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  • Title: Prostaglandin F2alpha stimulates interleukin-6 synthesis via activation of PKC in osteoblast-like cells.
    Author: Kozawa O, Suzuki A, Tokuda H, Uematsu T.
    Journal: Am J Physiol; 1997 Feb; 272(2 Pt 1):E208-11. PubMed ID: 9124324.
    Abstract:
    In previous studies, we reported that prostaglandin F2alpha (PGF2alpha) stimulates phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D in osteoblast-like MC3T3-E1 cells. In the present study, we examined the effect of PGF2alpha on synthesis of interleukin-6 (IL-6) and the involvement of protein kinase C (PKC) activation in the IL-6 synthesis in these cells. PGF2alpha significantly stimulated IL-6 synthesis in a dose-dependent manner in the range between 10 nM and 10 microM. A PKC-activating phorbol ester, 12-O-tetradecanoylphorbol-13-acetate (TPA), induced IL-6 synthesis. On the contrary, 4alpha-phorbol 12,13-didecanoate, a PKC-nonactivating phorbol ester, had no effect. The synthesis of IL-6 stimulated by a combination of PGF2alpha and TPA was not additive. Staurosporine, an inhibitor for protein kinases that suppressed the TPA-induced IL-6 synthesis, significantly inhibited the PGF2alpha-induced IL-6 synthesis. Calphostin C, a highly specific PKC inhibitor, also suppressed the PGF2alpha-stimulated synthesis of IL-6. The effect of PGF2alpha on IL-6 synthesis in PKC-downregulated cells was much weaker than that in intact cells. These results strongly suggest that PGF2alpha induces IL-6 synthesis via PKC activation in osteoblast-like cells.
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