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Centre Hospitalier Universitaire de Québec, Centre de Recherche du Pavillon l’Hôtel-Dieu de Québec, Quebec, Quebec, Canada
Several cytokines and LPS regulate the population of the
B1 receptors (B1Rs) for kinins; these are
responsive to des-Arg9-bradykinin (BK) and
Lys-des-Arg9-BK. B1R activation contributes to
inflammatory vascular changes and pain. Aortic rings isolated from
normal rabbits and incubated in vitro in Krebs physiological medium
were used as a model of tissue injury. From a null level of response,
these rings exhibit a time- and protein synthesis-dependent increase in
the maximal contractile response to des-Arg9-BK. Exposure
to exogenous IL-1ß or epidermal growth factor (EGF) considerably
increases the process of sensitization to the kinins. Freshly isolated
control aortic rings showed high mitogen-activated protein (MAP) kinase
activities (persistent activation of p38, but less prolonged for
extracellular signal-regulated kinase and c-Jun-N-terminal
kinase/stress-activated protein kinase pathways) relatively to the
basal activities found in various types of cultured cells. IL-1ß or
EGF further increased the activities of the extracellular
signal-regulated kinase and c-Jun-N-terminal kinase/stress-activated
protein kinase MAP kinases. The inhibitor of the p38 MAP kinase, SB
203580 (10 µM), massively (
75%) and selectively inhibited the
spontaneous sensitization to des-Arg9-BK over 6 h. SB
203580 also significantly reduced the development of the response to
des-Arg9-BK as stimulated by IL-1 or EGF. Both spontaneous
and IL-1ß-stimulated up-regulation of responsiveness to
des-Arg9-BK were significantly inhibited by the MAP kinase
extracellular signal-regulated kinase kinase 1 inhibitor PD 98059
(40%). The protein kinase inhibitors failed to inhibit protein
synthesis and to acutely inhibit the contractile effect of
des-Arg9-BK, suggesting that they do not influence
B1 receptor transduction mechanisms. In cultured aortic
smooth muscle cells stimulated with EGF, MAP kinase activation preceded
B1R mRNA induction. Protein kinase inhibitors reveal the
role of cell injury-controlled MAP kinase pathways, and singularly of
the p38 pathway, in the induction of B1R.
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