Calpain-induced light scattering in young rat lenses is enhanced by UV-B

Journal of Ocular Pharmacology and Therapeutics : the Official Journal of the Association for Ocular Pharmacology and Therapeutics
Y NakamuraT R Shearer

Abstract

The purpose of this study is to determine if UV-B enhances light scattering after proteolysis of crystallins by calpains, and to determine if lens-specific calpain Lp82 is involved, along with m-calpain, in the mechanism of in vitro precipitation. Lens soluble proteins from young rats were hydrolyzed for 24 hr by endogenous lens calpains, and the proteins were further incubated for up to 7 days with periodic irradiation by UV-B. Light scattering was measured daily at 405 nm. SDS-PAGE and immunoblotting assessed proteolysis of crystallins, activation of calpains, and formation of high molecular weight aggregations. Appreciable light scattering occurred in lens soluble proteins after proteolysis of crystallins by m-calpain and Lp82. UV-B markedly enhanced this light scattering and the formation of higher molecular weight aggregates consisting of proteolyzed alpha- and beta- and intact gamma-crystallins. Calpain inhibitor E64 and antioxidants DTE or GSH prevented the light scattering. These results show that calpain-induced light scattering is enhanced by the natural oxidant UV-B. Activation of Lp82, along with m-calpain, contributed to the light scattering. The linkage between proteolysis and oxidation is important because both o...Continue Reading

References

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Jul 23, 1999·Current Eye Research·Y NakamuraT R Shearer

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Citations

Jul 3, 2007·Chemical & Pharmaceutical Bulletin·Chiharu Kimura, Kakuji Tojo

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