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GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins |
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| Authors: | Yufeng Jiang Hailong Lv Min Liao Xiaoyuan Xu Shanshan Huang Huiping Tan Ting Peng Yinong Zhang He Li |
| Affiliation: | 1. Department of Anatomy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China;2. Department of Histology and Embryology, Medical College, Shihezi University, Shihezi, China;3. Department of General Surgery, First Affiliated Hospital, School of Medicine, Shihezi University, Shihezi, China |
| Abstract: | 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. |
| Keywords: | Huntington's disease Endoplasmic reticulum stress GRP78 Caspase12 |
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