Inhibition of MAP kinase kinase (MEK) blocks endothelial PGI2 release but has no effect on von Willebrand factor secretion or E‐selectin expression

Abstract
We have examined the potential role of MAP kinase in the regulation of endothelial cell PGI2 synthesis, vWF secretion and E-selectin expression using the specific MEK inhibitor PD98059. PD98059 dose-dependently attenuated the tyrosine phosphorylation and activation of p42mapk in response to thrombin or inflammatory cytokines. Inhibition of thrombin-induced p42mapk activation was paralleled by an inhibitory effect of PD98059 on thrombin-driven PGI2 generation but not on vWF secretion or IL-1α/TNFα-induced E-selectin expression. These results provide evidence for a key role for p42mapk in the acute regulation of PGI2 synthesis in human endothelial cells and suggest that activation of the MAP kinase cascade is not obligatory for cytokine-stimulated E-selectin expression.

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