GLYCATION (NONENZYMATIC GLYCOSYLATION) INACTIVATES GLUTATHIONE-REDUCTASE

被引:122
作者
BLAKYTNY, R
HARDING, JJ
机构
[1] Nuffield Laboratory of Ophthalmology, Oxford OX2 6AW, Walton Street
关键词
D O I
10.1042/bj2880303
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Non-enzymic binding of sugars to proteins (glycation) is a common biological phenomenon that is increased in diabetes. Most work has been directed towards strUCtural proteins which may be present for many years and would continue to accumulate sugar residues. As glycation is a non-specific reaction, other proteins Such as enzymes will also be susceptible to glycation and could well display altered activity. We investigated the effect of various sugars whose concentrations increase in diabetes in insulin-independent tissues On glutathione reductase, an enzyme that maintains the GSH level in cells. Glucose, glucose 6-phosphate and fructose all displayed a time-dependent inhibition of glutathione reductase activity, suggesting that these sugars glycate this enzyme. Aspirin gave some protection against the loss of activity induced by glucose.
引用
收藏
页码:303 / 307
页数:5
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