Recombinant Soluble Form of the Human High-affinity Immunoglobulin E (IgE) Receptor Inhibits IgE Production through Its Specific Binding to IgE-bearing B Cells


    loading  Checking for direct PDF access through Ovid

Abstract

A recombinant soluble form of the alpha subunit of the human high-affinity receptor for IgE (rsFcepsilonRIalpha), one of the potent IgE-binding molecules, was tested for its ability to regulate IL-4-induced IgE synthesis by human lymphocytes. Addition of rsFcepsilonRIalpha to cultures induced a dose-dependent inhibition of the T cell-dependent and independent synthesis of IgE. The suppression of IgE synthesis was observed at the protein and the mRNA levels, and it was IgE class specific. By flow cytometry, specific binding of rsFcepsilonRIalpha was detected on surface IgE-bearing B cells as well as on U266 cells, and it was completely blocked by preincubation with IgE. rsFcepsilonRIalpha bound to the cell surface IgE could be effectively dissociated not only by a large excess of IgE, but also by an anti-rsFcepsilonRIalpha mAb that competes with IgE for the binding to rsFcepsilonRIalpha. This mAb abolished the rsFcepsilonRIalpha-mediated suppression of IgE synthesis. These data suggest that rsFcepsilonRIalpha may have a function in selectively suppressing IgE synthesis through its interaction with the membrane-bound form of IgE. (J. Clin. Invest. 1994. 94:2162-2165.) Key words: IgE. IgE-binding molecule. IgE-bearing B cells. IL-4. epsilon mRNA

    loading  Loading Related Articles