Signalling through the high-affinity IgE receptor Fc epsilonRI

H Turner1, J P Kinet

  • 1Department of Pathology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, USA.

Nature
|December 10, 1999
PubMed

Insights

The high-affinity Fc epsilonRI receptor binds immunoglobulin E (IgE) to mast cells and basophils. This binding triggers signaling pathways, leading to allergic responses and potential protection against parasitic infections.

Area of Science:

  • Immunology
  • Cell Biology
  • Allergy Research

Background:

  • The Fc epsilonRI complex is a high-affinity cell-surface receptor for immunoglobulin E (IgE).
  • It is a multimeric receptor involved in initiating intracellular signaling cascades.
  • Fc epsilonRI plays a crucial role in mast cell and basophil activation in humans.

Purpose of the Study:

  • To elucidate the role of Fc epsilonRI in IgE-mediated immune responses.
  • To understand the signaling pathways initiated by Fc epsilonRI aggregation.
  • To explore the involvement of Fc epsilonRI in allergic reactions and parasitic infections.

Main Methods:

  • The study focuses on the molecular interactions and signaling events downstream of Fc epsilonRI activation.
  • Analysis of IgE-mediated antigen presentation and subsequent cellular responses.
  • Investigation of cytokine gene transcription and mediator secretion.

Main Results:

  • Fc epsilonRI aggregation upon multivalent antigen binding triggers diverse intracellular signaling pathways.
  • These pathways lead to the secretion of allergic mediators.
  • Induction of cytokine gene transcription, including interleukin-4, interleukin-6, tumor-necrosis factor-alpha, and granulocyte-macrophage colony-stimulating factor.

Conclusions:

  • Fc epsilonRI is central to the induction and maintenance of allergic responses.
  • The receptor system may provide physiological protection against parasitic infections.
  • Understanding Fc epsilonRI signaling is critical for developing allergy therapies.

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