A study of beta-crystallin aggregation and insolubilization as it occurs in mammalian lenses during normal aging and cataractogenesis is proposed. Biological probes in the form of monoclonal and/or monospecific polyclonal antibodies to native crystallins or synthetic polypeptides will be used to track specific beta- crystallin subunits as aggregation proceeds in vivo or as reaggregation of isolated subunits takes place in vitro. The influence of calcium on aggregation and whether or not degradation of subunits accompanies aggregation will be monitored. The composition of beta-crystallin aggregates in such cataractous lenses as occur in galactose fed rats, diabetic, hypermature and senile human lenses will be determined by comparison of microdissected opaque regions to adjacent nonopaque regions.
