Changes of lens crystallins photosensitized with tryptophan metabolites.
The effect of UV irradiation on bovine lens soluble proteins (crystallins) in the presence of tryptophan metabolites was investigated in vitro. The cross-linking of crystallins by UV irradiation was accelerated by kynurenine, 3-hydroxykynurenine, anthranilic acid and 3-hydroxyanthranilic acid. On denaturation of crystallins by photooxidation, alpha-crystallin was characterized by the formation of water-soluble HMW (high molecular weight) protein, while water-insoluble HMW protein was produced from beta- and gamma-crystallin. These HMW aggregates showed cross-linking by non-disulfide covalent bonds. LMW (low molecular weight) peptides were formed by degradation of alpha- and beta-crystallin.
Ichijima
H
H
Department of Biophysical Chemistry, Faculty of Pharmaceutical Sciences, Meijo University, Nagoya, Japan.
Iwata
S
S
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000378:metabolism*; D007908:Lens, Crystalline / Q000378:metabolism*; D011838:Radiation-Sensitizing Agents / Q000494:pharmacology*; D012995:Solubility; D014364:Tryptophan / Q000378:metabolism*; D014466:Ultraviolet Rays
D003459:Crystallins; D011838:Radiation-Sensitizing Agents; D014364:Tryptophan