Glycation of aspartate aminotransferase by methylglyoxal, effect of hydroxycitric and uric acid
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Bousova, Iva
[1
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Bacilkova, Eliska
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Charles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech RepublicCharles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech Republic
Bacilkova, Eliska
[1
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Dobrijevic, Sanja
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Charles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech RepublicCharles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech Republic
Dobrijevic, Sanja
[1
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Drsata, Jaroslav
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Charles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech RepublicCharles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech Republic
Drsata, Jaroslav
[1
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[1] Charles Univ Prague, Dept Biochem Sci, Fac Pharm Hradec Kralove, Hradec Kralove 50005, Czech Republic
Glycation is a process closely related to the aging and pathogenesis of diabetic complications. Reactive alpha-dicarbonyl compounds (e.g., methylglyoxal) are formed during middle stage of glycation reaction. Compounds that would inhibit the glycation process have been seeked for years. The objective of this study was to investigate the inhibitory effect of hydroxycitric (0.25-2.5 mM) and uric acid (0.4-1.2 mM) on middle stage of protein glycation in vitro using the model containing aspartate aminotransferase (AST) and 0.5 mM methylglyoxal. Hydroxycitric acid, at all tested concentrations, reduced AST activity decrease and formation of fluorescent AGEs during incubation of the enzyme with methylglyoxal at 37A degrees C. This compound also prevented formation of high-molecular weight protein cross-links and changes in molecular charge of AST caused by glycation. Uric acid showed no positive anti-glycation activity. The results support the hypothesis that hydroxycitric acid has beneficial effects in controlling protein glycation.