Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mouse monoclonal antibodies (MAbs) with different specificities against Dermatophagoides farinae (D. farinae) extract have been obtained. Fifteen of these antibodies reacted with allergen molecules contained in D. farinae and D. pteronyssinus extracts, immunoprecipitating the main allergen of D. farinae (DF29) and homologous allergen of D. pteronyssinus (DP28). In addition, the monoclonal antibody MADF2 immunoprecipitated DF29 together with two other polypeptides (mol. wt 20,000 and 40,000) from D. farinae extracts. Five monoclonal antibodies (MADF2, MADF5, MADF9, MADF10 and MADF13) were selected to study their epitope specificity and the relationship of the epitope location on the allergen with the IgE binding site. By cross-inhibition studies two different epitopes and two partly overlapping determinants were found. In addition, two of these epitopes, those defined by MADF13 and MADF5, are close to, or overlapping, IgE binding site(s) on the allergen molecule. DF29 allergen from D. farinae extract was purified by affinity chromatography using MADF5 coupled to Sepharose. The purified allergen had capacity to bind mite specific human IgE and demonstrated an allergenic activity of up to 70% of total extract of D. farinae. These results indicate that DF29 molecule is the main allergen from D. farinae extracts.
Mol Immunol 1986 Dec
PMID:Isolation and characterization of the main allergen of Dermatophagoides farinae by monoclonal antibodies that recognize IgE related epitopes. 243 43

The major allergen of the pollen of Parietaria judaica was characterized using an anti-allergen MAb AC/15.1. The antibody was able to immunoadsorb four different polypeptides (10,000, 20,000, 30,000 and 40,000 mol. wt) from the pollen proteins radioiodinated by the Bolton-Hunter's reagent. The four polypeptides have been shown not to be covalently linked, except for the 10,000 mol. wt polypeptide (Pj10), which appeared to form Pj10 dimers under non-reducing conditions. All of them contained the antigenic epitope defined by the monoclonal antibody and demonstrated human IgE binding ability. The structural relationship of these polypeptides in the native allergen is discussed.
Mol Immunol 1986 Dec
PMID:Identification of IgE binding polypeptides cross-reactive with the Parietaria judaica main allergenic polypeptide. 243 45

The allergenic composition of a low mol. wt fraction of the pollen extract of Parietaria officinalis (PO) was investigated. Fraction C, that was eluted after oxytocin (mol. wt 1040) when the pollen extract was gel filtered on Sephadex or on Biogel, was cross-reactive in the RAST with the major allergen P015 and was capable of eliciting histamine release from leukocytes of sensitive donors. RAST inhibition (RAST I) analysis of the eluate of gel filtration on Sephadex G-10 revealed several peaks of IgE binding activity. Analysis of fine specificity of response of individual patients carried out by skin-prick tests and by RAST I, revealed individual patterns of reactivity, indicating that allergens contained in fraction C were minor allergens.
Mol Immunol 1987 Mar
PMID:Low molecular weight allergens of the pollen of Parietaria officinalis. 244 Dec 52

A series of monoclonal antibodies (mAb) were produced following the immunization of mice with partially purified IgE receptors from the rat basophilic leukemia cell line (RBL-2H3). Twelve hybridoma cell lines were selected that secreted monoclonal antibodies capable of binding RBL-2H3 plasma membranes. These antibodies were all of the IgG1, or IgG2a subclass. All 12 antibodies bound to either intact or glutaraldehyde-fixed RBL-2H3 cells. Only one monoclonal (mAb 2AC3) inhibited 125I-labeled IgE binding (IC50 = 65 micrograms/ml compared to 1.0 microgram/ml for unlabeled IgE). This same mAb weakly precipitated the alpha component of the receptor from 125I-surface-labeled cells and directly triggered histamine secretion when incubated with RBL-2H3 cells. Therefore, this hybridoma most likely represents a low affinity anti-receptor antibody. Among the other 11 monoclonals, two caused direct histamine secretion from RBL-2H3 cells. These same two, as well as four others, released greater than 10% of total cellular histamine when rabbit anti-mouse antibody was added to cross-link mAb bound to the cell surface. One monoclonal (mA 1AD3) did not trigger histamine secretion but did inhibit IgE-mediated histamine release when incubated with pre-sensitized RBL-2H3 cells. Except for mAb 2AC3, none of the other monoclonal antibodies that caused or inhibited histamine secretion immunoprecipitated receptor or other protein components from either 125I-surface-labeled or intrinsically-labeled cells. However, two monoclonal antibodies (mAb 1CC4 and 1CD1) immunoprecipitated 45,000 and 55,000 proteins from 125I-surface-labeled cells. One hybridoma (mAb 2AA2) that failed to immunoprecipitate surface-labeled proteins did precipitate a 20,000 band from intrinsically-labeled cells. This band increased slightly in apparent mol. wt after reduction and, therefore, was not the previously described gamma component of the receptor. Because several mAb were capable of modulating histamine secretion, it appeared that some of the present monoclonal antibodies bound to undefined membrane components that are crucial to the secretory process of rat basophilic leukemia cells.
Mol Immunol 1987 Apr
PMID:Characterization of monoclonal antibodies produced by immunization with partially purified IgE receptor complexes. 244 33

