| Abstract: |
Fc∈RI is a tetrameric receptor, composed of a ligand recognition subunit, α, a β chain, and dimeric γ chains. Previous studies have indicated that the dimeric γ chain is associated with FcγRIIIA (CD16) on natural killer cells and macrophages as well as the clonotypic T cell receptor. Here we show that in mast cells, in addition to the dimeric γ chains, the β subunit is associated not only with Fc∈RI, but also with FcγRIIIA. Functional reconstitution studies with a mastocytoma cell line indicate that FcγRIIIA composed of α, β, and γ subunits has the capacity for signal transduction. These studies suggest that through the association of alternative ligand recognition subunits (β, γ2), a common signal transduction complex (α∈, αγ) mediates similar biochemical and effector functions in response to immunoglobulin G (IgG) and IgE. © 1992, Rockefeller University Press., All rights reserved. |
| Keywords: |
signal transduction; human cell; nonhuman; flow cytometry; protein analysis; animal cell; mouse; animal; gene expression; cell line; calcium; tumor cells, cultured; transfection; tyrosine; phosphorylation; immunoglobulin g; antigen recognition; immunoprecipitation; fc receptor; receptors, igg; antigens, cd; antigens, differentiation; electrophoresis, polyacrylamide gel; immunoglobulin e; rna analysis; mast cell; mast cells; receptors, ige; antigens, differentiation, b-lymphocyte; receptors, fc; human; priority journal; article; inositol phosphates; support, non-u.s. gov't
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