Mouse Langerhans cells do not express the high-affinity receptor for IgE

1999 ◽  
Vol 291 (4) ◽  
pp. 241-243 ◽  
Author(s):  
Satoru Hayashi ◽  
Hironori Matsuda ◽  
K. Okumura ◽  
C. Ra
Keyword(s):  
Langerhans Cells ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI).

1992 ◽  
Vol 175 (5) ◽  
pp. 1285-1290 ◽  
Author(s):  
T Bieber ◽  
H de la Salle ◽  
A Wollenberg ◽  
J Hakimi ◽  
R Chizzonite ◽  
...  
Keyword(s):  
Langerhans Cells ◽  
Immunoglobulin E ◽  
Atopic Disease ◽  
High Affinity ◽  
Basophil Cell ◽  
Ku812 Cells ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Human Basophils ◽  
Epidermal Langerhans Cells

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.

New insights in the structure and biology of the high affinity receptor for IgE (FcϵRI) on human epidermal Langerhans cells

1996 ◽  
Vol 13 (1) ◽  
pp. 71-75 ◽  
Author(s):  
Thomas Bieber ◽  
Stefan Kraft ◽  
Maren Jürgens ◽  
Isolde Strobel ◽  
Jörg Haberstok ◽  
...  
Keyword(s):  
Langerhans Cells ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Epidermal Langerhans Cells

Activation of the High Affinity Receptor for IgE on Human Oral Langerhans Cells Leads to the Induction of Tolerogenic Mechanisms

2006 ◽  
Vol 117 (3) ◽  
pp. 720 ◽  
Author(s):  
J. Allam ◽  
B. Niederhagen ◽  
T. Appel ◽  
S. Berge ◽  
T. Bieber ◽  
...  
Keyword(s):  
Langerhans Cells ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals Expression of the High-Affinity Receptor for IgE (Fc∈RI) on Human Langerhans Cells: The End of a Dogma

1992 ◽  
Vol 99 (5) ◽  
pp. S10-S11 ◽  
Author(s):  
Thomas Bieber ◽  
Henri de La Salle ◽  
Corinne de La Salle ◽  
Daniel Hanau ◽  
Andreas Wollenberg
Keyword(s):  
Langerhans Cells ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

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

Cells ◽  
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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