Protective role of heat shock proteins in Parkinson's disease

Neurodegener Dis. 2011;8(4):155-68. doi: 10.1159/000321548. Epub 2011 Jan 5.


Parkinson's disease (PD) is the second most common neurodegenerative disease after Alzheimer's disease. Despite a large amount of research, the pathogenetic mechanism of these diseases has not yet been clarified. Abnormal protein folding, oxidative stress, mitochondrial dysfunction, and apoptotic mechanisms have all been reported as causes of neurodegenerative diseases in association with neuroinflammatory mechanisms which, by generating deleterious molecules, could promote the cascade of events leading to neurodegeneration. Heat shock proteins (HSPs) play a central role in preventing protein misfolding and inhibiting apoptotic activity, and represent a class of proteins potentially involved in PD pathogenesis. The present review will focus on two HSPs, HSP70 and HSP90, with the aim of specifying their role in PD pathogenesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • HSP70 Heat-Shock Proteins / metabolism*
  • HSP90 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / metabolism
  • Humans
  • Parkinson Disease / metabolism*


  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins