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Coupling of bradykinin receptors to phospholipase C in cultured fibroblasts is mediated by a G-protein

✍ Scribed by Beth G. Etscheid; Mitchel L. Villereal

Publisher: John Wiley and Sons
Year: 1989
Tongue: English
Weight: 802 KB
Volume: 140
Category: Article
ISSN: 0021-9541
DOI: 10.1002/jcp.1041400211

No coin nor oath required. For personal study only.

✦ Synopsis

In cultured foreskin fibroblasts, bradykinin stimulates inositol phosphate generation, arachidonic acid release, and N a + / H + exchange, with doses of 1-3 n M yielding half-maximal stimulation. Binding of 'H-bradykinin to these cells demonstrates a single receptor site with a Kd of 2.0 n M and a B , , , of 91 fmoles/mg protein. Bradykinin analogs of the B2 type inhibit this binding. CTP synergizes with bradykinin to stimulate phosphatidylinositol turnover in permeabilized fibroblasts and GTP-7-S decreases the B,,,, of bradykiniti binding to fibroblast membranes, indicating that a G-protein couples the receptor to phospholipase C. Pretreatment of fibroblasts with either cholera or pertussis toxin enhances bradykinin stimulation of inositol phosphate accumulation.

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