives suggested that the proportion of dimers and oligomers increased with modification in both low and highly modified MG-SA and AGE-SA derivatives relative to unmodified serum albumins. In SDS-PAGE analysis, dimers and oligomers of low-modified MG-SA were dissociated into monomers, but not in highly modified MG-SA. MG-SA had increased anodic electrophoretic mobility under nondenaturing conditions atpH 8.6, indicating an increased net negative charge, which increased with extent of modification; highly modified MG-SA and AGE-SA had similar high electrophoretic mobilities. MG-SA derivatives were fluorescent: the fluorescence was characteristic of the arginine-derived imidazoloneNδ-(5-methyl-4-imidazolon-2-yl)ornithine, but other fluorophores were also present. AGE-SA had similar fluorescence, attributed, in part, to glucose-derived imidazolones. AGE formed from glucose-modified proteins and AGE-like compounds formed from methylglyoxal-modified proteins may both be signals for recognition and degradation of senescent macromolecules.

[1]  A. J. Furth.  The maillard reaction in aging, diabetes and nutrition: edited by John W. Baynes and Vincent M. Monnier, Alan R. Liss, 1989. $85.00 (xvii + 432 pages) ISBN 0 8451 5154 1 , 1990 .

[2]  B G Johansson,et al.  Agarose gel electrophoresis. , 1972, Scandinavian journal of clinical and laboratory investigation. Supplementum.

[3]  H. Klostermeyer,et al.  Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal , 1994 .

[4]  T. Sasaki,et al.  Induction of macrophage growth by advanced glycation end products of the Maillard reaction. , 1994, Journal of immunology.

[5]  Paul J Thornalley,et al.  Evidence against the formation of 2-amino-6-(2-formyl-5-hydroxymethyl-pyrrol-1-yl)-hexanoic acid ('pyrraline') as an early-stage product or advanced glycation end product in non-enzymic protein glycation. , 1993, Clinical science.

[6]  S. Krungkrai,et al.  Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[7]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[8]  Paul J Thornalley,et al.  The hydrolytic autoxidation of 1,4-naphthoquinone-2-potassium sulphonate: implications for 1,4-naphthoquinone-2-potassium sulphonate-induced oxidative stress in the red blood cell. , 1985, Chemico-biological interactions.

[9]  V. Monnier,et al.  Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. , 1989, The Journal of biological chemistry.

[10]  M. Crabbe,et al.  Non-specific binding of advanced-glycosylation end-products to macrophages outweighs specific receptor-mediated interactions. , 1994, The Biochemical journal.

[11]  A. Cerami,et al.  High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[12]  N. Morisaki,et al.  Angiogenic effects of advanced glycation end products of the Maillard reaction on cultured human umbilical cord vein endothelial cells. , 1993, Biochemical and biophysical research communications.

[13]  F. Hayase,et al.  Novel Imidazolone Compound Formed by the Advanced Maillard Reaction of 3-Deoxyglucosone and Arginine Residues in Proteins , 1994 .

[14]  V. Monnier,et al.  Immunohistochemical detection of advanced glycosylation end products in diabetic tissues using monoclonal antibody to pyrraline. , 1992, The Journal of clinical investigation.

[15]  Martina,et al.  Receptor-specific induction of insulin-like growth factor I in human monocytes by advanced glycosylation end product-modified proteins. , 1992, The Journal of clinical investigation.

[16]  Paul J Thornalley,et al.  Methylglyoxal concentration and glyoxalase activities in the human lens. , 1994, Experimental eye research.

[17]  Paul J Thornalley,et al.  The formation of methylglyoxal from triose phosphates , 1993 .

[18]  J. Baynes.  Role of Oxidative Stress in Development of Complications in Diabetes , 1991, Diabetes.

[19]  J. Casazza,et al.  Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes. , 1985, The Journal of biological chemistry.

[20]  Paul J Thornalley,et al.  Receptor-mediated endocytic uptake of methylglyoxal-modified serum albumin. Competition with advanced glycation end product-modified serum albumin at the advanced glycation end product receptor. , 1994, The Journal of biological chemistry.

[21]  K. Uchida,et al.  Autoxidative degradation of Amadori compounds in the presence of copper ion , 1991 .

[22]  G. Ghiggeri,et al.  Glycosylation of human albumin in diabetes mellitus II. Extensive in vitro modification by trioses and hexoses as revealed by isoelectric focusing , 1985 .

[23]  R. Hoeldtke,et al.  Acetone Metabolism in Humans During Diabetic Ketoacidosis , 1986, Diabetes.

