Home LiteratureArticle Details
PMID: 16417581 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Wild-type huntingtin protects neurons from excitotoxicity.

Journal of neurochemistry ·Vol. 96 ·No. 4 ·2006-02-00 ·Pages 1121-9

Leavitt BR, van Raamsdonk JM, Shehadeh J, Fernandes H, Murphy Z, Graham RK, Wellington CL, Raymond LA, Hayden MR

Abstract

Huntingtin is a caspase substrate, and loss of normal huntingtin function resulting from caspase-mediated proteolysis may play a role in the pathogenesis of Huntington disease. Here we tested the hypothesis that increasing huntingtin levels protect striatal neurons from NMDA receptor-mediated excitotoxicity. Cultured striatal neurons from yeast artificial chromosome (YAC)18 transgenic mice over-expressing full-length wild-type huntingtin were dramatically protected from apoptosis and caspase-3 activation compared with cultured striatal neurons from non-transgenic FVB/N littermates and YAC72 mice expressing mutant human huntingtin. NMDA receptor activation induced by intrastriatal injection of quinolinic acid initiated a form of apoptotic neurodegeneration within the striatum of mice that was associated with caspase-3 cleavage of huntingtin in neurons and astrocytes, decreased levels of full-length huntingtin, and the generation of a specific N-terminal caspase cleavage product of huntingtin. In vivo, over-expression of wild-type huntingtin in YAC18 transgenic mice conferred significant protection against NMDA receptor-mediated apoptotic neurodegeneration. These data provide in vitro and in vivo evidence that huntingtin may regulate the balance between neuronal survival and death following acute excitotoxic stress, and that the levels of huntingtin may modulate neuronal sensitivity to excitotoxic neurodegeneration. We suggest that further study of huntingtin's anti-apoptotic function will contribute to our understanding of the pathogenesis of Huntingdon's disease and provide insights into the selective vulnerability of striatal neurons to excitotoxic cell death.

MeSH Terms
Animals Apoptosis/drug effects Caffeine/pharmacology Caspase 3 Caspases/metabolism Chromosomes, Artificial, Yeast Humans Huntingtin Protein Mice Mice, Transgenic N-Methylaspartate/pharmacology Nerve Tissue Proteins/pharmacology Neurons/cytology,drug effects,physiology Neurotoxins/pharmacology Nuclear Proteins/pharmacology Recombinant Proteins/pharmacology Staurosporine/pharmacology
Chemicals
HTT protein, human Huntingtin Protein Nerve Tissue Proteins Neurotoxins Nuclear Proteins Recombinant Proteins Caffeine N-Methylaspartate CASP3 protein, human Casp3 protein, mouse Caspase 3 Caspases Staurosporine
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Leavitt Blair R
Centre for Molecular Medicine and Therapeutics, British Colombia Research Institute for Children's and Women's Health, Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia, Canada. [email protected]
van Raamsdonk Jeremy M
Shehadeh Jacqueline
Fernandes Herman
Murphy Zoe
Graham Rona K
Wellington Cheryl L
Raymond Lynn A
Hayden Michael R
Article Info
Journal
Journal of neurochemistry
Abbr.
J Neurochem
ISSN
0022-3042
Published
2006-02-00
Epub
2006-00-17
Pages
1121-9
Language
English
Region
England
NLM ID
2985190R
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]