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JOURNAL ARTICLE

The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells

Peiran Zhu, Weiwei Li, Mengxia Ni, Cui Zhang, Shuaimei Liu, Qiuyue Wu, Weijun Jiang, Jing Zhang, Mingchao Zhang, Xiaojun Li, Yingxia Cui, Chunyan Xue, Xinyi Xia
Biochemical and Biophysical Research Communications 2017 January 29, 483 (1): 463-467
28007594
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.

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