Prostaglandin F2α activates phospholipase D independently from activation of protein kinase C in osteoblast-like cells

✍ Scribed by Osamu Kozawa; Atsushi Suzuki; Jun Kotoyori; Haruhiko Tokuda; Yasuko Watanabe; Yoshiaki Ito; Yutaka Oiso

• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 527 KB
• Volume: 55
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240550315

✦ Synopsis

Abstract

We previously reported that prostaglandin F~2α~ (PGF~2α~) receptor is coupled to pertussis toxin (PTX)–sensitive GTP‐binding protein (G protein) in osteoblast‐like MC3T3‐E1 cells [Miwa et al. (1990): Biochem Biophys Res Commun 171:1229–1235]. In the present study, we examined the effect of PGF~2α~ on the activation of phosphatidylcholine‐hydrolyzing phospholipase D in MC3T3‐E1 cells. PGF~2α~ stimulated the formation of choline in a dose‐dependent manner in the range between 10 nM and 10 μM. The formation of choline was stimulated by 12‐O‐tetradecanoylphorbol‐13‐acetate (TPA), a protein kinase C (PKC)–activating phorbol ester. 4α‐Phorbol 12,13‐didecanoate, a PKC‐nonactivating phorbol ester, had little effect on choline formation. The formation of choline stimulated by a combination of PGF~2α~ and TPA was additive. Staurosporine, an inhibitor for protein kinases, which inhibited the effect of TPA on choline formation, dose‐dependently enhanced the formation of choline induced by PGF~2α~. NaF, an activator of G protein, stimulated the formation of choline. The formation of choline stimulated by a combination of PGF~2α~ and NaF was not additive. NaF‐induced formation of choline was dose‐dependently enhanced by staurosporine. PTX dose‐dependently inhibited the PGF~2α~‐induced formation of choline. These results strongly suggest that PGF~2α~ activates phospholipase D independently from the activation of PKC in osteoblast‐like cells and PTX‐sensitive G protein is involved in the PGF~2α~‐induced phospholipase D activation. © 1994 Wiley‐Liss, Inc.