1. The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells.
- Author
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Zhu, Peiran, Li, Weiwei, Ni, Mengxia, Zhang, Cui, Liu, Shuaimei, Wu, Qiuyue, Jiang, Weijun, Zhang, Jing, Zhang, Mingchao, Li, Xiaojun, Cui, Yingxia, Xue, Chunyan, and Xia, Xinyi
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GENETIC mutation , *CRYSTALLINS , *EPITHELIAL cells , *MISSENSE mutation , *ARGININE , *PROLINE - Abstract
αB-crystallin acts as an anti-apoptosis protein in human lens epithelial (HLE) cells. We recently identified a missense mutation in αB-crystallin that changes proline 20 to an arginine (P20R) in a Chinese family with autosomal dominant congenital posterior polar cataract. The impact of the P20R mutation on the anti-apoptosis function remains unclear. To explore the anti-apoptotic activity of αB-crystallin wild type (αB-wt) and its P20R mutant under oxidative stress, HLE cells were transfected with αB-wt and αB-P20R constructs and expression was measured by western blotting. Flow cytometry and terminal deoxynucleotidyl transferase (TdT)-mediated dUTP digoxigenin nick end-labelling (TUNEL) staining were performed to investigate apoptosis. We found that αB-wt performed a dominant role in inhibiting stress-induced apoptosis, but this function was impeded in cells expressing αB-P20R. The P20R mutant of αB-crystallin exhibits diminished anti-apoptotic activity compared with the native protein. [ABSTRACT FROM AUTHOR]
- Published
- 2017
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