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Role of the Mitogen-Activated Protein Kinases in the Expression of the Kinin B₁ Receptors Induced by Tissue Injury¹

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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