Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease.

@article{Wyttenbach2000EffectsOH,
  title={Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease.},
  author={Andreas Wyttenbach and Jenny Carmichael and Jina E Swartz and R. A. Furlong and Yolanda Narain and Julia Rankin and David C Rubinsztein},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 6},
  pages={2898-903}
}
Huntington's disease (HD), spinocerebellar ataxias types 1 and 3 (SCA1, SCA3), and spinobulbar muscular atrophy (SBMA) are caused by CAG/polyglutamine expansion mutations. A feature of these diseases is ubiquitinated intraneuronal inclusions derived from the mutant proteins, which colocalize with heat shock proteins (HSPs) in SCA1 and SBMA and proteasomal components in SCA1, SCA3, and SBMA. Previous studies suggested that HSPs might protect against inclusion formation, because overexpression of… CONTINUE READING

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