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Huntingtin aggregation and toxicity in Huntington's disease.
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- Author(s): Bates, Gillian
- Source:
Lancet. 5/10/2003, Vol. 361 Issue 9369, p1642. 3p. 1 Diagram.- Subject Terms:
- Source:
- Additional Information
- Abstract: Huntington's disease is a late onset neurodegenerative disorder for which the mutation is a CAG/polyglutamine (polyQ) repeat expansion in the gene encoding the huntingtin protein. In 1993 the Huntington's disease mutation was found to be a CAG repeat expansion in exon 1 of the Huntington's disease gene that encodes a stretch of polyglutamine (polyQ) residues close to the N-terminus of the huntingtin protein. Only in 1997 were polyQ aggregates reported in the brains of transgenic mice with Huntington's disease, in the form of nuclear inclusions, 3 and in the postmortem brains from patients with spinocerebellar ataxia 3 4 or Huntington's disease, 5 in the form of nuclear inclusions and dystrophic neurites. Whether the critical concentration of the aggregate precursor is ever reached in a given cell (likely to confer cell specificity) could be influenced by many factors, including the ability of the cell to divide, cell-specific expression levels, subcellular compartmentalisation, and differential processing of the full-length protein (the precursor for aggregation in Huntington's disease is likely to be an N-terminal fragment). Work in the author's laboratory is supported by grants from the Wellcome Trust, Hereditary Disease Foundation, Huntington's Disease Society of America, and Human Frontiers Science Program.
- Abstract:
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