Abstract
The interaction of ligands with the mouse macrophage Fc receptor which binds IgG2b and IgG1 immune complexes (FcRγ2b/γ1) triggers phagocytosis and secretion of various mediators of inflammation1–4. FcRγ2b/γ1 has been purified using a monoclonal anti-FcR antibody, 2.4G2 (refs 5, 6), and seems to be an integral membrane glycoprotein of molecular weight (Mr) 47,000–60,000 (ref. 6). Monoclonal antibody 2.4G2 is suitable as a tool for functional studies of FcR because it binds to a functional site of the receptor and induces cellular responses that are normally associated with the occupied receptor5,7,8. We reported previously that binding of ligands to the macrophage FcR resulted in Na+/K+ ion fluxes through the plasma membrane, and that similar ion fluxes were observed in proteoliposomes containing reconstituted FcR9,10. We have now incorporated FcR into planar lipid bilayers and report here that FcRγ2b/γ1 forms ligand-dependent cation-selective ion channels, with a conductance of 60 pS in 1M KCl and an average open channel lifetime of 250ms. The conductance decays to baseline levels within a few minutes. These results suggest a receptor–ionophore model for the signalling of phagocytosis and inflammatory responses.
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Ding-E Young, J., Unkeless, J., Young, T. et al. Role for mouse macrophage IgG Fc receptor as ligand-dependent ion channel . Nature 306, 186–189 (1983). https://doi.org/10.1038/306186a0
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DOI: https://doi.org/10.1038/306186a0
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