Signalling through the high-affinity IgE receptor FcεRI

Helen Turner and Jean-Pierre Kinet
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Helen Turner: Laboratory of Allergy and Immunology, Beth Israel Deaconess Medical Center and Harvard Medical School
Jean-Pierre Kinet: Laboratory of Allergy and Immunology, Beth Israel Deaconess Medical Center and Harvard Medical School

Nature, 1999, vol. 402, issue 6760, 24-30

Abstract: Abstract The FcεRI complex forms a high-affinity cell-surface receptor for the Fc region of antigen-specific immunoglobulin E (IgE) molecules. FcεRI is multimeric and is a member of a family of related antigen/Fc receptors which have conserved structural features and similar roles in initiating intracellular signalling cascades. In humans, FcεRI controls the activation of mast cells and basophils, and participates in IgE-mediated antigen presentation. Multivalent antigens bind and crosslink IgE molecules held at the cell surface by FcεRI. Receptor aggregation induces multiple signalling pathways that control diverse effector responses. These include the secretion of allergic mediators and induction of cytokine gene transcription, resulting in secretion of molecules such as interleukin-4, interleukin-6, tumour-necrosis factor-α and granulocyte-macrophage colony-stimulating factor. FcεRI is therefore central to the induction and maintenance of an allergic response and may confer physiological protection in parasitic infections.

Date: 1999
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DOI: 10.1038/35037021

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