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Neurosci Lett. 2012 May 16;516(2):182-7. doi: 10.1016/j.neulet.2012.03.074. Epub 2012 Apr 2.

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

Author information

1
Department of Anatomy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 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.

PMID:
22490889
DOI:
10.1016/j.neulet.2012.03.074
[Indexed for MEDLINE]

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