Mechanism of Cataract Formation in A-crystallin Y 118 D Mutation

RESULTS. Both native -crystallin from mutant lens and recombinant A-Y118D displayed higher molecular mass distribution than the wild-type. Circular dichroism spectra indicated changes in the secondary structures of A-Y118D. The AY118D protein prevented nonspecific protein aggregation more effectively than wild-type A-crystallin. The gel filtration and 2D gel electrophoresis analysis showed a significant reduction of Y118D mutant protein in comparison with wild-type A protein of heterozygous mutant lenses. Quantitative RT-PCR results confirmed a decrease in A and B transcripts in the homozygous mutant A(Y118D/Y118D) lenses.