Regulation of mRNA Levels of TNF-Alpha and the Alpha Chain of the High-Affinity Receptor for IgE in Mast Cells by IFN-Gamma and Alpha/Beta

1996 ◽  
Vol 110 (2) ◽  
pp. 114-123 ◽  
Author(s):  
Antonio Enciso ◽  
Elyse Y. Bissonnette ◽  
Dean Befus
Keyword(s):  
Mast Cells ◽  
Tnf Alpha ◽  
Mrna Levels ◽  
Ifn Gamma ◽  
Alpha Chain ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Alpha Beta

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.

scholarly journals Measles Virus Spread and Pathogenesis in Genetically Modified Mice

1998 ◽  
Vol 72 (9) ◽  
pp. 7420-7427 ◽  
Author(s):  
Branka Mrkic ◽  
Jovan Pavlovic ◽  
Thomas Rülicke ◽  
Pietro Volpe ◽  
Christian J. Buchholz ◽  
...  
Keyword(s):  
Measles Virus ◽  
Mononuclear Cells ◽  
High Dose ◽  
Peripheral Blood Mononuclear ◽  
High Affinity ◽  
Beta Interferon ◽  
Targeted Mutation ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Alpha Beta

Attenuated Edmonston measles virus (MV-Edm) is not pathogenic in standard mice. We show here that MV-Edm inoculated via the natural respiratory route has a limited propagation in the lungs of mice with a targeted mutation inactivating the alpha/beta interferon receptor. A high dose of MV-Edm administered intracerebrally is lethal for about half of these mice. To study the consequences of the availability of a high-affinity receptor for MV propagation, we generated alpha/beta interferon-defective mice expressing human CD46 with human-like tissue specificity. Intranasal infection of these mice with MV-Edm resulted in enhanced spread to the lungs and more prominent inflammatory response. Virus replication was also detected in peripheral blood mononuclear cells, the spleen, and the liver. Moreover, intracerebral inoculation of adult animals with low MV-Edm doses caused encephalitis with almost inevitably lethal outcome. We conclude that in mice alpha/beta interferon controls MV infection and that a high-affinity receptor facilitates, but is not strictly required for, MV spread and pathogenesis.

scholarly journals CD84 Negatively Regulates IgE High-Affinity Receptor Signaling in Human Mast Cells

2011 ◽  
Vol 187 (11) ◽  
pp. 5577-5586 ◽  
Author(s):  
Damiana Álvarez-Errico ◽  
Irene Oliver-Vila ◽  
Erola Ainsua-Enrich ◽  
Alasdair M. Gilfillan ◽  
César Picado ◽  
...  
Keyword(s):  
Mast Cells ◽  
Receptor Signaling ◽  
High Affinity ◽  
Human Mast Cells ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals Mast cells and mastocytosis

Blood ◽  
2008 ◽  
Vol 112 (4) ◽  
pp. 946-956 ◽  
Author(s):  
Dean D. Metcalfe
Keyword(s):  
Mast Cells ◽  
Kinase Inhibitors ◽  
Allergic Inflammation ◽  
Host Responses ◽  
High Affinity ◽  
Human Mast Cells ◽  
Proinflammatory Mediators ◽  
High Affinity Receptor ◽  
Ige Mediated ◽  
Affinity Receptor

Abstract Mast cells have been recognized for well over 100 years. With time, human mast cells have been documented to originate from CD34+ cells, and have been implicated in host responses in both innate and acquired immunity. In clinical immunology, they are recognized for their central role in IgE-mediated degranulation and allergic inflammation by virtue of their expression of the high-affinity receptor for IgE and release of potent proinflammatory mediators. In hematology, the clinical disease of mastocytosis is characterized by a pathologic increase of mast cells in tissues, often associated with mutations in KIT, the receptor for stem cell factor. More recently, and with increased understanding of how human mast cells are activated through receptors including the high-affinity receptor for IgE and KIT, specific tyrosine kinase inhibitors have been identified with the potential to interrupt signaling pathways and thus limit the proliferation of mast cells as well as their activation through immunoglobulin receptors.

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

2004 ◽  
Vol 199 (3) ◽  
pp. 357-368 ◽  
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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