Targeting Heat Shock Proteins in Prostate Cancer

W.      Hessenkemper; A.      Baniahmad

doi:10.2174/0929867311320220001

Abstract

Heat shock proteins (HSPs) and chaperones are highly conserved stress-induced factors. They regulate not only protein folding and stability but are also actively involved in protein transport and transcriptional regulation. HSPs have cytoprotective roles and are essential for cancer cell survival. Noteworthy, HSPs are often upregulated in cancer. Therefore, HSPs emerged as drug targets for cancer therapy. Especially for prostate cancer (PCa) therapy, a battery of different compounds has been identified that act with different modes to inhibit PCa growth. The androgen receptor (AR) is a major player in PCa progression and is a well-known interacting factor of HSPs. Since the AR function is very dependent on HSP activity, many emerging compounds address the AR-associated HSPs as novel drug targets. Here, we provide an insight into the different classes of HSPs, their association with the human AR, the role of HSPs in human PCa development and review also the targeting of HSPs in human PCa. Further, the function and the underlying molecular mechanisms of specific compounds that are currently under investigation for the use against PCa growth will be comprehensively summarized.

Keywords: Androgen receptor, chaperones, heat shock proteins, prostate cancer therapy.