Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In this report we are able to show that intravenous (i.v.) application (day 0) of a nonapeptide (residues 26-34) from the human C1q A-chain (designated peptide A-C1q) prior to intradermal (i.d.) administration of chicken type II collagen (CII) in arthritis-susceptible DBA/1 mice (H2q), leads to abrogation of polymorphonuclear neutrophil (PMN) invasion into the joints. This nonapeptide exhibits epitope characteristics and high homology to residues 137-147 of CB11 (a cyanogen bromide fragment of chicken CII, known to contain both arthritis inducing and suppressing determinants). Arthritis index was lowest in animals pretreated i.v. with CII (as internal control), though animals pretreated i.v. with peptide K (residues 137-147 with an additional glycine residue from CB11) or peptide A-C1q exhibited comparative arthritic indices. Only in the arthritis-positive control group (day 0: PBS i.v.) did i.d. application of CII lead to invasion of PMN into the synovial layer and the joint space. Analysis of antibody (Ab) responses at day 48 after i.v. immunization (day 0) and CII challenge (day 7) revealed IgE-Abs to native CII and also to native C1q. IgG titers to CII were highest in animals pretreated with peptide A-C1q. Abs from this group, exhibiting activity to peptide A-C1q (immunizing antigen), were of mainly IgG1 and IgG3 isotypes. Evaluation of the immune response following i.v. application of peptide A-C1q or CII, prior to i.d. CII administration, in DBA/1 mice, revealed IgM responses to peptide A-C1q and peptide K, but not to CII. Intravenous application of peptide A-C1q led to generation of IgG3-Abs reacting only with peptide A-C1q and peptide K, but not with native CII. Additionally, i.v. application of peptide A-C1q elicited IgG responses to a pentapeptide, resembling amino acid residues 26-30 (K-G-E-Q-G) of the C1q A-chain. This five residue antigenic determinant is present in peptide K, in chicken and human CII as well as in human C1q. No specific IgE response to any of the antigens tested could be detected. Since a peptide from the C1q A-chain is both capable of eliciting immune responses and modulating CII-induced arthritis in mice, we postulate that the collagen-like complement component C1q is involved in the development of CII-induced inflammatory arthritic lesions, and may represent, in vivo, the early antigen responsible for inducing anticollagen antibodies prior to CII in hyaline cartilage becoming available as antigen.
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PMID:Modulation of type II collagen-induced arthritis in DBA/1 mice by intravenous application of a peptide from the C1q-A chain. 139 37

In a series of works done on humans patterned after animal experimental models, we created an "in vitro" model which allowed us to produce soluble IgE regulator factors. We observed its biological activity in IgE synthesis and constructed changes that protein fractions from affinity chromatography (fractions enriched in soluble regulator IgE factors) exercised on IgE receptor expression. We then decided to determine the molecular weight of each one of the active protein fractions. We performed electrophoresis on the gel of polyacrylamide (Weber-Osborn technique). Protein bands were processed, with the aim of isolating the gel and quantifying the biological activity. The protein fractions obtained from the chromatographies with affinity to CON-A sepharose were subjected to electrophoresis in polyacrylamide gel, with the aim of obtaining molecular weights of proteins comprising it. Using rosette technique, there were no changes seen in Fc epsilon expression just as what happened in the experiment with material fractionated by chromatography. However, these changes are produced and are statistically significant using the immunofluorescence technique. The highest inhibition of rosettes or immunofluorescence is that of the protein band of 10,000 daltons extracted in NaCl and that of 20,000 daltons extracted in PBS. Both effects are similar. The inhibition reached by the 20,000 dalton band in NaCl is less although there are no significant differences. The material extracted in PBS of the band between 6.9 and 7.2 mm of gel (G4) did not have any changes. None of the proteins added to the culture medium had any effects of receptor gamma expression. The average values of the receptor expression was similar to basal levels.
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PMID:IgE receptors (FcR epsilon) modifications. II. Effect of regulator soluble factors of human IgE synthesis, isolated in polyacrylamide gels. 214 48

In previous studies from this laboratory it was shown that OVA(mPEG)n conjugates induced: (i) tolerance in mice with respect to IgG and IgE antibody responses to dinitrophenylated OVA (DNP-OVA); and (ii) OVA-specific suppressor T (Ts) cells which could down-regulate a primary immune response in vivo. For the present study, we have developed an in vitro culture system for assessing the activity of Ts cells of mice tolerized by an OVA(mPEG)13 conjugate. Spleen cells from mice which had been primed with DNP4-OVA in Al(OH)3 gel were cultured with DNP4-OVA to induce a secondary antibody response in vitro. After 6 days, cells secreting anti-DNP antibodies of the IgG1 class were enumerated by an immunoenzymatic plaque-forming cell assay. Addition to the culture of T cells from mice treated with 3 i.p. injections of 500 micrograms of OVA(mPEG)13 resulted in a 29-61% reduction in the number of IgG1 anti-DNP antibody-forming cells, in comparison with the effect of T cells from mice treated with PBS. It was concluded that this tolerogenic conjugate induced splenic Ts cells which were capable of suppressing secondary in vitro anti-DNP responses.
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PMID:Down-regulation of secondary in vitro antibody responses by suppressor T cells of mice treated with a tolerogenic conjugate of ovalbumin and monomethoxypolyethylene glycol, OVA(mPEG)13. 253 91

