IgE+and+ROS
IgE+and+GSH
Comparison of histamine release and prostaglandin E2 production of human basophils in atopic and normal individuals. 1987
Addition of glutathione (GSH), a coenzyme of PGE2-isomerase, increased PGE2 production 2 to 5-fold during stimulation with anti-IgE.
IgE and TNF-α
The regulation of immunoglobulin E class-switch recombination 2003
Regulation of IgE expression 2003
The regulation of immunoglobulin E class-switch recombination 2003
Histamine in allergic inflammation
The role of histamine H1 and H4 receptors in allergic inflammation: the search for new antihistamines 2008
Allergen entering the airways may crosslink immunoglobulin E (IgE) on mast cells (or basophils) to release histamine, lipid mediators and cytokines. Antigen is also processed by airway dendritic cells and macrophages for presentation to T-helper cells. During this process local release of histamine and cytokines may also occur. Resultant histamine from these processes can act on a variety of cells and at different levels.
Histamine can
- facilitate the recruitment of inflammatory cells by direct chemotaxis of additional dendritic cells, eosinophils and mast cells to the airways via action at H4 receptors (blue)
- while also aiding the chemotactic and inflammatory process through effects at H1 receptors (orange) on the airway epithelium and vascular endothelium.
Release of cytokines, such as interleukin 8 (IL8), from the airway epithelium and increased vascular permeability in response to H1 receptor activation enrich the inflammatory milieu. Constriction and proliferation of airway smooth muscle by H1 receptors also contributes to the asthma phenotype. Histamine has diverse effects on the activation of leukocytes by H1 and H4 receptors.
Complex autocrine and paracrine processes in response to dendritic cell histamine and cytokine release control the priming and education of T cells, via cytokines that are released from dendritic cells in response to H1 and H4 receptor activation, during antigen presentation. Histamine may additionally affect the cytokine release from CD8+ cells by H4 receptors and from mast cells, eosinophils and neutrophils through multiple histamine receptor activity. Histamine effects are represented by dashed black arrows, cytokine effects by solid black arrows, and plasma extravasation by red arrows.
IMMUNOGLOBULIN E-RHEUMATOID FACTOR IN JUVENILE RHEUMATOID ARTHRITIS 2002
New drugs for asthma 2004
Factors affecting IgE production
Liver X Receptors Control IgE Expression in B Cells 2009
Papers VDR IgE
Activities affected by IgE
Eur J Immunol. 2009 Dec;39(12):3511-9.
Involvement of hypoxia-inducible factor-1 HiF in IgE-mediated primary human basophil responses.
Basophils play a pivotal role in regulating chronic allergic inflammation as well as angiogenesis. Here, we show for the first time that IgE-mediated activation of primary human basophils results in protein accumulation of the alpha-subunit of hypoxia-inducible factor 1alpha (HIF-1alpha), which is differentially regulated compared with signals controlling histamine release. HIF-1 facilitates cellular adaptation to hypoxic conditions such as inflammation and tumour growth by controlling glycolysis, angiogenesis and cell adhesion. ERK and p38 MAPK, but not reactive oxygen species (ROS), ASK1 or PI 3-kinase, were critical for IgE-mediated accumulation of HIF-1alpha, although the latter crucially affected degranulation. Abrogating HIF-1alpha expression in basophils using siRNA demonstrated that this protein is essential for vascular endothelial growth factor (VEGF) mRNA expression and, consequently, release of VEGF protein. In addition, HIF-1alpha protein alters IgE-induced ATP depletion in basophils, thus also supporting the production of the pro-allergic cytokine IL-4.
Circulating immunoglobulin E (IgE) antibodies to L-thyroxine in a euthyroid patient with multinodular goiter and allergic rhinitis. 1984
A 30-yr-old woman with allergic rhinitis and multinodular goiter developed atopic manifestations on different desiccated thyroid extract treatment. Urticaria was observed when the patient was on L-T4 treatment; no atopy was experienced during L-T3 regimen. Serum total immunoglobulin E (IgE) concentration was 390 +/- 7kU/liter (mean +/- SD) prior to any treatment and rose to 850 +/- 7.5 kU/liter when the patient developed urticaria, but declined to baseline figures while she was on L-T3. Intracutaneous testing was positive for desiccated pork thyroid powder, L-T4 and D-T4, but negative for L-T3, DIT and L-tyrosine. Immunoradioligand analyses of mixtures of patient's serum or precipitated immunoglobulin fraction and of 125I-T4 or of 125I-T3 revealed binding of radiolabeled thyroxine to the patient's serum IgE, in turn bound to anti-human-IgE serum covalently coupled to paper discs. This binding was completely inhibited by the preincubation of immunoglobulin fraction with excess unlabeled L-T4 and D-T4, but not with excess nonradioactive L-T3, thus proving the specificity of the binding. Preadsorption experiments performed with desiccated pork thyroid powder solution mixed with the patient's immunoglobulin fraction suggested binding of some unknown component(s) of desiccated thyroid which was apparently not thyroglobulin. This study provides evidence of IgE antibodies to L-T4 cross reacting with D-T4 and capable of binding 125I-T4 in serum. It also suggests a model for the detection of circulating IgE antibodies to thyroid hormones.