[24]  F. Hayase,et al.  Polymerization of Proteins Caused by Reaction with Sugars and the Formation of 3-Deoxyglucosone under Physiological Conditions , 1988 .

[25]  J. Baynes,et al.  Chemistry of the fructosamine assay: D-glucosone is the product of oxidation of Amadori compounds. , 1994, Clinical chemistry.

[26]  Paul J Thornalley,et al.  Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. , 1994, Clinical science.

[27]  V. Monnier,et al.  Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole. , 1988, The Journal of biological chemistry.

[28]  F. Hayase,et al.  3-Deoxyglucosone Crosslinks Proteins under Physiological Conditions , 1987 .

[29]  S. Karonen,et al.  An enzymatic solid-phase method for trace iodination of proteins and peptides with 125-iodine. , 1975, Analytical biochemistry.

[30]  Paul J Thornalley.  The glyoxalase system in health and disease. , 1993, Molecular aspects of medicine.

[31]  R. Bucala,et al.  Advanced glycation end products contribute to amyloidosis in Alzheimer disease. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[32]  Paul J Thornalley,et al.  Modification of the glyoxalase system in streptozotocin-induced diabetic rats. Effect of the aldose reductase inhibitor Statil. , 1993, Biochemical pharmacology.

[33]  N. Taniguchi,et al.  beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. , 1993, The Journal of clinical investigation.

[34]  Paul J Thornalley,et al.  Mechanism of the degradation of non-enzymatically glycated proteins under physiological conditions. Studies with the model fructosamine, N epsilon-(1-deoxy-D-fructos-1-yl)hippuryl-lysine. , 1992, European journal of biochemistry.

[35]  J. Richard,et al.  Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance. , 1991, Biochemistry.

[36]  S. Ogawa,et al.  Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[37]  J. Baynes,et al.  Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. , 1986, The Journal of biological chemistry.

[38]  Paul J Thornalley,et al.  The assay of methylglyoxal in biological systems by derivatization with 1,2-diamino-4,5-dimethoxybenzene. , 1992, Analytical biochemistry.

[39]  P. Thornalley,et al.  Synthesis and chromatography of 1,2-diamino-4,5-dimethoxybenzene, 6,7-dimethoxy-2-methylquinoxaline and 6,7-dimethoxy-2,3-dimethylquinoxaline for use in a liquid chromatographic fluorimetric assay of methylglyoxal , 1992 .

[40]  J. Baynes,et al.  Oxidative degradation of glucose adducts to protein. Formation of 3-(N epsilon-lysino)-lactic acid from model compounds and glycated proteins. , 1988, The Journal of biological chemistry.

[41]  G. A. Lyles,et al.  The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amine oxidase in human umbilical artery. , 1992, Biochemical pharmacology.

[42]  Paul J Thornalley,et al.  The reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins. , 1994, Biochemical pharmacology.

[43]  T. Lyons,et al.  Role of Glycation in Modification of Lens Crystallins in Diabetic and Nondiabetic Senile Cataracts , 1991, Diabetes.

[44]  A. Cerami,et al.  Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. , 1988, The New England journal of medicine.

[45]  R. MacQuarrie,et al.  A sensitive fluorometric method for the determination of arginine using 9,10-phenanthrenequinone. , 1978, Analytical biochemistry.

[46]  Paul J Thornalley,et al.  The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ions. , 1984 .

[47]  Y. Morino,et al.  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. , 1988, The Journal of biological chemistry.

[48]  T. Lyons,et al.  Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. , 1993, The Journal of clinical investigation.

[49]  R. Bucala,et al.  Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging. , 1994, Laboratory investigation; a journal of technical methods and pathology.

[50]  J. Knowles,et al.  Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. , 1990, Biochemistry.

[51]  S. Ray,et al.  Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone. , 1987, The Journal of biological chemistry.

[52]  R. Cho,et al.  Responsibility of 3-Deoxyglucosone for the Glucose-Induced Polymerization of Proteins , 1987 .

[53]  C. Elmets,et al.  Relation between complications of type I diabetes mellitus and collagen-linked fluorescence. , 1986, The New England journal of medicine.

[54]  D. V. Vander Jagt,et al.  Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. , 1992, The Journal of biological chemistry.

[55]  Paul J Thornalley,et al.  Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin. , 1994, The Journal of biological chemistry.

[56]  K. Manogue,et al.  Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. , 1988, Science.

[57]  Y. Zou,et al.  Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. , 1994, The Journal of biological chemistry.