Introduction: Prostate cancer is among the leading causes of death in males in the Western world with progression to aggressive, metastatic disease associated with poor prognosis. The importance of ion channels is increasingly recognised in cancer biology. The Transient Receptor Potential (TRP) ion channel family is associated with several cancers, displaying both oncogenic and anti-oncogenic properties when expression is altered. The purpose of the present study was to examine the functional expression of TRPM8 channels in prostate cancer cells and normal prostate epithelial cells. Materials and Methods: A panel of cell lines was used including prostate cancer cells (PC3 and DU145) and immortalised normal prostate cells (RWPE1 and PNT2). Clonogenic cell survival assays, scratch-wound healing assays and immunofluorescence were performed. Quantitative data are expressed as mean±SD.Results: The TRPM8 inhibitor, AMTB hydrochloride1, caused a concentration-dependent decrease in cell survival of prostate cancer PC3 (IC50 6.51µM, N=6, P<0.001) and normal prostate PNT2 cells (IC50 6.60µM, N=6, P=<0.001) in clonogenic survival assays. In contrast, DU145 cells (N=6) were less sensitive (P>0.05) until concentrations above 17.5µM, when a significant decrease was observed (P<0.01). Activation of TRPM8 by menthol2 did not significantly affect the survival of normal prostate PNT2 cells (5-20µM, N=6, P>0.05) or prostate cancer PC3 cells (N=6, P>0.05).In scratch-wound healing assays, TRPM8 inhibition reduced cell migration although this was not significant in the prostate cancer cells PC3 (N=5, P>0.05) or DU145 (N=5, (P>0.05). A significant reduction in % wound closure of normal RWPE1 cells occurred (N=4, P<0.05, control 35.1±6.3% to AMTB 12.4±6.2%). TRPM8 activation increased migration in PC3 prostate cancer cells (N=5, P<0.05, control 47.9±19.9% to menthol 73.2±8.1%) and normal RWPE-1 cells (N=5, P<0.01, control 24.2±8.9% to menthol 42.3±4%).Immunofluorescence and confocal microscopy confirmed TRPM8 protein expression in prostate cancer and normal prostate epithelial cells. In normal prostate RWPE1 cells, TRPM8 was expressed throughout the cytoplasm whereas in PNT2 cells, perinuclear expression was highest. TRPM8 immunofluorescence was not homogeneous within prostate cancer PC3 cells, with greater intensity observed towards one of the edges perhaps indicative of a migration leading edge. In prostate cancer DU145 cells, TRPM8 expression was perinuclear. Conclusions: TRPM8 channels are functionally expressed in the panel of prostate cancer cells and normal prostate epithelial cells examined. Inhibition of TRPM8 reduced survival and migration of normal and prostate cancer cells. TRPM8 activation did not impact survival but increased the migration of normal prostate and prostate cancer cells.