PD Guide

Heat Shock Proteins

Symptomatic Relief, Stress Response Pathways, Targeting Heat Shock Proteins

Heat shock proteins are upregulated in response to cellular stresses, including temperature, inflammation, hypoxia, starvation and exposure to toxins. These proteins mainly function as intracellular chaperones, playing an essential role in protein folding and conformation and in preventing protein aggregation. They have also been found to interact with LRRK2 in vivo, and thus may play a role in LRRK2 mutant pathogenicity (Wang et al., 2008).

Reference: 
Wang L, Xie C, Greggio E, Parisiadou L, Shim H, Sun L, et al. The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2. J Neurosci. 2008;28(13):3384-91.
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