Related Experiment Video
Updated: Jul 14, 2026
Detection of True IgE-expressing Mouse B Lineage Cells
Published on: December 1, 2014
Soluble CD23 monomers inhibit and oligomers stimulate IGE synthesis in human B cells
Natalie McCloskey1, James Hunt, Rebecca L Beavil
1Medical Research Council Asthma UK Centre in Allergic Mechanisms of Asthma and the Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, United Kingdom. natalie.mccloskey@kcl.ac.uk
Insights
Soluble fragments of the low affinity IgE receptor (CD23) have paradoxical effects on IgE synthesis. Monomeric fragments inhibit, while oligomeric fragments stimulate IgE production in human B cells, offering potential therapeutic targets for allergies.
Area of Science:
- Immunology
- Molecular Biology
- Allergy Research
Background:
- The low affinity IgE receptor, CD23, plays a crucial role in regulating IgE levels.
- CD23 is proteolytically cleaved into soluble fragments with opposing effects on IgE synthesis.
- The molecular mechanisms behind these dual activities remain unclear.
Purpose of the Study:
- To characterize distinct CD23 fragments and elucidate their impact on IgE synthesis.
- To investigate the differential effects of monomeric versus oligomeric CD23 fragments.
- To explore the therapeutic potential of CD23 fragments in allergic diseases.
Main Methods:
- Characterization of three specific CD23 fragments: monomeric derCD23, monomeric exCD23, and oligomeric lzCD23.
- Assay of IgE synthesis in human B cells following heavy chain switching to IgE.
- Comparative analysis of the biological activities of the characterized fragments.
Main Results:
- Monomeric CD23 fragments (derCD23, exCD23) were found to inhibit IgE synthesis.
- The oligomeric CD23 fragment (lzCD23) was shown to stimulate IgE synthesis.
- These opposing effects were observed in human B cells after IgE class switching.
Conclusions:
- The oligomeric state of CD23 fragments dictates their function in regulating IgE synthesis.
- CD23 fragments represent potential therapeutic targets for modulating IgE production in allergic conditions.
- Understanding the structure-function relationship of CD23 fragments is key to developing targeted allergy therapies.
Abstract:
The low affinity IgE receptor, CD23, is implicated in IgE regulation and the pathogenesis of allergic disease. CD23 is a type II integral membrane protein, comprising a lectin "head," N-terminal "stalk," and C-terminal "tail" in the extracellular sequence. Endogenous proteases cleave CD23 in the stalk and the tail to release soluble fragments that either stimulate or inhibit IgE synthesis in human B cells. The molecular basis of these paradoxical activities is not understood. We have characterized three fragments of CD23, monomeric derCD23, monomeric exCD23, and oligomeric lzCD23. We show that the monomers inhibit and the oligomer stimulates IgE synthesis in human B cells after heavy chain switching to IgE. CD23 fragments could be targets for therapeutic intervention in allergic disease.
More Related Videos
08:26The Isolation, Differentiation, and Quantification of Human Antibody-secreting B Cells from Blood: ELISpot as a Functional Readout of Humoral Immunity
Published on: December 14, 2016
11:48Isolation Protocol of Mouse Monocyte-derived Dendritic Cells and Their Subsequent In Vitro Activation with Tumor Immune Complexes
Published on: May 31, 2018
Related Concept Videos
01:24T Cell Types and Functions
Th1 cells stimulate dendritic cells to express necessary co-stimulatory molecules on their surfaces for...
01:24B Cell Activation and Differentiation
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...