FEBS Letters | |
Alpha‐crystallin acting as a molecular chaperone protects catalase against steroid‐induced inactivation | |
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
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020302488ZK.pdf | 449KB | download |