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Protein kinase C activation amplifies prostaglandin F2α-induced prostaglandin E2 synthesis in osteoblast-like cells

✍ Scribed by Haruhiko Tokuda; Yutaka Oiso; Osamu Kozawa

Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
656 KB
Volume
48
Category
Article
ISSN
0730-2312

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✦ Synopsis

In cloned osteoblast-like cells, MC3T3-EII prostaglandin F, , (PGF,,) stimulated arachidonic acid (AA) release in a dose-dependent manner in the range between 1 n M and 10 pM. 12-O-tetradecanoylphorbol-l3-acetate (TPA), a protein kinase C (PKC) activator, which by itself had little effect on AA release, markedly amplified the release of AA stimulated by PGF, , in a dose-dependent manner. 4 a-phorbol 12,13-didecanoate, a phorbol ester which is inactive for PKC, showed little effect on the PGF,,-induced AA release. 1 -oleoyl-2-acetylglycerol (OAG), a specific activator for PKC, mimicked TPA by enhancement of the AA release induced by PGF, , . H-7, a PKC inhibitor, markedly suppressed the effect of OAG on PGF,,-induced AA release. Quinacrine, a phospholipase A, inhibitor, showed partial inhibitory effect on PGF,,-induced AA release, while it suppressed the amplification by OAG of PGF,,-induced AA release almost to the control level. Furthermore, TPA enhanced the AA release induced by melittin, known as a phospholipase A, activator. On the other hand, TPA inhibited the formation of inositol trisphosphate stimulated by PGF,G. Under the same condition, PGF2a indeed stimulated prostaglandin E, (PGE,) synthesis and TPA markedly amplified the PGF,,-induced PGE, synthesis as well as AA release. These results indicate that the activation of PKC amplifies PGF,,-induced both AA release and PGE, synthesis through the potentiation of phospholipase A, activity in osteoblast-like cells.

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