Lucilia Caesar larvae (LCL) are used as live fish bait by anglers. Five cases of asthma and rhinoconjunctivitis following exposure to LCL are reported. Three had work-related asthma as they were working on a fish bait farm or shop and two had asthma when they went fishing. In one subject exposure to LCL caused asthma, rhinoconjunctivitis and contact urticaria. In four subjects peak expiratory flow rate (PEFR) was monitored during exposure to LCL. In three out of four subjects there was evidence of LCL-related asthma. In one subject it was not possible to record PEFR during exposure to LCL, as he had not gone fishing since 1985. Two extracts of LCL were prepared: one was the PBS (phosphate-buffered saline) washing fluid of LCL, the other was the PBS extract of homogenized LCL. Positive cutaneous prick tests to both LCL extracts were detected in three out of four symptomatic subjects. Specific IgE against both LCL extract antigens were found by the RAST method in four out of five subjects with LCL-related asthma. One subject had both negative skin tests and RAST. Specificity and potency of LCL-IgE binding was shown by RAST inhibition method performed on the serum pool of four patients with positive RAST results. Significant inhibition of more than 50% by LCL washing fluid at a dilution extract was found at a dilution of 1:10 and by homogenized LCL extract at a dilution of 1:100. No significant inhibition of LCL-IgE binding by dermatophagoides, parietaria and milk antigens was found. This study demonstrated that LCL emanations are potent sensitizers and elicit IgE-mediated asthma.
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PMID:[Asthma caused by Lucilia Caesar larvae: clinical and immunologic study]. 263 Aug 95

We investigated in this study the effect of SO2-induced bronchopathy on airway sensitization to ovalbumin in the rat. Sprague-Dawley rats were immunized with a single intratracheal injection of ovalbumin (OA) 100 micrograms in 0.1 ml PBS or 0.1 ml Bordetella pertussis (BP) heat-killed vaccine (6.5 X 10(9) cells X ml-1). The rats were primed immediately after SO2 exposure (60 h, 200 ppm; group I, n = 16) and three months after exposure was achieved (group II, n = 24), then compared to a control group exposed to air (group III, n = 30). Airway sensitization was evaluated by the in vitro contractile response to antigen challenge using paired tracheal rings. Specific IgE level was determined with PCA reactions. No significant difference was found in the maximal contractile responses to carbamyl choline within and between each group. Excepted in animals of group III, OA alone was not found able to sensitize the airways. When OA was used in association with BP, sensitization of the airways occurred, but this occurrence was found to depend upon a previous SO2 exposure: 73.3% in group III, 41.7% in group II and 25% in group I were sensitized. In addition, only five animals (BP + OA injected rats of group III) displayed a PCA positive reaction. It is concluded that: 1) the concomitant intratracheal injection of BP with OA increased the occurrence of specific airway sensitization, 2) a previous chronic exposure to SO2 decreased the specific tracheal smooth muscle sensitization to intratracheal ovalbumin. This decrease persisted, although slighter, when immunization was done three months after the exposure to SO2 was stopped.
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PMID:SO2-induced bronchopathy decreases airway sensitization with intratracheal ovalbumin in the rat. 376 66

The classic histamine release test involved washing and isolating of leukocytes from heparinized whole blood. Siraganian automatized the extraction procedure, working initially with isolated leukocytes in Tris-human serum albumin-Ca++Mg++ buffer, with optimal results. One year later, he described a continuous flow system that permitted the study of whole blood from atopic patients. This method was easier to perform since the isolation of the white blood cells is no longer necessary. On the other hand, the results working with whole blood seem to be better than with isolated leukocytes. We have published modifications of the continuous flow technique, working also with whole blood. Our results agree with those of Siraganian and others. An alternative to working with whole blood or isolated cells in synthetic buffers could be the use of autologous diluted plasma. In this way, the cells are centrifuged and the plasma poured off. The plasma can be used for other determinations, such as RIA, ELISA, etc. The blood is reconstituted to its original volume with a PBS-Ca++Mg++ buffer and processed as described. The results using the whole blood and "washed cells" were very similar. But in some cases we found positive histamine release in "washed leukocytes" but not in whole blood. This striking phenomenon can be explained by the presence in plasma of blocking non-IgE antibodies. If this is the case, the removal of approximately 85% of the plasma will also lead to the disappearance of the 85% of these blocking antibodies. On the other hand, all the positive results obtained using whole blood have been confirmed using "washed cells". Therefore, the use of "washed cells" has several advantages with respect to whole blood assay or leukocyte isolation.
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PMID:[Comparison between automated histamine liberation in whole blood and in isolated cells]. 618 60

