title: IgE-binding molecules on human Langerhans cells.
abstract: We have recently demonstrated that normal human Langerhans cells are able to bind IgE. The study of IgE-binding molecules on normal LC led to the characterization of three distinct structures able to bind IgE, viz. the low affinity receptor for IgE, Fc epsilon R2/CD23, the so-called IgE-binding protein epsilon BP which is the human homologous of the murine Mac-2 antigen, and finally the high affinity receptor for IgE, Fc epsilon RI. In this review, we summarize the most recent data on these structures and their putative physiological relevance is discussed with regard to the atopic disease.
authors: Department of Dermatology, Ludwig-Maximilian University Medical School, Munich, Germany.
authors: T
authors: T
authors: Bieber
mesh_terms: D000943:Antigens, Differentiation / Q000276:immunology; D003876:Dermatitis, Atopic / Q000276:immunology*; D037502:Galectin 3; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D007801:Langerhans Cells / Q000276:immunology*; D017455:Receptors, IgE / Q000276:immunology
chemical_list: D000943:Antigens, Differentiation; D037502:Galectin 3; D017455:Receptors, IgE; D007073:Immunoglobulin E