Literature DB >> 22490889

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

Yufeng Jiang1, Hailong Lv, Min Liao, Xiaoyuan Xu, Shanshan Huang, Huiping Tan, Ting Peng, Yinong Zhang, He Li.   

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.
Copyright © 2012 Elsevier Ireland Ltd. All rights reserved.

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Year:  2012        PMID： 22490889     DOI： 10.1016/j.neulet.2012.03.074

Source DB:  PubMed          Journal:  Neurosci Lett        ISSN： 0304-3940            Impact factor:   3.046


  24 in total

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