Polyclonal antisera with pre-determined specificities for a range of rat IgE epitopes were produced by immunizing rabbits with KLH-conjugates of five different synthetic peptides representing sequences 378-396, 414-428, 491-503, 522-535 and 560-571 in the CH3 and CH4 domains of rat IgE. Each rabbit elicited peptide-specific antibodies which were capable of binding affinity-purified rat IgE (IR162) (titres 1/1000-1/10,000) and IgE in rat immunocytoma serum (IR162) either immobilized on microtitre-plates or in free-solution as assessed by ELISA. Heating a solution of rat IgE at 56 degrees C for 1 hr, a treatment known to abolish the cytophilic activity of rat IgE and also induce irreversible conformational changes in the CH3 and CH4 domains, resulted in enhanced binding of the immunoglobulin to antibodies directed against IgE sequences represented by two of the synthetic peptides 414-428 and 491-503, but not to the three other peptides. The five anti-peptide sera together with two previously studied antisera specific for rat IgE sequences 459-472 and 542-557 were tested in functional assays designed to investigate the mode of interaction between rat IgE and its receptor on rat mast cells. Each anti-peptide serum was capable of inhibiting the binding of IgE to mast cells and furthermore, able to initiate the secretion of histamine from cells sensitized with rat IgE in an "anti-IgE"-induced manner. In view of the evidence implicating the CH3 and/or CH4 domains as the location of the mast cell receptor-site on rat IgE, we propose a model to describe the mode of interaction between IgE and its mast cell receptor.
Mol Immunol 1987 Apr
PMID:Analysis of the interaction between rat immunoglobulin E and rat mast cells using anti-peptide antibodies. 244 34

Very sensitive assays of IgE are required for determining prevalence of allergic reactions in children. In order to develop a sensitive two-site IRMA two kinds of mAb were produced. Antibodies specific for D epsilon 1 determinants were derived from immunization with a 40 kDa papain Fc fragment. They bound equally native and 56 degrees C heated IgE. D epsilon 2 specific mAb were obtained after immunization with IgE anti-D epsilon 1 complex and were selected on the basis of their inability to bind heated IgE. In a two-site assay on plastic plates, D epsilon 1 specific mAb led to the binding of IgE but always prevented further binding of anti-D epsilon 1 mAb, anti-human kappa chain mAb or allergen on bound IgE. This was not true when CNBr activated cellulose was used. The influence of the nature of the solid phase disappeared when D epsilon 2 specific mAb were coated on plastic tubes. In this case, the binding of a second mAb with identical or different fine specificity was observed. The best matched pair was E 164 (anti-D epsilon 2) on the solid phase and 6H10 (anti-D epsilon 1) as a tracer. As little as 0.2 UI/ml of IgE could be detected in a 2 hr test.
Mol Immunol 1987 Nov
PMID:Conformational differences of human IgE on hydrophobic and hydrophilic solid phases detected by monoclonal antibodies. 244 90

