Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5505618 | Biochemical and Biophysical Research Communications | 2017 | 5 Pages |
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.
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Authors
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,