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Alpha‐crystallin acting as a molecular chaperone protects catalase against steroid‐induced inactivation
Author(s) -
Hook Darren W.A.,
Harding John J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00134-2
Subject(s) - catalase , in vivo , chemistry , hydrogen peroxide , peroxidase , biochemistry , reactive oxygen species , in vitro , chaperone (clinical) , pharmacology , enzyme , biology , medicine , pathology , microbiology and biotechnology
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.