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(Received for publication, September 27, 1994; and in revised form, December 20,
1994) From the
Vascular endothelial cell growth factor (VEGF), an endothelial
cell-specific mitogen that plays an important role in angiogenesis,
promotes the tyrosine phosphorylation of at least 11 proteins in bovine
aortic endothelial cells (BAEC). Proteins immunoprecipitated from
lysates of control- and VEGF-stimulated BAEC with antisera to
phospholipase C-
Volume 270,
Number 12,
Issue of March 24, 1995 pp. 6729-6733
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
ASSOCIATION WITH ENDOTHELIAL CELL PROLIFERATION (*)
(PLC-) were fractionated by
SDS-polyacrylamide gel electrophoresis and transferred to Immobilon-P.
Evaluation of the Western blots with antisera to phosphotyrosine
demonstrated that PLC- and two proteins (100 and 85 kDa) that
associate with PLC- were phosphorylated in response to VEGF. By
using antisera specific to other mediators of signal transduction that
contain SH2 domains for immunoprecipitation, it was demonstrated that
VEGF promotes phosphorylation of phosphatidylinositol 3-kinase, Ras
GTPase activating protein (GAP), and the oncogenic adaptor protein NcK.
Proteins of M
consistent with the VEGF receptors
Flt-1 and Flk-1/KDR were also tyrosine phosphorylated in stimulated
cells. Tyrosine-phosphorylated Nck, PLC-, and two GAP-associated
proteins, p190 and p62, were in GAP immunoprecipitates of
VEGF-stimulated BAEC, and tyrosine-phosphorylated NcK was in
phosphatidylinositol 3-kinase immunoprecipitates. These observations
suggest that VEGF promotes formation of multimeric aggregates of VEGF
receptors with proteins that contain SH2 domains and activate various
signaling pathways. VEGF-promoted proliferation of endothelial cells
and tyrosine phosphorylation of SH2 domain containing signaling
molecules were inhibited by the tyrosine kinase inhibitor genistein.
), phospholipase C-; PI-3 kinase, phosphatidylinositol
3-kinase; GAP, GTPase activating protein; PTyr Ab, antisera to
phosphotyrosine; PAGE, polyacrylamide gel electrophoresis; PDGF,
platelet-derived growth factor; EGF, epidermal growth factor; PAEC,
porcine aortic endothelial cells.
)
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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