Reaction of phenylglyoxal with arginine. The effect of buffers and pH

Cheung, Shu-Tong; Fonda, Margaret L.

doi:10.1016/0006-291x(79)91918-1

Cited by 85 publications

(34 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2C). This result is in agreement with previous reports showing that N ␣ -acetyl-L-arginine did not produce a Schiff base (23,30). Methylglyoxal is also known to react with arginine and cysteine residues in proteins, yielding stable imidazolone and hemithioacetal compounds, respectively (23).…”

Section: Resultssupporting

confidence: 83%

Oxidation-Reduction Properties of Methylglyoxal-modified Protein in Relation to Free Radical Generation

Lee¹,

Yim²,

Chock³

et al. 1998

Journal of Biological Chemistry

143

View full text Add to dashboard Cite

Glycation reaction (nonenzymatic glycosylation; Maillard reaction), which produces brown fluorescent compounds, is a chance event that may occur when a protein is in solution with a reducing sugar, such as glucose. In this reaction, free amino groups of protein react slowly with the carbonyl groups of reducing sugars to yield Schiff-base intermediates, which undergo Amadori rearrangement to stable ketoamine derivatives (1). These Amadori products subsequently degrade into ␣-dicarbonyl compounds, deoxyglucosones (2). Schiff bases can also be fragmented to glyoxal (3). These compounds are more reactive than the parent sugars with respect to their ability to react with amino groups of proteins. Thus, the ␣-dicarbonyl compounds or ␣-ketoaldehydes are mainly responsible for forming inter-and intramolecular cross-links of proteins, known as advanced glycation end products (AGEs) 1 (1). The AGEs, which are irreversibly formed, accumulate with aging, atherosclerosis, and diabetes mellitus, especially associated with long-lived proteins such as collagens, lens crystallins, and nerve proteins (4 -8).The ␣-dicarbonyl compounds are produced in a variety of ways. Fenton reaction-mediated oxidation of sugars, lipids, and proteins produces various ␣-dicarbonyl compounds. Accordingly, the transition metal ion-catalyzed oxidation of glucose is suggested to be a more important factor in glycation than the formation of the Amadori product of glucose itself (9 -11). The ␣-ketoaldehydes, such as methylglyoxal, are also found as a normal metabolite in mammals and microorganisms. The methylglyoxal is formed by the non-enzymatic or enzymatic elimination of phosphate from triose phosphate and by the oxidation of hydroxyacetone and aminoacetone (12-14). The increased formation of methylglyoxal was observed in hyperglycemia associated with diabetes mellitus (15, 16). In addition, it was shown that methylglyoxal-modified albumin underwent receptor-mediated endocytosis by macrophage, which may suggest the involvement of methylglyoxal in pathophysiology (17). Also, it was suggested that cellular oxidant stress or free radicals are generated by AGEs themselves (18,19) or as a consequence of the AGEs interaction with their receptors (20,21).Several AGEs were identified from the products formed during the reaction of methylglyoxal with model compounds and proteins. These species include N ⑀ -(carboxyethyl)lysine (22), imidazolone compounds (23), and imidazolium cross-link species, methylglyoxal-lysine dimer (24 -26). In addition to these AGEs, several investigations have also shown by electron paramagnetic resonance (EPR) spectroscopy that unidentified protein free radicals were produced during the reaction of methylglyoxal with proteins, such as bovine serum albumin (BSA) and casein (27,28). In our previous report (29), the free radical was assigned to be the radical cation of the cross-linked Schiff base on the basis of the detailed analysis of EPR spectra observed from the reaction mixture containing methylglyoxal and alanine. We also sugges...

show abstract

Section: Resultssupporting

confidence: 83%

Oxidation-Reduction Properties of Methylglyoxal-modified Protein in Relation to Free Radical Generation

Lee¹,

Yim²,

Chock³

et al. 1998

Journal of Biological Chemistry

143

View full text Add to dashboard Cite

show abstract

“…There are several possible ways by which intracellular ROS levels could be increased by MG. One is that ROS are produced during the glycation reaction of amino acids or proteins with MG. Another is that the glutathione content of cells are depleted during MG metabolism by the glyoxalase system and the cells, therefore, cannot efficiently eliminate ROS. Another possible mechanism is that MG modifies and inactivates enzymes which scavenge ROS, such as superoxide dismutases, glutathione peroxidases, and glutathione transferases because MG is able to bind to and modify arginine, lysine, and cysteine residues in proteins (45,46). Surprisingly, after treatment with 3-DG, a more rapid increase of intracellular peroxide was observed in RASMC (Fig.…”

