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

Citation
Rr. Schumann et al., 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, Blood, 87(7), 1996, pp. 2805-2814
Citations number
50
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Hematology
Journal title
BloodACNP
ISSN journal
0006-4971
Volume
87
Issue
7
Year of publication
1996
Pages
2805 - 2814
Database
ISI
SICI code
0006-4971(1996)87:7<2805:LITRTP>2.0.ZU;2-K
Abstract
Human vascular endothelial cells (HUVECs), which do not display the li popolysaccharide (LPS) receptor CD14, were examined for protein tyrosi ne phosphorylation after LPS stimulation in the presence and absence o f soluble CD14 (sCD14). By phosphotyrosine Western blotting and immuno -complex kinase assays we show that LPS was capable of inducing in the se cells rapid protein tyrosine phosphorylation and kinase activation of two members of the mitogen-activated protein kinase (MAPK) family e rk-1 and the newly discovered p38, requiring the presence of sCD14. LP S-induced tyrosine phosphorylation of MAPK was associated with increas ed transcript- and surface protein expression of intracellular adhesio n molecule-1 by HUVECs. MAPK phosphorylation and activation was induce d by LPS in concentrations as little as 30 ng/mL and as early as 15 mi nutes 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 bo th cell types. (C) 1996 by The American Society of Hematology.