INVITRO GLYCATION AND ACETYLATION (BY ASPIRIN) OF RAT CRYSTALLINS

被引:16
作者
CHERIAN, M
ABRAHAM, EC
机构
[1] Dept. of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta
关键词
D O I
10.1016/0024-3205(93)90478-L
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
In vitro studies with rat lens crystallins were conducted to explore the mechanism by which aspirin (ASA-acetylsalicylic acid) could inhibit cataractogenesis. The purpose of the present study is to show whether gamma-crystallin is the primary target for glycation by glucose and acetylation by ASA. Lens soluble fractions from one and seven month old Sprague-Dawley rats were incubated with 5 mM [C-14]glucose with and without 10 mM ASA. alpha, beta, and gamma-crystallins were separated by molecular sieve HPLC and specific activities of each crystallin determined. In vitro acetylation was also studied by measuring protein bound [C-14]acetyl groups after incubation with [C-14]acetyl ASA. There was 2 to 4-fold faster glycation of gamma-crystallin than all other crystallins from 1-month-old rats and ASA inhibited glycation of gamma-crystallin four times more than that of alpha and beta-crystallins,thus showing preferential glycation of gamma-crystallin and its selective inhibition by ASA. [C-14]acetyl incorporation showed increased acetylation of gamma-crystallin in one month old rats, whereas in older lenses acetylation of other crystallins predominated. Treatment with 10 mM ASA showed 35% decrease in free -NH2 groups but protein thiols remained unchanged.
引用
收藏
页码:1699 / 1707
页数:9
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