Document Detail


Glycation-induced inactivation of aspartate aminotransferase, effect of uric acid.
MedLine Citation:
PMID:  16180093     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glycation is common posttranslational modification of proteins impairing their function, which occurs during diabetes mellitus and aging. Beside extracellular glycation of long-lived proteins, intracellular modifications of short-lived proteins by more reactive sugars like fructose are possible. The process includes free oxygen radicals (glycoxidation). In an attempt to reduce glycoxidation and formation of advanced glycation products (AGE), influence of 0.2-1.2 mM uric acid as endogenous antioxidant on glycoxidation of purified pig heart aspartate aminotransferase (AST) by 50 mM and 500 mM D-fructose in vitro was studied. Uric acid at 1.2 mM concentration reduced AST activity decrease and formation of total AGE products caused by incubation in vitro of the enzyme with sugar up to 25 days at 37 degrees C. The results thus support the hypothesis that uric acid has beneficial effects in controlling protein glycoxidation. The in vitro system AST-fructose proved to be a useful tool for investigation of glycation process.
Authors:
Iva Bousová; Hilaire Bakala; Robert Chudácek; Vladimír Palicka; Jaroslav Drsata
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular and cellular biochemistry     Volume:  278     ISSN:  0300-8177     ISO Abbreviation:  Mol. Cell. Biochem.     Publication Date:  2005 Oct 
Date Detail:
Created Date:  2005-09-23     Completed Date:  2006-01-17     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0364456     Medline TA:  Mol Cell Biochem     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  85-92     Citation Subset:  IM    
Affiliation:
Department of Biochemical Sciences, Faculty of Pharmacy, Charles University in Prague, Czech Republic. bousova@faf.cuni.cz
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MeSH Terms
Descriptor/Qualifier:
Aspartate Aminotransferases / chemistry,  metabolism*
Dose-Response Relationship, Drug
Fructose / metabolism
Glycosylation End Products, Advanced / metabolism*
Time Factors
Uric Acid / metabolism,  pharmacology*
Chemical
Reg. No./Substance:
0/Glycosylation End Products, Advanced; 30237-26-4/Fructose; 69-93-2/Uric Acid; EC 2.6.1.1/Aspartate Aminotransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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