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Thrombin induces c-fos expression in cultured human endothelial cells by a
Ca2(+)-dependent mechanism
MG Lampugnani, F Colotta, N Polentarutti, M Pedenovi, A Mantovani and E Dejana
Istituto di Ricerche Farmacologische Mario Negri, Milan, Italy.
The proto-oncogene c-fos has been implicated in the modulation of various
cell functions. We have found that thrombin, a pleiotropic activator of
endothelial cells, induced c-fos mRNA in human umbilical vein endothelial
cells (HEC). This effect was dose-related (0.05 to 1.0 U/mL) and transient
(maximal after 1 hour and negligible within 4 hours). Since thrombin
activates phosphoinositide (PI) turnover through a pertussis toxin
(PT)-sensitive guanosine triphosphate-binding regulatory protein(s)
(G-protein) with subsequent stimulation of protein kinase C (PKC) and Ca2+
movements, we investigated whether these intracellular pathways are also
responsible for c-fos induction. PT inhibited thrombin's effect on c-fos
expression, but had no effect on c-fos expression by phorbol myristate
acetate (PMA). Down regulation of PKC by prolonged exposure to PMA had no
effect on thrombin and ionomycin stimulation of c-fos, but inhibited PMA
activation of this gene. Quenching of the Ca1(2+) increase in response to
quin2 loading in the absence of external Ca2+ suppressed thrombin activity
on c-fos transcription. Under the same conditions PMA activity was not
inhibited or only partially inhibited. Interleukin-1 beta (IL-1 beta) and
basic fibroblast growth factor (bFGF) stimulation of c-fos mRNA level were
not inhibited by quin2; on the contrary, ionomycin effect was blocked by
this agent. These results indicate that thrombin-induced c-fos expression
in HEC does not require a fully active PKC but is dependent on normal
intracellular Ca2+ availability.
Volume 76,
Issue 6,
pp. 1173-1180,
09/15/1990
Copyright © 1990 by The American Society of Hematology
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