Are heat shock proteins therapeutic target for Parkinson's disease?

Guang Rui Luo, Sheng Chen, Wei Dong Le

Research output: Contribution to journalReview articlepeer-review

46 Scopus citations


Heat shock proteins (HSPs), known as molecular chaperone to assist protein folding, have recently become a research focus in Parkinson's disease (PD) because the pathogenesis of this disease is highlighted by the intracellular protein misfolding and inclusion body formation. The present review will focus on the functions of different HSPs and their protective roles in PD. It is postulated that HSPs may serve as protein folding machinery and work together with ubiquitin-proteasome system (UPS) to assist in decomposing aberrant proteins. Failure of UPS is thought to play a key role in the pathogenesis of PD. In addition, HSPs may possess anti-apoptotic effects and keep the homeostasis of dopaminergic neurons against stress conditions. The critical role of HSPs and recent discovery of some novel HSPs inducers suggest that HSPs may be potential therapeutic targets for PD and other neurodegenerative disorders.

Original languageEnglish (US)
Pages (from-to)20-26
Number of pages7
JournalInternational Journal of Biological Sciences
Issue number1
StatePublished - 2007


  • Apoptosis
  • Heat shock proteins (HSPs)
  • Parkinson's disease (PD)
  • Ubiquitin-proteasome system (UPS)

ASJC Scopus subject areas

  • Cell Biology
  • Developmental Biology
  • Molecular Biology
  • Ecology, Evolution, Behavior and Systematics
  • Applied Microbiology and Biotechnology


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