The alpha subunit of the human IgE receptor (FcERI) is sufficient for high affinity IgE binding

J Biol Chem. 1990 Dec 25;265(36):22079-81.

Abstract

The alpha subunit of the FcERI binds IgE with high affinity. Previous studies have demonstrated that alpha subunit expression requires the presence of beta and/or gamma subunits, and it is not known how these two subunits contribute to the ability of the alpha subunit to bind IgE. In this report, we describe the expression and characterization of a human chimeric alpha subunit. The data demonstrate that high affinity IgE binding does not require the presence of the beta and/or gamma subunits and that this activity is localized to the extracellular domain (residues 26-201) of the human alpha subunit. Permanent cell lines expressing the chimeric receptor were used to characterize the binding parameters of the alpha subunit. These cell lines provide a means of identifying therapeutic agents which may be effective in the treatment/management of allergic diseases.

MeSH terms

  • Animals
  • Antigens, Differentiation, B-Lymphocyte / genetics
  • Antigens, Differentiation, B-Lymphocyte / metabolism*
  • Binding, Competitive
  • Cell Line
  • Fluorescent Antibody Technique
  • Genetic Vectors
  • Humans
  • Immunoglobulin E / isolation & purification
  • Immunoglobulin E / metabolism*
  • Kinetics
  • Macromolecular Substances
  • Rats
  • Receptors, Fc / genetics
  • Receptors, Fc / metabolism*
  • Receptors, IgE
  • Recombinant Proteins / metabolism
  • Transfection

Substances

  • Antigens, Differentiation, B-Lymphocyte
  • Macromolecular Substances
  • Receptors, Fc
  • Receptors, IgE
  • Recombinant Proteins
  • Immunoglobulin E