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Am J Physiol Cell Physiol 277: C859-C869, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 5, C859-C869, November 1999

Receptor phosphorylation does not mediate cross talk between muscarinic M3 and bradykinin B2 receptors

Gary B. Willars1, Werner Müller-Esterl2, and Stefan R. Nahorski1

1 Department of Cell Physiology and Pharmacology, University of Leicester, Leicester, United Kingdom; and 2 Institute of Physiological Chemistry and Pathobiochemistry, Johannes Gutenberg University at Mainz, Mainz, Germany

This study examined cross talk between phospholipase C-coupled muscarinic M3 and bradykinin B2 receptors coexpressed in Chinese hamster ovary (CHO) cells. Agonists of either receptor enhanced phosphoinositide signaling (which rapidly desensitized) and caused protein kinase C (PKC)-independent, homologous receptor phosphorylation. Muscarinic M3 but not bradykinin B2 receptors were also phosphorylated after phorbol ester activation of PKC. Consistent with this, muscarinic M3 receptors were phosphorylated in a PKC-dependent fashion after bradykinin B2 receptor activation, but muscarinic M3 receptor activation did not influence bradykinin B2 receptor phosphorylation. Despite heterologous phosphorylation of muscarinic M3 receptors, phosphoinositide and Ca2+ signaling were unaffected. In contrast, marked heterologous desensitization of bradykinin-mediated responses occurred despite no receptor phosphorylation. This desensitization was associated with a sustained component of muscarinic receptor-mediated signaling, whereas bradykinin's inability to influence muscarinic receptor-mediated responses was associated with rapid and full desensitization of bradykinin responses. Thus the mechanism of functional cross talk most likely involves depletion of a shared signaling component. These data demonstrate that receptor phosphorylation is not a prerequisite for heterologous desensitization and that such desensitization is not obligatory after heterologous receptor phosphorylation.

receptor desensitization; phospholipase C-coupled receptors


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