Polyphenols and proteostasis: The role of heat shock response and the ubiquitin-proteasome system

Reduced proteostasis is believed to be one of the major consequences of aging and oxidative stress. Exogenous compounds that promote proteostasis by regulating the heat shock response and the ubiquitin-proteasome system – key components of the proteostasis framework – are being investigated as potential therapeutics that slow down, or even prevent, loss of healthy proteostasis. A number of plant-derived polyphenols are assessed as potential promoters of proteostasis by monitoring their effect on proteasome activity, on expression levels of ubiquitin-proteasome (UPS) subunits, and on the heat shock response (HSR). A preliminary proteomics study was carried out to identify and quantify levels of UPS subunits, levels of HSR proteins, and other stress response proteins during exposure to a plant polyphenol. A number of small HSR proteins were upregulated in the presence of the polyphenol. There was no change in the levels of UPS subunits, however organismal proteasome activity was altered in a concentration dependent manner. The preliminary proteome study also identified additional stress-responsive pathways associated with exposure to plant polyphenols.

Acknowledgements: National Institutes of Health.

Keywords: Polyphenol, proteomics, ubiquitin-proteasome system, heat shock response.

No conflict of interest has been declared by the author(s).