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J Biol Chem, Vol. 274, Issue 15, 10002-10007, April 9, 1999
,
From the Departments of Vascular endothelial growth factor (VEGF)
receptor Flk-1/KDR in endothelial cells is activated during
vasculogenesis and angiogenesis upon ligand-receptor interaction.
Activated Flk-1/KDR has been shown to recruit Src homology 2 domain-containing signaling molecules that are known to serve as links
to the activation of the mitogen-activated protein (MAP) kinase
signaling pathway. To define the functional significance of
phosphatidylinositol (PI) 3-kinase in VEGF signaling, we have examined
its role in human umbilical vein endothelial cell (HUVEC) cycle
progression. We show herein that p85, the regulatory subunit of PI
3-kinase, is constitutively associated with Flk-1/KDR. The treatment of
HUVECs with VEGF promoted tyrosine autophosphorylation of Flk-1/KDR and
also induced phosphorylation of p85. This was followed by an increase
in the PI 3-kinase activity, which was sensitive to wortmannin, a
potent PI 3-kinase inhibitor. VEGF also induced a striking activation
of MAP kinase in a time-dependent manner. Inhibition
studies with both a dominant-negative p85 mutant and the PI 3-kinase
inhibitor, wortmannin, were employed to show for the first time that
VEGF-stimulated PI 3-kinase modulates MAP kinase activation and nuclear
events such as transcription from c-fos promoter and entry
into the synthesis (S)-phase. Our data demonstrate the importance of PI
3-kinase as a necessary signaling component of VEGF-mediated cell cycle progression.
Cardiothoracic Surgery and
§ Pathology, Weill Medical College of Cornell University,
New York, New York 10021
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