The Protein Kinase C Activator, Phorbol Ester, Elicits Disparate Functional Responses in Androgen-Sensitive and Androgen-Independent Human Prostatic Cancer Cells (original) (raw)

1998, Biochemical and Biophysical Research Communications

AR gene , other cellular pathways may be involved. The protein kinase C (PKC) activator 12-O-tetrade-Growth factors that are recognized to have an imcanoyl-phorbol-13-acetate (TPA) activated cell death portant role in prostatic tumor biology (2, 7, 8) signal in androgen-sensitive LNCaP cells but not in androthrough protein kinase C (PKC) (9-11) to elicits a plethgen-independent DU-145 or PC-3 cells, whose growth ora of cellular responses on cell growth and differentiawas significantly decreased by PKC inhibitors staurotion (12, 13). Furthermore, androgenic regulation of sporine and H7. All cell lines had similar levels of total prostatic genes, including the androgen receptor, is dis-PKC activities which, however, differed on their derupted when cells are treated with protein kinase C pendency on Ca 2/ ions and lipid and were regulated activators (14). Here we show that the PKC activator differently by TPA. Furthermore, expression of the im-TPA elicits disparate responses in androgen-sensitive mediate early genes c-fos and c-jun was up-regulated and insensitive prostatic cancer cells suggesting that by TPA only in LNCaP and DU-145 cells, whereas PCalterations in PKC-isozymes may contribute to andro-3 cells failed to express c-fos mRNA. The regulation gen insensitivity in prostatic cancer. of the c-myc mRNA by TPA correlated inversely with activation of cell death being down-regulated in LNCaP cells, and slightly increased in the androgen-MATERIALS AND METHODS independent cell lines. These results suggest that the PKC signal transduction pathway functions differ-Probes. The glyceraldehyde-3-phosphate dehydrogenase (GADPH) 2 Corresponding

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