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Am J Physiol Cell Physiol 266: C206-C212, 1994;
0363-6143/94 $5.00
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AJP - Cell Physiology, Vol 266, Issue 1 C206-C212, Copyright © 1994 by American Physiological Society

ARTICLES

Basic FGF activates phospholipase D in endothelial cells in the absence of inositol-lipid hydrolysis

A. Ahmed, R. Plevin, M. A. Shoaibi, S. A. Fountain, R. A. Ferriani and S. K. Smith
Department of Obstetrics and Gynecology, University of Cambridge, Rosie Maternity Hospital, United Kingdom.

In the absence of inositol-lipid hydrolysis, mitogenic concentrations of basic fibroblast growth factor (bFGF) stimulated phosphatidylbutanol formation in the presence of butan-1-ol in [3H]myristate-labeled human umbilical vascular endothelial (HUVE) cells, indicating that the fibroblast growth factor receptor was able to couple to the activation of phospholipase D (PLD). The ability of bFGF and 12-O-tetradecanoylphorbol-13-acetate (TPA) to stimulate PLD activity was completely abolished in cells pretreated with 400 nM TPA for 48 h to downregulate protein kinase C (PKC). bFGF-stimulated PLD activity was inhibited by genistein (5 microM; P < 0.02) and the PKC inhibitor 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7, 5 microM; P < 0.001) as well as by the removal of calcium from extracellular environment. bFGF induced DNA synthesis in a dose-dependent manner, and pretreatment of cells with H-7 inhibited the mitogenic activity of bFGF. These results indicate that activation of PKC is responsible for bFGF-induced PLD activation and the mitogenic activity of bFGF in HUVE cells. A coupled PLD/3-sn-phosphatidate phosphohydrolase pathway may play a role in the regulation of endothelial cell proliferation.


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