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

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. - Highlights: • We identified a novel mutation (P20R) in αB-crystallin. • The mutation decreased anti-apoptotic activity in αB-crystallin, which compared with the native protein. • We speculate that the mutation may influence phosphorylation, especially Ser19.

Authors:
; ; ; ; ; ; ; ; ; ; ; ;
Publication Date:
OSTI Identifier:
22696833
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 483; Journal Issue: 1; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CONGENITAL DISEASES; LENSES; MUTANTS; MUTATIONS

Citation Formats

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. The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells. United States: N. p., 2017. Web. doi:10.1016/J.BBRC.2016.12.121.
Zhu, Peiran, Li, Weiwei, Ni, Mengxia, Zhang, Cui, Liu, Shuaimei, Wu, Qiuyue, Jiang, Weijun, Zhang, Jing, Zhang, Mingchao, Li, Xiaojun, Cui, Yingxia, Xue, Chunyan, & Xia, Xinyi. The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells. United States. doi:10.1016/J.BBRC.2016.12.121.
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. Sun . "The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells". United States. doi:10.1016/J.BBRC.2016.12.121.
@article{osti_22696833,
title = {The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells},
author = {Zhu, Peiran and Li, Weiwei and Ni, Mengxia and Zhang, Cui and Liu, Shuaimei and Wu, Qiuyue and Jiang, Weijun and Zhang, Jing and Zhang, Mingchao and Li, Xiaojun and Cui, Yingxia and Xue, Chunyan and Xia, Xinyi},
abstractNote = {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. - Highlights: • We identified a novel mutation (P20R) in αB-crystallin. • The mutation decreased anti-apoptotic activity in αB-crystallin, which compared with the native protein. • We speculate that the mutation may influence phosphorylation, especially Ser19.},
doi = {10.1016/J.BBRC.2016.12.121},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 483,
place = {United States},
year = {2017},
month = {1}
}