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Updated: May 23, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins
Yufeng Jiang1, Hailong Lv, Min Liao
1Department 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.
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