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J. Biol. Chem., Vol. 269, Issue 5, 3219-3225, Feb, 1994
G Sa and PL Fox
Basic fibroblast growth factor (bFGF) stimulates migration and
proliferation of vascular endothelial cells (EC). Fibroblast growth factor
(FGF) receptors have an intrinsic tyrosine kinase activity involved in
FGF-mediated proliferation, but the signal transduction pathway(s)
responsible for movement is not known. We compared the role of
signal-transducing G-proteins in migratory and proliferative responses of
bovine aortic EC in vitro. Pertussis toxin, which ADP- ribosylates
susceptible G-proteins, reduced bFGF-stimulated EC migration by 80%. The
toxin did not block serum-stimulated movement, indicating that structural
components required for motility were not impaired. The toxin did not
inhibit bFGF-stimulated EC proliferation, showing that distinct
intracellular signaling mechanisms are involved in the migratory and
proliferative responses to bFGF. Three experimental approaches indicated
that promigratory responses were due to release of arachidonic acid: (i) of
the second messengers induced by G-protein-coupled effectors, only
arachidonic acid over-came the pertussis toxin block, (ii) bFGF stimulated
arachidonic acid release from EC in a pertussis toxin-sensitive manner, and
(iii) phospholipase A2 inhibitors blocked the EC migration in response to
bFGF. These data provide evidence that the migratory response of vascular
EC to bFGF may be mediated by a G-protein-coupled phospholipase A2
activity.
Basic fibroblast growth factor-stimulated endothelial cell movement is mediated by a pertussis toxin-sensitive pathway regulating phospholipase A2 activity
Department of Cell Biology, Cleveland Clinic Research Institute, Ohio 44195.
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