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

The major allergens of birch (Bet v I), alder (Aln g I), hazel (Cor a I) and hornbeam (Car b I) were investigated by means of high-resolution two-dimensional electrophoresis combined with immunoblotting. Eleven sera derived from patients allergic to birch pollen as well as mouse monoclonal antibodies BIP 1 and BIP 4, raised against Bet v I, were used as probes. Human IgE antibodies detected 10 spots in birch (Mr 17 kDa, pI 4.9-5.9); four spots in alder (Mr 18.5 kDa, pI 4.7-5.3); four spots in hazel (Mr 17 kDa, pI 5.0-5.8); and 12 + 7 spots in hornbeam (Mr 16.5 kDa, pI 4.9-6.6 and Mr 18 kDa, pI 5.2-6.7), respectively, representing major allergens. Each patient tested reacted in a similar fashion with the spot cluster(s) of a certain allergen. BIP 1 detected the same spot clusters as patients' IgE. BIP 4 reacted with the 17-, 18.5- and 18-kDa spots of birch, alder and hornbeam, but did not react with the 17-kDa spots of hazel and the 16.5-kDa spots of hornbeam. In inhibition experiments with birch pollen extract as inhibitor, IgE binding to Bet v I, as well as to Aln g I, Cor a I and Car b I was abolished, thus suggesting that IgE binding to major tree pollen allergens is confined to shared epitopes. These findings indicate that it might be sufficient to use only Bet v I for diagnostic procedures as well as for immunotherapy in patients with tree pollen allergy.
Mol Immunol 1991 Aug
PMID:The immunological relationship of epitopes on major tree pollen allergens. 171 32

Three rat monoclonal antibodies specific for mouse IgE (C12B9, 23G3, and B1E3) were established by using monoclonal anti-DNP mouse IgE (mIgE) as immunogen. These antibodies, as well as a fourth, (R1E4) were characterized. It was found that one antibody (C12B9) recognizes an allotypic determinant (Igh-7a) found on the C epsilon chain of mIgE. Antibody cross-blocking studies and epitope mapping studies using recombinant mIgE indicated that 3 antibodies (C12B9, R1E4 and 23G3) were directed against the C epsilon 3 domain while one (B1E3) was directed against the C epsilon 4 domain. A highly specific sandwich RIA for mIgE was developed using these antibodies. Use of these monoclonal anti-mIgE antibodies in conjunction with recombinant chimeric mIgE-human IgG1 molecules, demonstrated that the C epsilon 3 domain is important in the binding of mIgE to the murine B cell Fc epsilon RII as well as to the murine mast cell F epsilon RI. The presence of the C epsilon 4 domain influenced the binding of the recombinant IgE to the Fc epsilon RII; in contrast to the C epsilon 4 domain had no effect on binding to the Fc epsilon RI.
Mol Immunol 1991 Oct
PMID:Characterization of new rat anti-mouse IgE monoclonals and their use along with chimeric IgE to further define the site that interacts with Fc epsilon RII and Fc epsilon RI. 171 39

Fourteen synthetic peptides of 15 amino acid residues length, overlapping by five residues and spanning the entire sequence of the major allergen Der p II from the house dust mite Dermatophagoides pteronyssinus were synthesized. These peptides were coupled to CNBr-activated Sepharose-4B and used as solid-phase antigens in epitope mapping studies using human IgE antisera. These antibodies bound predominantly to the peptide comprising residues 65-78, the binding of which was inhibited by native Der p II. In addition these antisera bound, to a lesser extent, to the peptide that comprised residues 1-15, which binding was not inhibited by native Der p II. Thus, we found one sequential epitope for a number of IgE sera.
Mol Immunol 1991 Nov
PMID:Epitope mapping of the Dermatophagoides pteronyssinus house dust mite major allergen Der p II using overlapping synthetic peptides. 172 May 4

Expression of Ig isotypes other than IgD together with IgM on the membranes of single B cells has been reported in different experimental models. This paper describes the co-expression of IgG2b or IgE with IgM-IgD on the surface of single B cell subpopulations from normal rats. Their expression was demonstrated with anti-IgE or IgG2b monoclonal antibodies and their F(ab')2 fragments. After pronase digestion, the re-expression of these isotypes together with IgM-IgD was observed in vitro and was inhibited by cycloheximide. These observations imply that mechanisms other than class switching may participate in the expression of membrane isotypes in vivo. The role of these membrane isotypes is still to be established, but could be important as IgG2b molecules are found on a large B cell subpopulation.
Mol Immunol 1992 Jan
PMID:IgG2b or IgE molecules can be co-expressed with those of the IgM and IgD isotypes of the membrane of normal rat B cells. 173 Nov 86

