Int J Biol Sci 2007; 3(1):20-26. doi:10.7150/ijbs.3.20 This issue

Review

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

Guang-Rui Luo1, Sheng Chen2, Wei-Dong Le1

1. Institute of Health Sciences, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, Shanghai, China
2. Institutes of Neurology, Medical School of Jiao Tong University, Shanghai, China

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Citation:
Luo GR, Chen S, Le WD. Are heat shock proteins therapeutic target for Parkinson's disease?. Int J Biol Sci 2007; 3(1):20-26. doi:10.7150/ijbs.3.20. Available from https://www.ijbs.com/v03p0020.htm

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Abstract

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.

Keywords: Parkinson's disease (PD), heat shock proteins (HSPs), ubiquitin-proteasome system (UPS), apoptosis