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J.-P. Liu, J. Qin, Q. Yan, H.-G. Chen, D. W. Li; Alpha-Crystallins Modulate P53 Phosphorylation Status to Attenuate Uva-Induced Apoptosis. Invest. Ophthalmol. Vis. Sci. 2007;48(13):2425.
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UVA-induced apoptosis is linked to cataractogenesis of the ocular lens. The ocular lens normally guards apoptosis of the lens epithelial cells through the function of the lens structure proteins, alpha-crystallins. In our previous studies, we have demonstrated that alpha-crystallins can negatively regulate UVA-induced apoptosis through suppression of the ERK-mediated pathway and activation of the AKT signaling pathway. In the present study, we present evidence to show that alpha-crystallins can modulate the phosphorylation status of the tumor suppressor, p53 to antagonize UVA-induced apoptosis.
UVA was used to irradiate human lens epithelial cells stably expressing GFP vector, HαA-GFP, and HαB-GFP fusion proteins. Western blot analysis was used for detection of p53 phosphorylation status. Hochst staining was used for apoptosis assay.
Human lens epithelial cells expressing either alphaA- or alphaB-crystallin are substantially resistant to UVA-induced apoptosis. UVA-induces distinct phosphorylation of p53 at Ser-15 in vector-transfected cells. However, in alphaA- or alphaB-crystallin-transfected cells, phosphorylation of p53 at Ser-15 was distinctly attenuated.
Alpha-crystallins prevent UVA-induced apoptosis at multiple signaling transduction pathways.
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