Exposure of mice to aerosolized ovalbumin (OA) once weekly for 5 min, or once weekly to 10 microgram OA in PBS intranasally, elicited transient IgE responses which declined by the seventh week. When these animals were challenged intraperitoneally (i.p.) with soluble or alum-precipitated OA, their subsequent IgE responses were markedly suppressed relative to controls. In contrast, i.p. challenge provoked hemaagglutinating antibody (HA) responses to OA in the same animals which were considerably more vigorous than in controls. Adoptive transfer experiments employing splenocytes from mice repeatedly exposed to OA via the respiratory tract revealed the presence of suppressor cells active against OA-specific IgE but not HA responses. Radiotracer studies employing 125I-OA, administered intranasally and by aerosol, indicated that much of the antigen rapidly became associated with the gut.
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PMID:Inhibition of specific IgE responses in mice by pre-exposure to inhaled antigen. 720 28

Coffee workers with occupational allergic symptoms and positive skin tests to green coffee bean and factor dust antigens have elevated serum IgE antibodies (by radioallergosorbent test--RAST) to green coffee and castor bean allergens. These antibodies were used in a RAST inhibition assay to analyse coffee and castor allergens. Bean allergens were extracted by homogenization in PBS, centrifugation and concentration of supernates by ultrafiltration. Green coffee bean allergens, fractionated by gel filtration and Pevikon block electrophoresis, were shown to be very heterogeneous with a molecular weight range of 50 000 to 500 000 daltons. Castor allergens were more homogeneous with a molecular weight of 14 000 daltons and were partially purified by Pevikon block electrophoresis, gel filtration and isoelectrofocusing. Chemical analysis showed that protein was the major component in both allergen extracts. However, proteolytic enzymes could only partially destroy allergenic activity. Such isolation and characterization of these allergens should result in better methods of diagnosis and treatment of coffee workers with occupational allergic disease.
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PMID:Analysis of green coffee bean and castor bean allergens using RAST inhibition. 729 6

The effect of cytokine treatment on the in vivo maturation and Ig isotype switching of human B cells was studied in a modified SCID-hu mouse model. SCID mice, subcutaneously cotransplanted with small fragments of fetal human thymus and bone (SCID-hu BM/T mice) generated all human leukocyte lineages including T and B lymphocytes, macrophages, and granulocytes. All SCID-hu BM/T mice spontaneously produced human IgM and IgG, whereas IgE and IgA were detected in 37 and 80% of the mice, respectively, indicating that productive human T-B cell interactions resulting in Ig isotype switching occur in these mice. Administration of IL-4 to SCID-hu BM/T mice enhanced human B cell maturation, as judged by the increase in the percentages of CD45+, CD19+ bone marrow B cells expressing CD20, CD23, CD40, sIgM, and sIgD. Furthermore, these cells were also functionally more mature because they spontaneously produced human IgG/IgG4 in vitro and could be induced to secrete human IgE by addition of anti-CD40 mAb alone. In contrast, B cells isolated from PBS-treated mice only produced significant Ig levels after stimulation with anti-CD40 mAb in the presence of exogenous IL-4. IL-4 administration also induced human IgE synthesis in 44% of the mice, which had no serum IgE before treatment. More importantly, ongoing human IgE synthesis in SCID-hu BM/T mice was suppressed by > 90% following administration of an IL-4 mutant protein, which acts as an IL-4 and IL-13 receptor antagonist. These results suggest that IL-4/IL-13 receptor antagonists have potential clinical utility in treating human atopic diseases associated with enhanced IgE production.
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PMID:IL-4 induces human B cell maturation and IgE synthesis in SCID-hu mice. Inhibition of ongoing IgE production by in vivo treatment with an IL-4/IL-13 receptor antagonist. 759 71

Specific IgE antibodies against salt-insoluble wheat proteins were investigated in sera from 60 patients with atopic dermatitis (AD) positive to wheat specific CAP-RAST. The salt-insoluble wheat protein fraction was prepared from whole protein fraction of wheat flour, which was extracted by PBS containing 6 M urea. IgE antibodies to salt-insoluble proteins were detected in 15 of the sera. IgE-ELISA was applied to these 15 sera, with whole wheat proteins, salt-soluble proteins, and salt-insoluble proteins used as antigens. Wheat specific CAP-RAST values correlated well with the IgE-ELISA titers against salt-soluble proteins (r = 0.918 p < 0.001). On the other hand, IgE-ELISA titers against both the salt-insoluble proteins and the whole wheat proteins correlated least with CAP-RAST values (r = 0.161 and r = 0.113). The inhibition tests indicated that IgE antibodies against salt-insoluble proteins were different from those against salt-soluble ones. Thus, IgE antibodies to salt-insoluble proteins were another antigen target of IgE-mediated allergy manifestation. To determine the molecular weight of antigens reacting with IgE, IgE-immunoblotting was performed. Several polypeptides with molecular weights of 33-45, 84, 90 and 98 KD were detected. However, the antigen patterns of the blots varied depending on the sera used. These findings suggest that salt-insoluble wheat proteins are the major antigens in some wheat-dependent AD, and that IgE detection against salt-insoluble wheat proteins is important for the diagnosis of wheat allergy.
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PMID:[Detection of IgE antibodies to salt-insoluble wheat proteins in sera of patients with atopic dermatitis by ELISA and immunoblotting techniques]. 764 70


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