The high-affinity receptor for immunoglobulin E: a target for therapy of allergic diseases.
The high-affinity receptor for IgE (Fc epsilon RI) on mast cells and basophils is a tetrameric complex, alpha beta gamma 2. Here we summarize the latest developments on the structure and function of this receptor. By genetic transfer, we have engineered a cell line secreting substantial amounts of a peptide containing exclusively the extracellular domain of the alpha-subunit. This domain by itself is sufficient to mediate high-affinity binding of IgE. Glycosylation and the presence of the other subunits are not necessary for the binding function. The gamma-subunit of Fc epsilon RI is part of other receptors such as Fc gamma RIII and the T cell receptor, and therefore is likely to play an important although still undefined functional role. A detailed knowledge of how the receptor interacts with IgE and induces cellular degranulation may lead to the design of new therapeutic approaches to allergic diseases. The potential strategies are discussed.
Kinet
J P
JP
Molecular Allergy and Immunology Section, National Institute of Allergy and Infectious Diseases, Rockville, Md.
Blank
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U
Brini
A
A
Jouvin
M H
MH
Küster
H
H
Mejan
O
O
Ra
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C
D000818:Animals; D000944:Antigens, Differentiation, B-Lymphocyte / Q000737:chemistry / Q000502:physiology*; D001665:Binding Sites; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology / Q000628:therapy*; D007073:Immunoglobulin E / Q000378:metabolism*; D008958:Models, Molecular; D011961:Receptors, Fc / Q000737:chemistry / Q000502:physiology*; D017455:Receptors, IgE
D000944:Antigens, Differentiation, B-Lymphocyte; D011961:Receptors, Fc; D017455:Receptors, IgE; D007073:Immunoglobulin E