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(Received for publication, December 3, 1996, and in revised form, June 10, 1997)
From the Ludwig Institute for Cancer Research, Biomedical Centre,
Box 595, S-751 24 Uppsala, Sweden, § CRC Institute for
Cancer Studies, Queen Elizabeth Hospital,
Birmingham B15 2TH, United Kingdom, and ¶ Friedrich-Miescher
Institute, P. O. Box 2543, CH-4002 Basel, Switzerland
p70s6k has a role in cell cycle
progression in response to specific extracellular stimuli. The signal
transduction pathway leading to activation of p70s6k by
fibroblast growth factor receptor-1 (FGFR-1) was examined in
FGF-2-treated rat L6 myoblasts. p70s6k was activated in a
biphasic and rapamycin-sensitive manner. Although phosphatidylinositol
3
Volume 272, Number 37,
Issue of September 12, 1997
pp. 23347-23353
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
-Kinase-independent p70 S6 Kinase
Activation by Fibroblast Growth Factor Receptor-1 Is Important for
Proliferation but Not Differentiation of Endothelial Cells
-kinase was not activated in the FGF-2 treated cells, as judged from
in vitro and in vivo analyses, wortmannin and
LY294002 treatment inhibited p70s6k activation. Inhibition
of protein kinase C (PKC), by bisindolylmaleimide or by chronic phorbol
ester treatment of the FGFR-1 cells, suppressed but did not block
p70s6k activation. In cells expressing a point-mutated
FGFR-1, Y766F, unable to mediate PKC activation, p70s6k was
still activated, in a bisindolylmaleimide- and phorbol ester-resistant manner. The involvement of S6 kinase in FGFR-1-dependent
biological responses was examined in murine brain endothelial cells. In
response to FGF-2, these cells differentiate to form tube-like
structures in collagen gel cultures and proliferate when cultured on
fibronectin. p70s6k was not activated in endothelial cells
on collagen, whereas activation was observed during proliferation on
fibronectin. In agreement with this finding, rapamycin inhibited the
proliferative but not the differentiation response. Our results
indicate that FGFR-1 mediates p70s6k activation by a
phosphatidylinositol 3-kinase-independent mechanism that does
not require PKC activation and, furthermore, proliferation, but not
differentiation of endothelial cells in response to FGF-2, is
associated with p70s6k activation.
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