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

FEBS Letters

Hook, Darren W.A.¹  Harding, John J.¹ 

[1] Nuffield Laboratory of Ophthalmology, University of Oxford, Walton Street, Oxford OX2 6AW, UK

关键词: Catalase;    Prednisolone-21-hemisuccinate;    α-Crystallin;    Steroid-induced cataract;    Chaperone;   

DOI  :  10.1016/0014-5793(96)00134-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A link between corticosteroid therapy and the development of cataract has been known for many years. 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. α-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 α-crystallin with catalase in a 1:2 molar ratio (one α-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.

【 授权许可】

Unknown