GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins

被引：38
作者：
Jiang, Yufeng [2 ]
Lv, Hailong [3 ]
Liao, Min
Xu, Xiaoyuan
Huang, Shanshan
Tan, Huiping
Peng, Ting
Zhang, Yinong
Li, He [1 ]
机构：
[1] Huazhong Univ Sci & Technol, Tongji Med Coll, Dept Anat, Div Histol & Embryol, Wuhan 430030, Peoples R China
[2] Shihezi Univ, Coll Med, Dept Histol & Embryol, Shihezi, Peoples R China
[3] Shihezi Univ, Sch Med, Affiliated Hosp 1, Dept Gen Surg, Shihezi, Peoples R China
来源：
NEUROSCIENCE LETTERS | 2012年 / 516卷 / 02期
基金：
中国国家自然科学基金;
关键词：
Huntington's disease; Endoplasmic reticulum stress; GRP78; Caspase12; NEURONAL INTRANUCLEAR INCLUSIONS; ENDOPLASMIC-RETICULUM; ER STRESS; OXIDATIVE STRESS; BREAST-CANCER; CASPASE-12; ACTIVATION; RESISTANCE; INDUCTION; DISEASE;
D O I：
10.1016/j.neulet.2012.03.074
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
The ER-localized chaperone glucose-regulated protein (GRP78) protects neurons against excitotoxicity and apoptosis. Here we show that overexpressing GRP78 protects N2a cells against mutant huntingtin proteins, reduces formation of mutant huntingtin aggregates, inhibits caspase-12 activation and blocks cell death. Our data suggest that GRP78 may be a promising therapeutic target for the treatment of Huntington's disease. (c) 2012 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码：182 / 187
页数：6
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