Journal of Biological Chemistry · 1990 · 150 citations · 21 references
Life SciencesImmunologyMolecular BiologyAllergyHypersensitivityMolecular ImmunologyAllergic DiseaseAntibody CharacterizationChimeric AntibodiesIge-mediated AllergyLigand BindingType I HypersensitivityAntibody Structure-function RelationshipsFc ReceptorsIge-mediated ActivationIge-mediated HypersensitivityIge-mediated ResponsesImmunoglobulin E (Ige)Immunoglobulin E-mediated ResponsesSubunit Association
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.
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Molecular cloning of cDNA encoding human interleukin-2 receptor
Toshio Nikaido, Akira Shimizu, Norio Ishida et al. · Nature · 1984 · 566 citations
Complete structure and expression in transfected cells of high affinity IgE receptor
Ulrich Blank, L Miller, K.N. White et al. · Nature · 1989 · 519 citations