Antibody anti-histamine

Other than protein, histamine in human blood samples was determined by the immunoassay method. It was detected by its binding with anti-histamine IgG, which was coupled to ferrocene (Fc-IgG). Separation of histamine and its complex with antibody was based on p/ differences, and it was achieved in a PMMA chip consisting of a multichannel matrix column coated with a cation-exchange resin (Nation). Histamine was detected electrochemically a decrease in the current due to Fc-IgG occurred after its binding to histamine [1012],... 

Monoclonal antibodies anti-HCG or antihistamine were labeled with ferrocene carboxylic acid 7 in the presence of EDAC alone [33, 34] or in the presence of EDAC and sulfo-NHS [35] to yield immunoconjugates with acceptable immimo-logical activity. They were used in amperometric immunoassays of HCG and histamine, respectively (see Ghapter 8, Sections 8.4.1 and 8.5.3). 

The principle underlying the BAT is that the attachment of the antigen to the IgE present on the surface of the basophil leads to the activation of the basophil and the release of its mediators (histamine, leukotrienes, prostaglandins, etc.) and the expression on its membrane of molecules such as CD63, CD203c or others which are markers of basophil activation. The basophils are identified with monoclonal antibodies marked with fluorochromes and anti-IgE and anti-CD63 receptors [for a complete review, we suggest readers read references 19-22]. 

One limitation of serum-specific IgE is that given the cross-reactivity between different Hymenoptera venoms, and also due to the presence of anti-carbohydrate antibodies, it is frequent to find several simultaneous positive results in patients with non-identified insect stings, a situation which makes diagnosis of the same difficult. In these cases, RAST inhibition and the release of histamine occasionally provide data on the venom involved and when this is not the case, it is advisable to administer immunotherapy against both [44]. 

Interleukin-1 (IL-1) produced by monocytes and several other cell types [70, 146] has a wide array of biological properties, including T cell activation and inflammatory interactions with muscle, liver, fibroblasts, brain and bone [70, 146], IL-1, both natural and recombinant, has been shown to release histamine from human basophils and from human adenoidal mast cells [70,146,151] and this release was abolished by an IL-1 antibody. However, the average release produced by 10 units of IL-1 was less than 20% and there was considerable variability between populations of basophils in the extent of histamine release. Moreover, the secretory response elicited was quite slow (within 15 min) compared with that of other peptides [151]. Desensitization of the basophils by anti-IgE serum had no effect on the subsequent IL-1 response, suggesting different mechanisms of action [ 151], as has been the case with other peptides. Interestingly, the portion of the IL-1 molecule that is responsible for its immu-nostimulatory activity appears to be separate from that portion responsible for its proinflammatory effects [152]. However, that portion of the molecule responsible for eliciting basophil and mast-cell histamine release has not as yet been defined. 

There are other ways in which endotoxins may act to produce cotton dust induced airway disease. These include 1) an instrinsic toxicity due to lipid A, responsible for both pyro-genicity and tissue damage 2) a hypersensitivity reaction involving anti-lipid A antibodies. Further, changes in mechanical properties of the lung could be explained by the release of histamine or serotonin caused by endotoxins. 

Insulin allergy, an immediate type hypersensitivity, is a rare condition in which local or systemic urticaria results from histamine release from tissue mast cells sensitized by anti-insulin IgE antibodies. In severe cases, anaphylaxis results. Because sensitivity is often to noninsulin protein contaminants, the human and analog insulins have markedly reduced the incidence of insulin allergy, especially local reactions. 

Omalizumab is an anti-IgE recombinant humanized monoclonal antibody that is approved for the treatment of allergic asthma in adult and adolescent patients whose symptoms are refractory to inhaled corticosteroids (see Chapter 20). The antibody blocks the binding of IgE to the high-affinity Fes receptor on basophils and mast cells, which suppresses IgE-mediated release of type I allergy mediators such as histamine and leukotrienes. Total serum IgE levels may remain elevated in patients for up to 1 year after administration of this antibody. 

IL-16. IL-16 was originally described as a lymphocyte chemoattractant factor (C4). It is produced by CD8+ T cells upon induction of lectins, histamine, or serotonin (LI). It is also produced by CD4+ T cells stimulated with lectins, antigen, or anti-CD3 antibodies (C5) and from eosinophils (L13), epithelial cells (C5), and mast cells (R8). Recently, IL-16 has been found to induce eosinophil chemotaxis (CIO), and plasma IL-16 is elevated in allergic rhinitis (PH). 

Protein Fv binds specifically to the VH domain of immunoglobulins [22], Consequently, this endogenous protein is similar to multivalent antigens or to divalent anti-IgE antibodies. To evaluate the mechanism whereby this protein activates basophils, we incubated protein Fv with human monoclonal IgM from diverse VH families [19,29], Preincubation of basophils with three preparations of human monoclonal IgM VH3+ concentration-dependently inhibited the histamine-releasing activity of protein Fv. In contrast, a monoclonal IgM that has a Vh6 domain had no such effect. These results are compatible with the hypothesis that protein Fv binds to IgE VH3 + bound to FceRI+ cells. 

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