Early expression of high-affinity receptor for immunoglobulin E (Fc epsilon RI) during differentiation of mouse mast cells and human basophils.

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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WIP Regulates Signaling via the High Affinity Receptor for Immunoglobulin E in Mast Cells

Journal of Experimental Medicine ◽

10.1084/jem.20030652 ◽

2004 ◽

Vol 199 (3) ◽

pp. 357-368 ◽

Cited By ~ 43

Author(s):

Alexander Kettner ◽

Lalit Kumar ◽

Inés M. Antón ◽

Yoji Sasahara ◽

Miguel de la Fuente ◽

...

Keyword(s):

Mast Cells ◽

Actin Cytoskeleton ◽

Cell Activation ◽

Immunoglobulin E ◽

Mast Cell Activation ◽

Interacting Protein ◽

High Affinity ◽

High Affinity Receptor ◽

Affinity Receptor ◽

Cytoskeleton Rearrangement

Wiskott-Aldrich syndrome protein–interacting protein (WIP) stabilizes actin filaments and is important for immunoreceptor-mediated signal transduction leading to actin cytoskeleton rearrangement in T and B cells. Here we report a role for WIP in signaling pathways downstream of the high affinity receptor for immunoglobulin (Ig)E (FcϵRI) in mast cells. WIP-deficient bone marrow–derived mast cells (BMMCs) were impaired in their capacity to degranulate and secrete interleukin 6 after FcϵRI ligation. Calcium mobilization, phosphorylation of Syk, phospholipase C-g2, and c-Jun NH2-terminal kinase were markedly decreased in WIP-deficient BMMCs. WIP was found to associate with Syk after FcϵRI ligation and to inhibit Syk degradation as evidenced by markedly diminished Syk levels in WIP-deficient BMMCs. WIP-deficient BMMCs exhibited no apparent defect in their subcortical actin network and were normal in their ability to form protrusions when exposed to an IgE-coated surface. However, the kinetics of actin changes and the cell shape changes that follow FcϵRI signaling were altered in WIP-deficient BMMCs. These results suggest that WIP regulates FcϵRI-mediated mast cell activation by regulating Syk levels and actin cytoskeleton rearrangement.

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Functional expression of high-affinity receptor for immunoglobulin E on mast cells precedes that of tryptase during differentiation from human bone marrow-derived CD34 progenitors cultured in the presence of stem cell factor and interleukin-6

Clinical & Experimental Allergy ◽

10.1111/j.1365-2222.2004.01971.x ◽

2004 ◽

Vol 34 (6) ◽

pp. 917-925 ◽

Cited By ~ 9

Author(s):

Y. Shimizu ◽

T. Suga ◽

T. Maeno ◽

F. Aoki ◽

H. Tsukagoshi ◽

...

Keyword(s):

Bone Marrow ◽

Stem Cell ◽

Mast Cells ◽

Interleukin 6 ◽

Stem Cell Factor ◽

Immunoglobulin E ◽

Functional Expression ◽

High Affinity ◽

High Affinity Receptor ◽

Affinity Receptor

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IL-33 and Superantigenic Activation of Human Lung Mast Cells Induce the Release of Angiogenic and Lymphangiogenic Factors

Cells ◽

10.3390/cells10010145 ◽

2021 ◽

Vol 10 (1) ◽

pp. 145

Author(s):

Leonardo Cristinziano ◽

Remo Poto ◽

Gjada Criscuolo ◽

Anne Lise Ferrara ◽

Maria Rosaria Galdiero ◽

...

Keyword(s):

Mast Cells ◽

Human Lung ◽

Protein A ◽

Protein L ◽

Variable Regions ◽

Prolonged Incubation ◽

High Affinity ◽

High Affinity Receptor ◽

Affinity Receptor ◽

Pleiotropic Functions

Human lung mast cells (HLMCs) express the high-affinity receptor FcεRI for IgE and are strategically located in different compartments of human lung, where they play a role in several inflammatory disorders and cancer. Immunoglobulin superantigens (e.g., protein A of Staphylococcus aureus and protein L of Peptostreptococcus magnus) bind to the variable regions of either the heavy (VH3) or light chain (κ) of IgE. IL-33 is a cytokine expressed by epithelial cells that exerts pleiotropic functions in the lung. The present study investigated whether immunoglobulin superantigens protein A and protein L and IL-33 caused the release of inflammatory (histamine), angiogenic (VEGF-A) and lymphangiogenic (VEGF-C) factors from HLMCs. The results show that protein A and protein L induced the rapid (30 min) release of preformed histamine from HLMCs. By contrast, IL-33 did not induce the release of histamine from lung mast cells. Prolonged incubation (12 h) of HLMCs with superantigens and IL-33 induced the release of VEGF-A and VEGF-C. Preincubation with IL-33 potentiated the superantigenic release of histamine, angiogenic and lymphangiogenic factors from HLMCs. Our results suggest that IL-33 might enhance the inflammatory, angiogenic and lymphangiogenic activities of lung mast cells in pulmonary disorders.

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