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1 Department of Veterinary Basic Sciences, The Royal Veterinary College, University of London, London NW1 0TU; and 2 Centre for Cardiovascular Biology and Medicine, King's College London, London SE1 1UL, United Kingdom
We have examined the mechanisms regulating
prostacyclin (PGI2) synthesis after acute exposure of human
umbilical vein endothelial cells (HUVEC) to interleukin-1
(IL-1).
IL-1 evoked an early (30 min) release of PGI2 and
[3H]arachidonate that was blocked by the cytosolic
phospholipase A2 (cPLA2) inhibitor
arachidonyl trifluoromethyl ketone. IL-1-mediated activation
of extracellular signal-regulated kinase 1/2 (ERK1/2; p42/p44mapk) coincided temporally with phosphorylation of
cPLA2 and with the onset of PGI2
synthesis. The mitogen-activated protein kinase (MAPK) kinase (MEK)
inhibitors, PD-98059 and U-0126, blocked IL-1-induced ERK
activation and partially attenuated cPLA2
phosphorylation and PGI2 release, suggesting that
ERK-dependent and -independent pathways regulate cPLA2
phosphorylation. SB-203580 treatment enhanced IL-1-induced MEK,
p42/44mapk, and cPLA2 phosphorylation but
reduced thrombin-stimulated MEK and p42/44mapk activation.
IL-1, but not thrombin, activated Raf-1 as assessed by
immune-complex kinase assay, as did SB-203580 alone. These results show
that IL-1 causes an acute upregulation of PGI2
generation in HUVEC, establish a role for the
MEK/ERK/cPLA2 pathway in this early release, and provide
evidence for an agonist-specific cross talk between p38mapk
and p42/44mapk that may reflect receptor-specific
differences in the signaling elements proximal to MAPK activation.
human endothelium; interleukin-1; thrombin; mitogen-activated
protein kinases; cytosolic phospholipase A2; prostacyclin; extracellular signal-regulated kinase
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