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Published on: November 1, 2014
Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI)
T Bieber1, H de la Salle, A Wollenberg
1Department of Dermatology, University of Munich Medical School, Germany.
Insights
Epidermal Langerhans cells (LC) express the high-affinity IgE receptor (Fc epsilon RI), previously found only on mast cells and basophils. This discovery offers new insights into allergic disease mechanisms involving antigen-presenting cells.
Area of Science:
- Immunology
- Dermatology
- Cell Biology
Background:
- Epidermal Langerhans cells (LC) bearing immunoglobulin E (IgE) are implicated in atopic disease genesis.
- The specific IgE receptor on LC was previously unidentified, hindering understanding of allergen binding.
- Identifying the IgE receptor on LC is crucial for elucidating cellular events in allergic responses.
Purpose of the Study:
- To identify the high-affinity IgE receptor on epidermal Langerhans cells (LC).
- To investigate the expression of Fc epsilon RI subunits (alpha, beta, gamma) in LC.
- To compare Fc epsilon RI expression in LC with that of mast cells and basophils.
Main Methods:
- Immunohistochemical staining of epidermal LC with antibodies against Fc epsilon RI alpha subunit.
- Detection of Fc epsilon RI alpha and gamma transcripts in LC using RT-PCR.
- Analysis of Fc epsilon RI beta subunit expression in LC, human basophils, and KU812 cell line.
Main Results:
- Epidermal LC express the high-affinity IgE receptor, Fc epsilon RI.
- LC react with antibodies specific for the Fc epsilon RI alpha subunit.
- LC express transcripts for Fc epsilon RI alpha and gamma subunits, similar to human basophils.
- LC express the Fc epsilon RI beta subunit, indicating the complete receptor structure.
Conclusions:
- Human epidermal LC express the complete high-affinity IgE receptor (Fc epsilon RI).
- This finding suggests a significant role for Fc epsilon RI on LC in antigen presentation and allergic diseases.
- Opens new avenues for understanding the functional role of Fc epsilon RI in immune responses mediated by antigen-presenting cells.
Abstract:
It has been suggested that epidermal Langerhans cells (LC) bearing immunoglobulin E (IgE) may be involved in the genesis of atopic disease. The identity of the IgE receptor(s) on LC remained unclear, although it represents a crucial point in understanding cellular events linked to the binding of allergens to LC via IgE. In this report, we demonstrate that epidermal LC express the high affinity receptor for the Fc fragment of IgE (Fc epsilon RI) which has, so far, only been described on mast cells and basophils. Epidermal LC react with antibodies specific for the alpha subunit of the tetrameric (alpha, beta, 2 gamma) Fc epsilon RI. Specific transcripts for Fc epsilon RI alpha and Fc epsilon RI gamma were detected in LC and correspond to those of human basophils and of the human basophil cell line KU812. Furthermore, human basophils, KU812 cells, and LC express the putative beta subunit. Thus human LC express the complete structure of Fc epsilon RI. This finding opens new perspectives in the putative functional role of this structure on antigen-presenting cells.
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