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  • Title: Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase C gamma 1 in vascular endothelial cells.
    Author: Venema VJ, Ju H, Sun J, Eaton DC, Marrero MB, Venema RC.
    Journal: Biochem Biophys Res Commun; 1998 May 08; 246(1):70-5. PubMed ID: 9600070.
    Abstract:
    Bradykinin (BK) B2 receptor signaling involves activation of phospholipase C (PLC). PLC activation by other receptors consists of either allosteric activation of PLC beta isoforms by G-proteins or tyrosine phosphorylation of PLC gamma isoforms. Because the B2 receptor is a G-protein-coupled receptor, it has been assumed that the receptor signals through PLC beta. In the present study, however, we have found that BK stimulation of IP3 production and the Ca2+ signal in endothelial cells is dependent on tyrosine phosphorylation. Furthermore, stimulation of B2 receptors in these cells is accompanied by a transient tyrosine phosphorylation of PLC gamma 1. Phosphorylation is correlated with increased IP3 production and association of PLC gamma 1 with the C-terminal intracellular domain of the B2 receptor. The B2 receptor can thus physically associate with intracellular proteins other than G-proteins. Activation of PLC gamma isoforms, rather than PLC beta isoforms, may, therefore, be primarily responsible for BK-stimulated IP3 generation in endothelial cells.
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