β‐Crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β‐crystallins insolubilized during cataract

FEBS Letters

David, Larry L.¹  Shearer, Thomas R.¹ 

[1] Departments of Oral Molecular Biology,Oregon Health Sciences University, Portland, OR 97201, USA

关键词: Crystallin;    Cataract;    Calpain;   

DOI  :  10.1016/0014-5793(93)80131-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Incubation of soluble proteins from rat lens with the protease calpain II caused the precipitation of β-crystallin polypeptides. Two-dimensional electrophoresis and sequence analysis identified β-crystallin polypeptides both before and after their precipitation by calpain II. β-crystallin polypeptides precipitated by calpain were cleaved at their NH₂-terminal extensions. These cleavage sites were similar to cleavage sites occurring in β-crystallin polypeptides precipitated during formation of experimental cataract induced by an overdose of selenite. These data suggested that calpain II caused β-crystallin insolubilization during cataract formation, and indicated that the process can be mimicked in vitro.

【 授权许可】

Unknown