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
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
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页码:281 / 284
页数:4
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