Section: Discussionmentioning

confidence: 99%

Selective Induction of Heparin-binding Epidermal Growth Factor-like Growth Factor by Methylglyoxal and 3-Deoxyglucosone in Rat Aortic Smooth Muscle Cells

Che

Asahi

Takahashi

et al. 1997

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

Methylglyoxal (MG) and 3-deoxyglucosone (3-DG), reactive dicarbonyl metabolites in the glyoxalase system and glycation reaction, respectively, selectively induced heparin-binding epidermal growth factor (HB-EGF)-like growth factor mRNA in a dose-and time-dependent manner in rat aortic smooth muscle cells (RASMC). A nuclear run-on assay revealed that the dicarbonyl may regulate expression of HB-EGF at the transcription level. The dicarbonyl also increased the secretion of HB-EGF from RASMC. However, platelet-derived growth factor, another known growth factor of smooth muscle cells (SMC), was not induced by both dicarbonyls. The dicarbonyl augmented intracellular peroxides prior to the induction of HB-EGF mRNA as judged by flow cytometric analysis using 2 ,7 -dichlorofluorescin diacetate. N-Acetyl-L-cysteine and aminoguanidine suppressed both dicarbonyl-increased HB-EGF mRNA and intracellular peroxide levels in RASMC. DL-Buthionine-(S,R)-sulfoximine increased the levels of 3-DG-induced HB-EGF mRNA. Furthermore, hydrogen peroxide alone also induced HB-EGF mRNA in RASMC. These results indicate that MG and 3-DG induce HB-EGF by increasing the intracellular peroxide levels. In addition, the pretreatment with 12-O-tetra-decanoylphorbol-13-acetate failed to alter dicarbonyl-induced HB-EGF mRNA expression in RASMC, suggesting that the signal transducing mechanism is not mediated by protein kinase C. Since HB-EGF is known as a potent mitogen for smooth muscle cells and is abundant in atherosclerotic plaques, the induction of HB-EGF by MG and 3-DG, as well as the concomitant increment of intracellular peroxides, may trigger atherogenesis during diabetes.Methylglyoxal (2-oxopropanal; MG), 1 a reactive ␣,␤-dicarbonyl metabolite and physiological substrate for the glyoxalase system (1), is formed by the non-enzymatic and enzymatic elimination of phosphate from dihydroxyacetone phosphate, glyceraldehyde-3-phosphate (2, 3), and by the oxidation of hydroxyacetone and aminoacetone (4 -6). The estimated rate of formation of methylglyoxal in tissues of normal healthy subjects is approximately 125 M/day which can largely be accounted for as a result of fragmentation of triose phosphates (2). The glyoxalase system, using reduced glutathione as a cofactor, catalyzes the conversion of methylglyoxal to D-lactate via the intermediate S-D-lactoylglutathione. The formation of methylglyoxal in cultured human red blood cells is increased under hyperglycemic conditions and by the addition of fructose,

show abstract

“…Methylglyoxal reacts with arginine and arginyl residues in proteins (Takahashi, 1977a,b;Cheung & Fonda, 1979). Methylglyoxal (> 10 mM) inhibits glycolytic enzymes (Leonici et al, 1989) and inhibits microtubule assembly (Miglietta & Gabriel, 1986).…”

Section: Reaction Of Methylglyoxal With Biological Moleculesmentioning

confidence: 99%

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

Thornalley

1990

Biochemical Journal

716

502

View full text Add to dashboard Cite

Reaction of phenylglyoxal with arginine. The effect of buffers and pH

Cited by 85 publications

References 19 publications

Oxidation-Reduction Properties of Methylglyoxal-modified Protein in Relation to Free Radical Generation

Oxidation-Reduction Properties of Methylglyoxal-modified Protein in Relation to Free Radical Generation

Selective Induction of Heparin-binding Epidermal Growth Factor-like Growth Factor by Methylglyoxal and 3-Deoxyglucosone in Rat Aortic Smooth Muscle Cells

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

Contact Info

Product

Resources

About