Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lymphocytes from normal nonallergic donors and patients with atopic disorders were analyzed for subpopulations bearing Fc receptors for immunoglobulin (Ig)E (Fc(epsilon)) and IgG (Fc(gamma)), surface IgM (sIgM) and IgD (sIgD), and for T cells forming spontaneous rosettes with sheep erythrocytes (E). The patients were divided into three groups according to serum IgE concentrations and systemic corticosteroid treatment. Group I consisted of 12 atopic patients with either normal or moderately increased IgE levels up to 4,000 U/ml. Four patients of group II and three of group III had 10,500-31,000 U/ml and severe atopic dermatitis. Patients of group III, but not I and II, were receiving corticosteroids systemically. The percentage (mean +/-SD) and total number of Fc(epsilon) (+) lymphocytes were 1.2+/-0.5%, 41+/-24/mm(3) in 12 normals; 1.6+/-0.9%, 59+/-43/mm(3) in patients of group I: 7.0+/-2.0%, 187+/-67/mm(3) in group II; and 0.3+/-0.1%, 13+/-5/mm(3) in patients of group III. The increase in group II and decrease in group III of Fc(epsilon) (+) cells were statistically significantly different from the normal persons and patients of group I. In contrast, the patients did not differ significantly from the donors in sIgM(+), sIgD(+), Fc(gamma) (+), and E(+) cell populations. As shown by depletion of sIg(+) cells in four patients with atopic disorders, the great majority of the Fc(epsilon) (+) lymphocytes were B cells. However, two patients with elevated Fc(epsilon) (+) cell numbers had small numbers of mixed E- and Fc(epsilon)-rosetting cells, presumably T cells. Two patients of group II were examined during an acute herpes simplex infection. Both showed an congruent with80% decrease of Fc(epsilon) (+) cells at that time. No apparent correlation between numbers of Fc(epsilon) (+) cells and IgE level existed in patients of group I. Injection of an IgE myeloma protein into two monkeys did not significantly change their percentages of Fc(epsilon) (+) lymphocytes. The data indicate that Fc(epsilon) (+) lymphocytes are increased in patients with markedly elevated serum IgE and severe atopic disease, suggesting that these cells may be involved in the regulation and(or) synthesis of IgE antibody formation.
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PMID:Lymphocytes with immunoglobulin E Fc receptors in patients with atopic disorders. 11 9

In 1966 a new immunoglobulin was found in persons with allergies and in non-typical myeloma proteins. Normally this immunoglobulin E is present only in nanogramms and rests with predilection on the membrane of mast-cells. There is a reaginic-anaphylactic reaction after re-exposure of antigens to the antigen-antibody reaction followed by denudation of mediators of the anaphylactic reaction. With the Radio-Immuno-Sorbent-Test (RIST) the IgE can be quantitatively determined. Elevated IgE-blood levels are typically found in atopic eczema. With the Radio-Allergo-Sorbent-Test (Rast) the allergen specific IgE can be defined. A conformity with appropriate patchtests can be achieved in 60-80% of the cases. In this review advantoses and problem of RIST- and RAST-diagnoses are described. RAST represents a valuable aid in diagnosis of allergies beeing not burdensome and risky, as it is easy to perform and bears no risk to the patients. At the present time, however, patch tests are necessary in the diagnosis of allergies.
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PMID:[IgE and the significance of the radio-allergo-sorbent-test (RAST)]. 79

Leukocyte chemotaxis studies were performed in 14 patients with atopic dermatitis. Monocyte chemotactic responsiveness (MCR), polymorphonuclear leukocyte (PMN) chemotactic responsiveness (PCR), and patient serum inhibition of normal monocyte chemotaxis were evaluated. The most common defect noted was depressed MCR. This was found in 8 of the 14 patients and was associated with a chemotactic inhibitor in the serum of 5 of 6 of the 8 with depressed MCR whose sera were so tested. Depressed PCR was found in 3 of 10 patients studied. Ten of the 14 patients had depressed chemotaxis of at least one cell type. Depressed chemotaxis was not related to the presence of infection, to the serum IgE level, or to the severity of the eczema, and it could not be produced in vitro by incubating normal cells with histamine or IgE myeloma. These studies demonstrate a high frequency of leukocyte chemotactic abnormalities in patients with severe atopic dermatitis. Elucidation of the clinical significance of the leukotactic abnormalities observed and determination of whether they are basic or secondary to the disease process must await further study.
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PMID:Abnormalities of leukotaxis in atopic dermatitis. 87 12

The anti-IgE autoantibody was detected, using a radioimmunoassay, in 17 out of 35 (48.6%) of patients with atopic dermatitis. Significant increased levels of IgG-anti-IgE were seen in the patients studied compared with the control group. The specificity of the anti-IgE autoantibody was confirmed by competitive inhibition assay using IgG, IgM, IgE myeloma. A correlation was observed between the levels of IgG-anti-IgE and serum IgE but not between the IgG subclasses with anti-IgE activity and the clinical status. These data demonstrate that the IgG subclass distribution with anti-IgE activity belongs mostly to the IgG1 and IgG4 subclasses compared with the controls. Moreover, ultracentrifugation analysis indicated that the IgG-anti-IgE in the serum samples from the patients with atopic dermatitis was present in the form of an immune complex with self-IgE. These observations may suggest that the anti-IgE complexes may play a broader role in the modulation of the immune response and that this autoantibody may mask recognition of IgE in conventional assays.
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PMID:Evidence for IgE immune complexes and distribution of IgG subclasses with anti-IgE activity in patients with atopic dermatitis. 191 72

