Alpha-crystallin acting as a molecular chaperone protects catalase against steroid-induced inactivation

被引：40

作者：

Hook, DWA ^{[1
]}

Harding, JJ ^{[1
]}

机构：

[1] UNIV OXFORD,NUFFIELD LAB OPHTHALMOL,OXFORD OX2 6AW,ENGLAND

来源：

FEBS LETTERS | 1996年 / 382卷 / 03期

关键词：

catalase; prednisolone-21-hemisuccinate; alpha-crystallin; steroid-induced cataract; chaperone;

D O I：

10.1016/0014-5793(96)00134-2

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：

A link between corticosteroid therapy and the development of cataract has been known for many Sears. However, the precise underlying molecular mechanism of pathology has not been characterised, although a role for direct deleterious interactions between corticosteroids and lenticular proteins has been investigated. alpha-Crystallin is a major lens protein that has exhibited chaperone properties in vitro. Catalase is a ubiquitous enzyme that is an important scavenger of hydrogen peroxide in vivo. The corticosteroid prednisolone-21-hemisuccinate was found to inactivate bovine liver catalase, in vitro in a progressive manner. Coincubation of alpha-crystallin with catalase in a 1:2 molar ratio (one alpha-crystallin to two catalase molecules) fully protected against this inactivation. The protection was specific. Aspirin-like analgesics, putative anti-cataract drugs offered no such protection.

引用

页码：281 / 284

页数：4

共 33 条

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