Basic fibroblast growth factor stimulates phosphatidylcholine-hydrolyzing phospholipase D in osteoblast-like cells

✍ Scribed by Atsushi Suzuki; Junji Shinoda; Shigeru Kanda; Yutaka Oiso; Osamu Kozawa

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 822 KB
• Volume: 63
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/(sici)1097-4644(19961215)63:4<491::aid-jcb10>3.0.co;2-h

✦ Synopsis

We examined the effect of basic fibroblast growth factor (bFGF) on the activation of phosphatidylcholinehydrolyzing phospholipase D in osteoblast-like MC3T3-EI cells. bFCF stimulated both the formations of choline (ECS0 was 30 ng/ml) and inositol phosphates (ECS0 was 10 ng/ml). Calphostin C, an inhibitor of protein kinase C (PKC), had little effect on the bFGF-induced formation of choline. bFGF stimulated the formation of choline also in PKC down regulated cells. Genistein and methyl 2,5-dihydroxycinnamate, inhibitors of protein tyrosine kinases, significantly suppressed the bFGF-induced formation of choline. Sodium orthovanadate, an inhibitor of protein tyrosine phosphatases, enhanced the bFGF-induced formation of choline. In vitro kinase assay for FGF receptors revealed that FGF receptor 1 and 2 were autophosphorylated after FGF stimulation. bFGF dose-dependently stimulated DNA synthesis of these cells. These results strongly suggest that bFGF activates phosphatidylcholine-hydrolyzing phospholipase D through the activation of tyrosine kinase, but independently of PKC activated by phosphoinositide hydrolysis in osteoblast-like Cells. D 1996 Wiley-Liss, Inc.