Mugwort (Artemisia vulgaris L.) pollen allergens, separated by SDS-PAGE or IEF, were identified after transfer to NCM by incubation with a panel of sera from 16 patients with clinical mugwort pollen allergy, followed by [125I]anti-IgE and autoradiography. Of the at least 23 components separated by SDS-PAGE in a 15% polyacrylamide gel, at least 15 components with mol. wts 12,000-100,000 bound IgE from the panel of patient sera. A component of mol. wt 22,000 bound IgE from at least 94% of the patient sera tested and for all but three sera this component also bound the greatest quantity of IgE. Five other components with mol. wts 12,000, 17,000, 29,000, 39,000 and 42,000 bound IgE from 75-94% of the patient sera. After separation by IEF, at least 28 protein bands were detected in the pI region 3.5-7.2 and at least seven bands were found in the region 8.6-9.3. At least 11 bands in the pI range 4.2-7.3 and at least five bands in the pI region 8.5-9.2 bound IgE from the panel of patient sera. The most intense radiostaining was observed with a component having a pI of 4.35, which bound IgE from 31% of the patient sera. Immunoblotting of the SDS-PAGE and IEF gels using specific rabbit antisera and human sera against three important mugwort pollen allergens, denoted Ag 9, Ag 12 and Ag 13, was performed to determine the mol. wt and pI of these allergens which had earlier only been identified in CIE/CRIE. The results revealed that Ag 13 had a mol. wt of 61,000 and a pI of 4.35, Ag 12 had a mol. wt of 22,000 and AG 9 had pIs in the region 4.55-5.55 (six isoforms). Ag 9 did not bind IgE after SDS-PAGE and was thus not identified in the SDS-PAGE pattern, and Ag 12 failed to be detected in the NCM after transfer from IEF gels. By crossed immunoelectrofocusing, Ag 12 was found to consist of several isoforms predominantly located in the pI region 3.5-5.1. The immunoblotting analysis also revealed that the glycoprotein allergen Art v II was not detected after transfer from either SDS-PAGE or IEF gels. In conclusion, immunoblotting analysis of SDS-PAGE and IEF gels are useful methods for characterization of mugwort pollen extract, but it should be noted that some important allergens which are easily identified in CIE/CRIE may fail to be detected by these methods.
Mol Immunol 1991 Jul
PMID:Identification and characterization of important allergens from mugwort pollen by IEF, SDS-PAGE and immunoblotting. 185 51

Serotonin release from rat basophilic leukemia (RBL) cells, sensitized with a DNP-binding monoclonal IgE, was stimulated with solid surface (polystyrene)-bound DNP-amino acids. The stimulatory potency of DNP-amino acids was dependent on the structure of amino acid attached to DNP. Generally, DNP-amino acids with high affinities to the sensitizing IgE (I(50) less than 10 microM) were stimulatory in polystyrene-bound form; DNP-amino acids with lower affinities (Pro, Cys, Trp), and aliphatic aromatic DNP-amino acid derivatives were inactive. In addition to structural analogues of DNP, lymecycline, that is chemically unrelated to DNP but was found to have high affinity to IgE(aDNP), was also stimulatory in this system. This drug, and various quinones (e.g. acenaphthene-quinone) in BSA-conjugated forms also stimulated serotonin release from RBL cells sensitized with IgE(aDNP). These studies suggest that (1) There is a threshold of intrinsic ligand binding affinities at approximately I(50) = 10-100 microM; ligands with lower affinities do not stimulate mediator release even if they are presented in multivalent forms; (2) The above affinity threshold for mediator cell stimulation is valid for various ligands, irrespective of their chemical similarity to the immunogen; (3) Multispecific stimulation of mediator release may contribute to the frequently observed allergic cross-reactions, false positive tests for allergies, and anaphylactic reactions to drugs upon first exposure.
Mol Immunol 1991 Jun
PMID:Mechanism of allergic cross-reactions--II. Cross-stimulation, by chemically unrelated ligands, of rat basophilic leukemia cells sensitized with an anti-DNP IgE antibody. 186 80

In vitro co-culture of IgE-secreting hybridoma cells (B53) with spleen cells harvested from mice with established B53 tumours results in a specific, T cell-dependent suppression of epsilon-chain expression in the B53 cells. The role of immunoglobulin enhancers in the suppression of IgE synthesis in B53 cells was examined by transfecting B53 cells with CAT expression vectors containing the immunoglobulin heavy- or kappa light-chain intron enhancers or a Rous sarcoma virus (RSV) LTR. When epsilon-chain expression of transfected cells was suppressed in vitro. CAT expression was also suppressed in cells transfected with vectors containing the immunoglobulin heavy-chain gene enhancer, but not in cells transfected with vectors containing the kappa enhancer or RSV LTR. Thus, the T cell-dependent suppression of IgE synthesis in B53 cells correlates with a specific inactivation of the immunoglobulin heavy chain enhancer, strongly suggesting that T cell-mediated suppression of Ig synthesis can normally occur through specific repression of Ig enhancer function. This represents a new regulatory pathway involved in the control of IgE synthesis and is the first indication that the enhancer mediated expression of Ig genes in B cells can be modulated through T cell-dependent processes.
Mol Immunol 1991 Jun
PMID:Enhancer mediated suppression of epsilon heavy-chain gene expression in a murine IgE-producing hybridoma. 190 51

