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Am J Physiol Cell Physiol 274: C789-C798, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 3, C789-C798, March 1998

Activation of p42mapk in human umbilical vein endothelial cells by interleukin-1alpha and tumor necrosis factor-alpha

Michael J. May, Caroline P. D. Wheeler-Jones, Rebecca A. Houliston, and Jeremy D. Pearson

Vascular Biology Research Centre, Biomedical Sciences Division, King's College London, Kensington, London W8 7AH, United Kingdom

Work from this and other laboratories has identified a role for protein tyrosine kinases in interleukin-1alpha (IL-1alpha )- and tumor necrosis factor-alpha (TNF-alpha )-induced responses in endothelial cells. In this study, we show that activation of human umbilical vein endothelial cells (HUVEC) by IL-1alpha leads to increased tyrosine phosphorylation of several proteins including one with a molecular mass of ~42 kDa. This protein was identified as p42mapk by Western blot analysis. Tyrosine phosphorylation and catalytic activation of p42mapk by IL-1alpha was transient, reaching maximal levels after 30 min and returning to basal levels by 120-300 min. Activation of p42mapk in HUVEC was also observed in response to TNF-alpha or to the protein kinase C (PKC)-activating phorbol ester phorbol 12-myristate 13-acetate (PMA). Pretreatment of HUVEC with IL-1alpha or TNF-alpha prevented reactivation of p42mapk by either cytokine but did not affect subsequent activation in response to PMA. Activation of p42mapk by PMA was significantly reduced by the PKC inhibitor Ro-31-8220 and completely inhibited by the protein tyrosine kinase inhibitor genistein. Genistein, but not Ro-31-8220, attenuated IL-1alpha - and TNF-alpha -induced p42mapk activation. Taken together, the results of this study demonstrate 1) that p42mapk is transiently activated in HUVEC by IL-1alpha and TNF-alpha , 2) that this activation is PKC independent, and 3) that a genistein-inhibitable tyrosine kinase may be an upstream regulator of cytokine-induced p42mapk activation in human endothelium.

cytokines; signal transduction; protein kinases; phosphatases


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