The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
Open accessAbstract
Neuronal loss and intraneuronal protein aggregates are characteristics of Huntington's disease (HD), which is one of 10 known neurodegenerative disorders caused by an expanded polyglutamine [poly(Q)] tract in the disease protein. N-terminal fragments of mutant huntingtin produce intracellular aggregates and cause toxicity. Several studies have shown that chaperones suppress poly(Q) aggregation and toxicity/cell death, but the mechanisms by which they prevent poly(Q)-mediated cell death remain unclear. In the present study, we identified heat shock protein 27 (HSP27) as a suppressor of poly(Q) mediated cell death, using a cellular model of HD. In contrast to HSP40/70 chaperones, we showed that HSP27 suppressed poly(Q) death without suppressing poly(Q) aggregation. We tested the hypotheses that HSP27 may reduce poly(Q)-mediated cell death either by binding cytochrome c and inhibiting the mitochondrial death pathway or by protecting against reactive oxygen species (ROS). While poly(Q)-induced cell death was reduced by inhibiting cytochrome c (cyt c) release from mitochondria, protection by HSP27 was regulated by its phosphorylation status and was independent of its ability to bind to cyt c. However, we observed that mutant huntingtin caused increased levels of ROS in neuronal and non-neuronal cells. ROS contributed to cell death because both N-acetyl-L-cysteine and glutathione in its reduced form suppressed poly(Q)-mediated cell death. HSP27 decreased ROS in cells expressing mutant huntingtin, suggesting that this chaperone protects cells against oxidative stress. We propose that a poly(Q) mutation can induce ROS that directly contribute to cell death and that HSP27 is an antagonist of this process.
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Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142
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Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985
Self-citationAgeing and neuronal vulnerability
Mattson, M. P., & Magnus, T. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1886 · Cited by 957
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Schmitt, E., Gehrmann, M., Brunet, M., Multhoff, G., & Garrido, C. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0306167 · Cited by 573
Huntington's disease: from pathology and genetics to potential therapies
Imarisio, S., Carmichael, J., Korolchuk, V., Chen, C.-W., Saiki, S., Rose, C., Krishna, G., Davies, J. E., Ttofi, E., Underwood, B. R., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071619 · Cited by 409
Metadata
- Authors
- Wyttenbach, A.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-05-01
- Volume
- 11
- Issue
- 9
- Pages
- 1137-1151
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2112360818
- Cited by
- 494
- References
- 53
- FWCI
- 10.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
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