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Beta-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to beta-crystallins insolubilized during cataract.

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