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Vol. 57, Issue 6, 1123-1131, June 2000
:
Modulation by Dexamethasone
Department of Thoracic Medicine (E.-B.H., A.J.F., J.R., P.J.B.,
K.F.C.), National Heart and Lung Institute, Imperial College
School of Medicine, London, United Kingdom; and Novartis Institute for
Medical Sciences (G.B., P.M.), London, United Kingdom
The cellular and molecular mechanisms governing bradykinin B1 and B2
receptor expression and function are poorly understood. We investigated
the regulation of both B1 and B2 receptors in human embryonic lung
fibroblasts (HEL 299) by the proinflammatory cytokines tumor necrosis
factor 
(TNF-) and interleukin 1
(IL-1). TNF- and
IL-1 both induced a rapid and transient increase in B1 and B2
receptor mRNA expression that was maximal by 2 h, accompanied by
an increase in B1 and B2 receptor protein, as measured by radioligand binding assay with [3H]des-Arg10-kallidin,
and [3H]bradykinin, respectively. The induced B1
receptors were functionally coupled, because the B1 agonist,
des-Arg10-kallidin, induced an increase in arachidonic acid
release in TNF--stimulated cells but not in control cells. The
induction of B1 and the up-regulation of B2 receptors by TNF- was
partly mediated through activation of p38 mitogen-activated protein
kinase and that of B2 receptor by protein kinase A. TNF- and IL-1
regulation of both B1 and B2 receptors was inhibited by dexamethasone.
When compared with vehicle-treated cells, dexamethasone increased the rate of decline of both B1 and B2 receptor mRNAs. Nuclear run-on experiments demonstrate that the induction of B1 and the up-regulation of B2 receptors as well as the inhibitory effect of dexamethasone are
entirely mediated through post-transcriptional mechanisms.
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