The crystallins of the aging human lens become progressively
pigmented, cross-linked, oxidized, and fragmented with age, and it is
generally thought that these modifications predispose the lens toward
formation of senile cataract. Saxena et al. (p. 1473) have tested the
hypothesis that Nε-carboxymethyl-l-lysine
(CML), a modification occurring in aging lens crystallins, can bind
redox active copper due to its EDTA-like structure. The authors find
that copper content and copper binding by CML-rich lens crystallin
extracts from senile cataracts are increased, and that the crystallin
copper complexes can oxidize ascorbic acid. When crystallins are
modified by ascorbic acid degradation products, they form CML and bind
redox active copper. The occurrence of this process in the aging human
lens may lead to a vicious cycle consisting of glycoxidation,
lipoxidation, and metal binding.