The main allergen of Parietaria judaica pollen, Par j I, is a glycopolypeptide with mol. wt about 10,000. It shows a considerable charge heterogeneity which is mostly due to the carbohydrate prosthetic groups, since treatment with trifluoromethanesulfonic acid yielded a deglycosylated protein with 8500 mol. wt that displayed only a few bands on IEF, in a narrow pH-region around 5.0. Deglycosylated Par j I exhibited a specific allergenic activity slightly lower than that of native Par j I; however, no allergenic determinants should be located on the sugar moiety since both native and deglycosylated Par j I inhibited up to a similar extent the binding of specific human IgE to P. judaica-coated wells in ELISA. The decrease of specific allergenic activity following deglycosylation could be ascribed to conformational changes evidenced by CD experiments. On the other hand, fluorescence spectroscopy showed that Par j I bears unidentified yellow-brown chromophores strongly linked to the polypeptide chain. These chromophores were not removed by TFMS treatment. Finally, reduction and alkylation caused the complete loss of allergenic activity, showing that disulphide bridges are essential for the IgE-binding ability of Par j I.
Mol Immunol
PMID:Studies on the relationship between structure and IgE-binding ability of Parietaria judaica allergen I. 201 Nov 24

The peptide regulatory factors (PRFs), variously termed cytokines, lymphokines, interleukins, colony stimulating factors, interferons, etc., play a key role in the quantitative and qualitative regulation of protective responses--both in initiating immunological and inflammatory responses and in mediating and controlling the effector mechanisms that protect the body against micro-organisms. The process of immunization--involving antigen-presentation, lymphocyte-activation and clonal proliferation--depends on the action of a variety of PRFs. The function of accessory cells--the dendritic cells, macrophages, etc.--is stimulated by PRFs such as interferon-gamma, IL-1, TNF, GM-CSF and IL-4. The activation and expansion of T-lymphocytes requires IL-1, IL-2, IL-4, interferon-gamma, IL-6 and probably IL-7. Likewise, the activation and expansion of B-lymphocytes is regulated by PRFs such as IL-1, IL-2, IL-4, IL-5, IL-6, IL-7 and interferon-gamma. It is likely, although unproven, that PRFs also regulate the differentiation of B-cells to memory cells. Successful vaccination requires the immune system to be primed in such a way that natural challenge with a micro-organism or its products evokes an immune response that has the qualitative and the quantitative characteristics of both the humoral and cellular responses. Antibody class is critically influenced by particular PRFs, e.g. interferon-gamma regulates IgG2a; IL-4, IgE and IgG1; IL-5 and TGF-beta, IgA. PRFs are both produced by and regulate the T-lymphocytes which have key roles in protective responses--either directly, viz. the cytotoxic T-lymphocytes important in protection against certain viruses, or indirectly through the secretion of PRFs that regulate the speed, magnitude and quality of antibody cellular responses. The recruitment and enhanced production and function of granulocytic and phagocytic cells involves a number of T-lymphocyte PRFs including GM-CSF, IL-3, IL-5, IL-4, and IL-6. We do not have a good understanding of the fine-tuning of cellular responses nor of how infection with different pathogens results in different types of inflammatory responses; it is clear, however, that certain cellular responses are due to the action of specific PRFs, e.g. IL-3 induces a mastocytosis and IL-5 an eosinophilia. There is increasing evidence that the relative levels of different PRFs are important determinants of the effectiveness of responses.(ABSTRACT TRUNCATED AT 400 WORDS)
Mol Immunol 1991 Mar
PMID:Peptide regulatory factors and optimization of vaccines. 201 99

In an effort to identify membrane components participating in coupling stimulus to secretion in mast cells, monoclonal antibodies were produced from spleen cells of mice immunized with plasma membranes isolated from rat mast cells of the RBL-2H3 line. The resultant mAbs were screened by their capacity to modulate the secretory response of these cells to crosslinking of their type 1 Fc epsilon receptor (Fc epsilon RI). Following this scheme, we obtained a hybridoma designated B17, which secretes an IgM-class mAb (B17) that binds to and modulates secretion from RBL-2H3 cells. By immunoblotting, B17 was shown to bind to a membrane component of low molecular weight, later identified as a glycolipid. While B17 partially inhibits IgE binding to RBL-2H3 cells, no noticeable inhibition of B17 binding by IgE was observed. mAb B17 does not cause any secretory response on its own, and its modulatory effect on Fc epsilon RI-mediated secretion is bimodal: it either enhances or inhibits secretion, depending on the B17 dose and also on the nature and dose of the agent used for crosslinking the Fc epsilon RI. When secretion was induced by IgE and suboptimal or optimal doses of multivalent antigen, B17 (2-80 nM) caused an increase in secretion. However, higher doses of B17 (greater than 150 nM) inhibited secretion. Secretion induced by supraoptimal doses of antigen, or by the Fc epsilon RI-specific mAb F4 was inhibited by B17 at all the dose range tested (2-200 nM). In contrast, B17 had no effect on secretion induced by Ca2+ ionophores. These results demonstrate that Fc epsilon RI function is modulated by a mAb binding to a membrane glycolipid.
Mol Immunol 1990 Dec
PMID:A glycolipid-specific monoclonal antibody modulates Fc epsilon receptor stimulation of mast cells. 214 9


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>