Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase Cγ1 in vascular endothelial cells

Virginia J. Venema, Hong Ju, Jimin Sun, Douglas C. Eaton, Mario B. Marrero, Richard C. Venema

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Bradykinin (BK) B2 receptor signaling involves activation of phospholipase C (PLC). PLC activation by other receptors consists of either allosteric activation of PLCβ isoforms by G-proteins or tyrosine phosphorylation of PLCγ isoforms. Because the B2 receptor is a G-protein-coupled receptor, it has been assumed that the receptor signals through PLCβ. 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 PLCγ1. Phosphorylation is correlated with increased IP3 production and association of PLCγ1 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 PLCγ isoforms, rather than PLCβ isoforms, may, therefore, be primarily responsible for BK-stimulated IP3 generation in endothelial cells.

Original languageEnglish (US)
Pages (from-to)70-75
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume246
Issue number1
DOIs
StatePublished - May 8 1998

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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