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The Journal of Immunology, 1998, 161: 1000-1006.
Copyright © 1998 by The American Association of Immunologists

Regulation of the High Affinity Receptor for IgE on Human Epidermal Langerhans Cells1

Stefan Kraft*, Jörg H. M. Weßendorf*, Daniel Hanau{dagger} and Thomas Bieber2,*

* Department of Dermatology, Friedrich Wilhelms University, Bonn, Germany; and {dagger} Laboratoire d’Histocompatibilité, Etablissement Régional de Transfusion Sanguine, Strasbourg, France

Human epidermal Langerhans cells (LC) express variable amounts of the high affinity receptor for IgE (Fc{epsilon}RI); the strongest expression is characteristic of atopic dermatitis. The receptor is suggested to take part in the pathophysiology of this disease by acting as a link between aeroallergens and Ag-specific T cells in an IgE-mediated, delayed-type hypersensitivity reaction. In the present study we show that even in the absence of surface expression, normal LC maintain an intracellular pool of the {alpha}-chain of Fc{epsilon}RI (Fc{epsilon}RI{alpha}) of the same m.w. as the surface-bound Fc{epsilon}RI{alpha} that is able to bind significant amounts of IgE. The lack of surface expression is linked to the absence or very low expression of the {gamma}-chain (Fc{epsilon}RI{gamma}). Moreover, the amount of Fc{epsilon}RI{alpha} expressed at the cell surface significantly correlates with the amount of Fc{epsilon}RI{gamma}. LC differentiation toward lymphoid dendritic cells is accompanied by the disappearance of transcripts for Fc{epsilon}RI{alpha}, but not for Fc{epsilon}RI{gamma}. This leads to a rapid decrease in the intracellular and surface levels of Fc{epsilon}RI{alpha}, which cannot be influenced by IL-4, IgE, or other agents. Overall, our findings suggest that these mechanisms enable LC to be highly versatile APCs by rapidly adapting the surface level of Fc{epsilon}RI to distinct inflammatory environments.




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