The influence of selenium and neuroleptics on the rat brain nuclear regulatory mechanism in carcinogenesis

alpha-Crystallins possess molecular chaperone properties and are one of the most abundant of the lenticular proteins. Posttranslational modifications of these proteins have been implicated as a possible etiology of human cataracts. This article will review current knowledge concerning the effects of known posttranslational modifications upon the molecular chaperone properties and aggregation behavior of alpha-A and alpha-B crystallin. Based upon these effects, experimental approaches will be discussed that may be useful in the development of reagents that may selectively inhibit the cataractogenic process in the aging human lens.