Heat Shock Protein 90: Inhibitors in Clinical Trials

摘要

The function of the heat shock proteins (HSPsa) is to fold and maintain the proper conformation of other proteins, referred to as “clients”. HSPs are therefore molecular chaperones. They are overexpressed when a cell is subjected to a transient increase in temperature or to other stresses, such as oxidants or radiations, to assist in refolding denatured client proteins. In addition tomediating critical cellular stress responses, HSPs also play a routine homeostatic role in regulating client protein folding under nonstressed conditions. Molecular chaperones are among the most abundant of cellular proteins, constituting 5-10%of all proteins in the cell, including HSP90, which even under basal, nonstressed conditions comprises approximately 1% of the cellular protein population.