Expression and Post-translational Modification of Heat Shock Protein 27 (HSP27) in Cancer

Abstract

Heat shock protein 27 (HSP27) is induced by heat shock, environmental, and pathophysiological stressors. HSP27 functions as a molecular chaperone and an anti-apoptotic protein in cells. Dynamic changes such as phosphorylation and oligomerization of HSP27 allow cells to adapt to changes in physiological functions and mount a protective response to damage. HSP27 is highly expressed in aggressive cancers, where it is involved in numerous pro-tumorigenic signaling pathways and is associated with poor prognosis and treatment resistant. This review focuses on the recent findings of the role of HSP27, particularly post-translational modification of HSP27 in cancer, and the strategies for therapeutic purposes by using HSP27 inhibitors.