正常大鼠和遗传性白内障大鼠αA-晶体蛋白翻译后修饰的比较。

Comparison of post-translational modifications of alpha A-crystallin from normal and hereditary cataract rats.

作者信息

Fujii N, Takeuchi N, Fujii N, Tezuka T, Kuge K, Takata T, Kamei A, Saito T

机构信息

Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan.

出版信息

Amino Acids. 2004 Mar;26(2):147-52. doi: 10.1007/s00726-003-0050-8. Epub 2003 Dec 18.

DOI:10.1007/s00726-003-0050-8

PMID:15042443

Abstract

In order to investigate the relationship between lens opacities and the various modifications of lens proteins, we analyzed and compared the properties of lens proteins of 85-day old normal Wistar rats and the hereditary cataract model, ICR/f rats. The present study identified many differences between normal and mutant lens proteins. In the ICR/f mutant rats, the relative amounts of gamma-crystallin decreased and high molecular weight (HMW) protein increased. Racemization and isomerization of Asp-151 of alpha A-crystallin was observed in the mutant ICR/f rats, and Met-1 of alpha A-crystallin was oxidized to methionine sulfoxide. These modifications were not found in the age-matched normal rats. These tendencies are consistent with aged and cataractous human lenses.

摘要

为了研究晶状体混浊与晶状体蛋白各种修饰之间的关系，我们分析并比较了85日龄正常Wistar大鼠和遗传性白内障模型ICR/f大鼠的晶状体蛋白特性。本研究确定了正常和突变晶状体蛋白之间的许多差异。在ICR/f突变大鼠中，γ-晶状体蛋白的相对含量降低，高分子量（HMW）蛋白增加。在突变的ICR/f大鼠中观察到αA-晶状体蛋白的Asp-151发生消旋化和异构化，并且αA-晶状体蛋白的Met-1被氧化为甲硫氨酸亚砜。在年龄匹配的正常大鼠中未发现这些修饰。这些趋势与老年人和白内障患者的晶状体一致。