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N. Senda, N. Katai, T. Yanagidaira, T. Kyomoto, T. Murata; Nonrefractive Role of BetaB2–Crystallin . Invest. Ophthalmol. Vis. Sci. 2006;47(13):2016.
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© ARVO (1962-2015); The Authors (2016-present)
Although ß and γ–Crystallin had been considered to be structure proteins of the lens, recent studies reported that ß and γ–Crystallin families are expressed in many non–lens tissues. However, the function of ß and γ–Crystallin expressed in extralenticular tissues is unknown. In this study, we investigated the nonrefractive role of the ß B2–Crystallin.
Lens epithelial cells isolated from porcine lens and 293 cells were cultured in DMEM with 10% FBS. Cellular localization of ßB2–Crystallin was examined by using anti– ßB2–Crystallin antibody and α–actin antibody. GFP tagged–ßB2–Crystallin plasmid was transfected to cells and dynamic translocation was observed under the fluorescence biomicroscope after stimulation of growth factors.
ßB2–Crystallin was strongly localized to the leading edges of cultured lens epithelial cells and colocalized with actin. GFP tagged–ßB2–Crystallin was translocated to the leading edge of migrating lens epithelial cells after stimulation.
Our studies suggested that ßB2–Crystallin was related with actin polymerization during cell migration, changing of cell shape and cytoskeletal organization.
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