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Lipopolysaccharide induces the rapid tyrosine phosphorylation of the
mitogen-activated protein kinases erk-1 and p38 in cultured human vascular
endothelial cells requiring the presence of soluble CD14
RR Schumann, D Pfeil, N Lamping, C Kirschning, G Scherzinger, P Schlag, L Karawajew and F Herrmann
Department of Medical Oncology and Applied Molecular Biology, Humboldt-
Universitat, Berlin, Germany.
Human vascular endothelial cells (HUVECs), which do not display the
lipopolysaccharide (LPS) receptor CD14, were examined for protein tyrosine
phosphorylation after LPS stimulation in the presence and absence of
soluble CD14 (sCD14). By phosphotyrosine Western blotting and immunocomplex
kinase assays we show that LPS was capable of inducing in these cells rapid
protein tyrosine phosphorylation and kinase activation of two members of
the mitogen-activated protein kinase (MAPK) family erk-1 and the newly
discovered p38, requiring the presence of sCD14. LPS-induced tyrosine
phosphorylation of MAPK was associated with increased transcript- and
surface protein expression of intracellular adhesion molecule-1 by HUVECs.
MAPK phosphorylation and activation was induced by LPS in concentrations as
little as 30 ng/mL and as early as 15 minutes after stimulation.
Furthermore, tyrosine kinase inhibitors such as Genistein partially
inhibited this effect. These results show that LPS triggers similar
signaling events in both CD14+ myelo-monocytic cells and cells lacking the
putative LPS-receptor CD14, suggesting the presence of a common, yet
unidentified element in LPS-signaling in both cell types.
Volume 87,
Issue 7,
pp. 2805-2814,
04/01/1996
Copyright © 1996 by The American Society of Hematology
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