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Analysis of oxidative events induced by expanded polyglutamine huntingtin exon 1 that are differentially restored by expression of heat shock proteins or treatment with an antioxidant

Firdaus, Wance J.J., Wyttenbach, Andreas, Diaz-Latoud, Chantel, Currie, R.W. and Arrigo, André-Patrick (2006) Analysis of oxidative events induced by expanded polyglutamine huntingtin exon 1 that are differentially restored by expression of heat shock proteins or treatment with an antioxidant Febs Journal, 273, (13), pp. 3076-3093. (doi:10.1111/j.1742-4658.2006.05318.x).

Record type: Article

Abstract

We recently reported that the transient expression of polyglutamine tracts of various size in exon 1 of the huntingtin polypeptide (httExl) generated abnormally high levels of intracellular reactive oxygen species that directly contributed to cell death. Here, we compared the protection generated by heat shock proteins to that provided by the antioxidant agent N-acetyl-L-cysteine. In cells expressing httExl with 72 glutamine repeats (httEx1-72Q), the overexpression of Hsp27 or Hsp70 plus Hdj-1(Hsp40) or treatment of the cells with N-acetyl-L-cysteine inhibited not only mitochondrial membrane potential disruption but also the increase in reactive oxygen species, nitric oxide and protein oxidation. However, only heat shock proteins and not N-acetyl-L-cysteine reduced the size of the inclusion bodies formed by httExl-72Q. In cells expressing httExl polypeptide with 103 glutamine repeats (httEx1-103Q), heat shock proteins neither decreased oxidative damage nor reduced the size of the inclusions. In contrast, N-acetyl-L-cysteine still efficiently decreased the oxidative damage induced by httExl-103Q polypeptide without altering the inclusions. N-Acetyl-L-cysteine was inactive with regard to proteasome inhibition, whereas heat shock proteins partially restored the caspase-like activity of this protease. These observations suggest some relationships between the presence of inclusion bodies and the oxidative damage induced by httExl-polyQ.

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Published date: 1 July 2006
Keywords: heat shock proteins, huntingtin polyQ inclusion bodies, oxidized proteins, proteasome, reactive oxygen species

Identifiers

Local EPrints ID: 56594
URI: http://eprints.soton.ac.uk/id/eprint/56594
ISSN: 1742-464X
PURE UUID: 123e40a8-ca6b-4057-8011-aa58537f5b03

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Date deposited: 06 Aug 2008
Last modified: 17 Jul 2017 14:30

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Contributors

Author: Wance J.J. Firdaus
Author: Andreas Wyttenbach
Author: Chantel Diaz-Latoud
Author: R.W. Currie
Author: André-Patrick Arrigo

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