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  • Immediate and transient phosphorylation of the heat shock protein 27 initiates chemoresistance in prostate cancer cells.

Immediate and transient phosphorylation of the heat shock protein 27 initiates chemoresistance in prostate cancer cells.

Oncology reports (2014-09-19)
Matthias B Stope, Martin Weiss, Melanie Preuss, Andreas Streitbörger, Christoph A Ritter, Uwe Zimmermann, Reinhard Walther, Martin Burchardt
ABSTRACT

Drug resistance minimizes the effects of prostate cancer (PC) chemotherapy with docetaxel and is generally considered to be associated with the expression of heat shock protein (HSP) 27 including various cytoprotective pathways. In the present study, we investigated the effects of HSP27 phosphorylation on PC cell growth underlying docetaxel treatment. Cell counting revealed significantly reduced cell growth during docetaxel treatment as a result of both activation of mitogen-activated protein kinase p38 (MAPK p38) and protein kinase D1 (PKD1), and, most importantly, the overexpression of the phosphorylation-mimicking mutant HSP27-3D. Further analysis revealed a docetaxel-dependent induction of HSP27 accompanied by an initial phosphorylation and rapid dephosphorylation of the protein. Based on the data, we can conclude that phosphorylation of HSP27 protein is a crucial mechanism in the initiation of chemoresistance in PC. Moreover, the results indicate a key impact of HSP27 on viability and proliferation of PC cells underlying anticancer therapy. The protective function depends on the initial phosphorylation status of HSP27 and represents a putative co-therapeutic target to prevent chemoresistance during docetaxel therapy.

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