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Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase C gamma 1 in vascular endothelial cells.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Venema VJ,Ju H,Sun J,Eaton DC,Marrero MB,Venema RC

doi

10.1006/bbrc.1998.8574

subject

Has Abstract

pub_date

1998-05-08 00:00:00

pages

70-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)98574-6

journal_volume

246

pub_type

杂志文章

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