© 1995 American Heart Association, Inc.
Articles |
Calcium Signaling in Endothelial Cells Involves Activation of Tyrosine Kinases and Leads to Activation of Mitogen-Activated Protein Kinases
From Zentrum der Physiologie, Klinikum der JWG-Universität, Frankfurt/Main, Germany.
Correspondence to Dr Ingrid Fleming, Zentrum der Physiologie, Klinikum der JWG-Universität, Theodor-Stern-Kai 7, D-60590 Frankfurt/Main, Germany.
Abstract The activation of endothelial cells following
exposure to a variety of receptor-dependent and -independent stimuli is
associated with the release of Ca2+ from
intracellular stores as well as the influx of Ca2+
from the extracellular space. In the present study, we investigated
the interaction between Ca2+ signaling in cultured
human umbilical vein endothelial cells and tyrosine phosphorylation.
Stimulation of endothelial cells with either bradykinin (100 nmol/L),
histamine (1 µmol/L), or the Ca2+-ATPase inhibitor
thapsigargin (30 nmol/L) resulted in a slightly delayed but prolonged
tyrosine phosphorylation of two low molecular weight proteins (
42
and 44 kD). These proteins were identified by immunoprecipitation as
the 42- and 44-kD isoforms of mitogen-activated protein kinase (MAP
kinase). The agonist-induced tyrosine phosphorylation of the 42-/44-kD
doublet was sensitive to the tyrosine kinase inhibitors genistein (100
µmol/L) and piceatannol (10 µmol/L) and was inhibited by the
removal of Ca2+ from the extracellular medium. In
fura 2–loaded endothelial cells, inhibition of tyrosine kinases
attenuated Ca2+ signaling after stimulation with
either bradykinin (30 nmol/L) or thapsigargin (30 nmol/L). Since
inhibition of tyrosine kinases specifically attenuates the plateau
phase of the Ca2+ response after stimulation, the
effect of tyrosine kinase inhibition appeared to be mostly associated
with the influx of Ca2+ from the extracellular
space. These data demonstrate that the signal transduction cascade
initiated by receptor-dependent and -independent stimulation of
endothelial cells includes the following: a tyrosine kinase
inhibitor–sensitive transmembranous influx of Ca2+
and the tyrosine phosphorylation of two cytosolic protein substrates
identified as MAP kinases. Furthermore, on one hand, an increase in
[Ca2+]i was essential for tyrosine
phosphorylation; on the other, the Ca2+ influx was
modulated by tyrosine phosphorylation. This finding documents the
mutual dependence of these two crucial signaling pathways in
endothelial cells.
Key Words: endothelial cells • mitogen-activated protein kinase • intracellular Ca2+ • genistein
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