Abstract
We previously showed that prostaglandin (PG) D2stimulates Ca2+influx from extracellular space and activates phosphoinositidc (PI)-hydrolyzing phospholipase C and phosphatidylcholine (PC)-hydrolyzing phospholipase D independently from PGE2or PGF2αin osteoblast-like MC3T3-E1 cells. In the present study, we investigated the effect of PGD2on the synthesis of interleukin-6 (IL-6) and its regulatory mechanism in MC3T3-E1 cells. PGD2 significantly stimulated IL-6 synthesis dose-dependently in the range between 10nM and 10μM. The depletion of extracellular Ca2+by EGTA reduced the PGD2-induced IL-6 synthesis. TMB-8, an inhibitor of intracellular Ca2+mobilization, significantly inhibited the PGD2-induced IL-6 synthesis. On the other hand, calphostin C, a specific inhibitor of protein kinase C (PKC), enhanced the synthesis of IL-6 induced by PGD2. In addition, U-73122, an inhibitor of phospholipase C, and propranolol, a phosphatidic acid phosphohydrolase inhibitor, enhanced the PGD2-induced IL-6 synthesis. These results strongly suggest that PGD2stimulates IL-6 synthesis through intracellular Ca2+mobilization in osteoblasts, and that the PKC activation by PGD2itself regulates the over-synthesis of IL-6.
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