Abstract
ICR/f mutation in rat, an inherited disorder, is characterized by the development of cataracts. In this study, we analuzed and compared the crystallins in normal and cataractous rat lenses using gel filtration and two-dimensional gel electrophoresis, and determined the transglutaminase activities and Ca2+ content in the mutant and normal lenses. The Ca2+ content about 10-fold and the activity of transglutaminase was about 1.8-fold higher in the cataractous lenses than in the normal lenses. Analysis of the cataractous lens proteins showed a remarkable decrease in γ-, βB1-, βA3-, and βA4-crystallin content, accompanied with some increase in α-crystallin (or its aggregate). Higher molecular weight proteins were also observed in the cateractous lenses, with molecular masses which correspond to those fo cross-linked dimera (43 to 55 kDa) of β-crystallins. We consider that the mutation accelerates the aggregation of the crystallins, which is assosiated with their cross-linking by transglutaminase.
