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PROTEIN KINASE C PATHWAY IS INVOLVED IN REGULATING THE SECRETION OF PROSTATIC ACID PHOSPHATASE IN HUMAN PROSTATE CANCER CELLS

✍ Scribed by Ming-Fong Lin; Xiu-Qing Zhang; Jeanenne Dean; Fen-Fen Lin

Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
171 KB
Volume
25
Category
Article
ISSN
1065-6995

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✦ Synopsis

The stimulated secretion of prostatic acid phosphatase (PAcP) has been known to be a hallmark of androgen action on human prostate epithelial cells for the last five decades. The molecular mechanism of androgen action on PAcP secretion, however, has remained mostly unknown. We investigated the molecular mechanism that promotes PAcP secretion in LNCaP human prostate carcinoma cells which express PAcP and are androgen‐responsive. Treatment with 12‐o‐tetradecanoyl phorbol‐13‐acetate (TPA), a protein kinase C (PKC) activator, resulted in an increased secretion of PAcP in a dose‐ and time‐dependent fashion. 4α‐Phorbol, a biologically inactive isomer of TPA, had no effect. This TPA stimulation of PAcP secretion was observed 2h after exposure, while TPA did not have a significant effect on the mRNA level even with a 6h treatment. A23187 calcium ionophore, known to mobilize cellular calcium which is a co‐factor of PKC, also activated PAcP secretion. This TPA stimulation of PAcP secretion was more potent than the conventional stimulating agent 5α‐dihydrotestosterone (DHT) at the same concentration of 50n m. Furthermore, the action of TPA and DHT on PAcP secretion was blocked by five different PKC inhibitors. Results also showed that DHT, as well as TPA, could rapidly modulate PKC activity. Therefore, PKC can regulate PAcP secretion, and may also be involved in DHT action on PAcP secretion.

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