4.4 Article

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

Journal

NEUROSCIENCE LETTERS
Volume 516, Issue 2, Pages 182-187

Publisher

ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2012.03.074

Keywords

Huntington's disease; Endoplasmic reticulum stress; GRP78; Caspase12

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Funding

  1. National Natural Science Foundation of China [30430260, 30671106]
  2. Zhejiang Provincial Natural Science Foundation [Y206764]

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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.

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