Degranulation of IgE-sensitized rat mast cells by antigen was studied quantitatively in vitro and in vivo by electron microscopy. The inhibition of this degranulation by an anti-allergic drug, N-(3,4-dimethoxycinnamoyl)anthranilic acid (Tranilast), was also examined both in vitro and in vivo. In the in vitro study using peritoneal mast cells, alteration of the granules, cavity formation by fusion of the perigranular membrane and granule discharge due to fusion of the cavity membrane with the cell membrane were observed and were accompanied by histamine release. Scanning electron microscopy disclosed the extrusion of smooth, round bodies from pores formed on the cell surface. In the in vivo study of passive cutaneous anaphylaxis (PCA), the characteristic features of mast cell degranulation were obvious 5 min after the injection of antigen; leakage of dye increased progressively from 5 to 30 min but was not found at 6 h. From quantitative analysis of the substructure of mast cells, it was demonstrated that degranulation of IgE-sensitized mast cell induced by antigen was achieved by sequential exocytosis both in vitro and in vivo. Tranilast inhibited these changes to a remarkable extent and it was concluded that the inhibition of mast cell degranulation by this drug might play an important role in anti-allergic treatment.
Virchows Arch B Cell Pathol Incl Mol Pathol 1988
PMID:Mast cell degranulation and its inhibition by an anti-allergic agent tranilast. An electron microscopic study. 245 82

In a search for the region in the IgE molecule, which is recognized by the Fc epsilon receptor (Fc epsilon R) on mast cells and basophils, we have generated and characterized anti-IgE monoclonal antibodies (MAbs). The novel rat anti-mouse IgE MAb described herein (denoted 84-1c) interacts with an antigenic determinant which is associated with the Fc epsilon R recognition site on the IgE molecule. The MAb can bind to the Fc epsilon of IgE and block its binding to rat basophil leukemia (RBL) cells. The epitope recognized by 84-1c MAb was completely masked by the Fc epsilon R either in its cellular or soluble form. This epitope was dependent on the native conformation of the IgE molecule and differed from the ones that were recognized by the anti-IgE MAbs we described before.
Mol Immunol 1988 Aug
PMID:Anti-IgE monoclonal antibodies directed at the Fc epsilon receptor binding site. 246 Jul 56

A synthetic peptide corresponding to sequence 91-101 of the Chironomus thummi thummi haemoglobins (Chi t I) components III and IV was used to investigate binding and cross-reactivity with polyclonal human IgE and rabbit IgG antibodies and murine IgG1 subclass monoclonal antibodies (MABs). The synthetic peptide reacted with antibodies from all three mammals. The specificity of the reaction, especially that with IgE antibodies was shown by dose dependent inhibition with native Chi t I component III. Epitope(s) reacting with these antibodies were also found in haemoglobins from 14 of the 15 chironomid species analyzed. The synthetic peptide III/IV 91-101 enabled the identification of an important antigenic/allergenic determinant of the broadly distributed insect family Chironomidae. The antigenic potency of this synthetic peptide as shown by testing with human IgE, rabbit IgG and mouse MABs, and the widespread occurrence of the epitope in an identical or homologous sequence and/or superficial location, qualifies the peptide for therapeutic applications in medicine.
Mol Immunol 1988 Oct
PMID:A common epitope on major allergens from non-biting midges (Chironomidae). 246 34

The antigenic and allergenic profiles of codfish extract have been examined and a comparison made of the specificities of the determinants defined by mouse monoclonal antibodies and human IgE antibodies. By gel electrophoresis, codfish extract was found to comprise a heterogeneous mixture of proteins, in which the principal component and allergen was Gad cI (allergen M). Using monoclonal antibodies and sera from human cod-allergic subjects as immunological probes, common antigenic and allergenic determinants were demonstrated on some codfish proteins. It was also established that, although two monoclonal antibodies recognized the same determinant on Gad cI, there was no cross-reactivity between this determinant and those specified by IgE antibodies in the sera of cod-allergic patients. The specificity of IgE populations directed against Gad cI was found to vary from patient to patient, and was indicative of the existence of two types of allergenic determinants: those unique to a particular allergen and those shared by other proteins in the extract. These studies promote speculation regarding the relative immunogenicity of antigenic and allergenic determinants and the size and diversity of the IgE repertoire, given the potential immunogenicity of the entire protein surface.
Mol Immunol 1989 May
PMID:Common antigenic and allergenic determinants on codfish proteins detected with mouse monoclonal IgG and human IgE antibodies. 247 64


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