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J. Liu, L. Gong, M. Deng, D. Yuan, L. Zhang, S. Sun, H. Ma, D. Li; Alpha-Crystallins Interact With Caspase-3 and Bax in vitro and in vivo to Prevent Stress-Induced Apoptosis and Cataractogenesis. Invest. Ophthalmol. Vis. Sci. 2010;51(13):6362.
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© ARVO (1962-2015); The Authors (2016-present)
Previous studies from our lab and others have shown that alpha-crystallins can regulate members in both caspase and Bcl-2 families to prevent stress-induced apoptosis, which leads to cataractogenesis. However, the exact mechanisms by which alpha-crystallins regulate these members remain uncertain. In the present study, we examined the interactions between alpha-crystallins and Caspase-3 as well as Bax to explore how alpha-crystallins regulate stress-induced apoptosis.
Cell flow cytometry and MTT assays were used to detect apoptosis. In vitro binding assay, surface plasmon resonance, co-immunoprecipitation, and yeast two hybrid selection were used to detect the interactions between alpha-crystallins and caspase-3 as well as Bax.
Both alpha-crystallins interact with caspase-3 and Bax in vitro. AlphaB-crystallin display stronger affinity to caspase-3 than alphaA-crystallin does. The interacting complexes between alpha-crystallins and caspase-3/Bax were detected in both lens epithelial cell lines and also in developing and adult lenses.
alpha-crystallins directly interact with Caspase-3 as well as Bax to prevent stress-induced apoptosis.
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