IgE is highly glycosylated, but the function of the oligosaccharide side chains is largely unknown. The previous discovery of an animal lectin, IgE-binding protein (epsilon BP), affords an opportunity to study potential carbohydrate-dependent effector functions of IgE. epsilon BP is a beta-galactoside-specific lectin with binding affinity for IgE and is now known to be equivalent to carbohydrate-binding protein 35 and the Mac-2 Ag; thus, it may have multiple functions in addition to IgE binding. We have previously shown that rat r epsilon BP recognizes sialidase-treated human myeloma IgE to a much greater extent than the untreated IgE. In contrast, human epsilon BP binds essentially equivalently to a monoclonal murine IgE with or without sialidase pretreatment. To validate a possible role for epsilon BP in the IgE system, we investigated the pattern of recognition of epsilon BP for various polyclonal human IgE samples. We show that polyclonal IgE derived from four individuals with hyper-IgE syndrome or atopic dermatitis recognizes epsilon BP and that there is individual variation in the proportion of IgE recognized by epsilon BP, ranging from greater than 60% for one sample to almost undetectable levels in another. We conclude that epsilon BP does indeed recognize polyclonal IgE and that this recognition is modulated by sialylation of IgE oligosaccharides. Furthermore, there exist different IgE glycoforms, varying in the degree of sialylation, and these are distributed in a distinct manner in different individuals.
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PMID:Heterogeneous IgE glycoforms characterized by differential recognition of an endogenous lectin (IgE-binding protein). 191 4

IgG antibodies containing anti-IgE activity isolated from a patient with atopic dermatitis (H-aIgE) induced mediator release from human basophils and mast cells isolated from skin and lung tissues. The release of histamine was calcium- and temperature-dependent and did not involve cytotoxicity. There was an excellent correlation (r = 0.88; p less than 0.001) between the maximum percent histamine release from human basophils induced by rabbit anti-IgE (R-aIgE) and H-aIgE. H-aIgE was approximately 30 times more potent than R-aIgE in inducing mediator release from human basophils, skin, and lung mast cells. H-aIgE specifically desensitized human basophils to a subsequent challenge with both H-aIgE and R-aIgE. Lactic acid removal of IgE from human basophils blocked the releasing activity of both R-aIgE and H-aIgE. Passive sensitization with hyperimmune sera or purified IgE myeloma restored the response of basophils to both R-aIgE and H-aIgE. IgE purified from three different myeloma patients concentration-dependently blocked the histamine releasing activity of both R-aIgE and H-aIgE.
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PMID:IgG anti-IgE from atopic dermatitis induces mediator release from basophils and mast cells. 278 23

A hybridoma-producing monoclonal antibody blocking the binding of human IgE to lymphocytes Fc receptor (Fc epsilon R) was established by the fusion of murine myeloma cells. P3X63.653.Ag8, with BALB/c spleen cells immunized with Fc epsilon R(+) human B lymphoblastoid cell line cells, RPMI1788. A clone of the hybridoma (H107) produced a monoclonal IgG2b antibody that inhibited the rosette formation of Fc epsilon R(+) human B lymphoblastoid cell line cells (RPMI1788, RPMI8866, CESS, Dakiki, and IM9) with fixed ox red blood cells (ORBC) conjugated with human IgE (IgE-ORBC). In contrast, the rosette formation with IgG-conjugated ORBC (IgG-ORBC) on Fc gamma R(+), Fc epsilon R(-) Daudi cells were not affected by the H107 antibodies. A close association of Fc epsilon R and the antigenic determinant recognized by H107 antibody was suggested by the following results. First, the bindings of 125I-labeled IgE (125I-IgE) or 125I-labeled H107 IgG2b antibody (125I-H107) to RPMI8866 cells were inhibited by cold human IgE and H107 IgG2b but not by other classes of human Ig (IgA and IgG), MPC11 IgG2b, or unrelated monoclonal antibodies. Second, H107 antibody reacted with Fc epsilon R(+) B cell lines but not with Fc epsilon R(-) B cell lines as determined by an indirect immunofluorescence. Third, Fc epsilon R(+) cells were depleted by the incubation in the dish coated with H107 antibody or IgE but not in the dish coated with unrelated antibodies. Finally, there was a correlation between the increase of Fc epsilon R(+) cells and that of H107(+) cells in the peripheral blood lymphocytes of the patients with atopic dermatitis. The surface antigens on Fc epsilon R(+) RPMI8866 cells recognized by H107 antibodies had the molecular size of 45,000 as determined by immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis.
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PMID:Monoclonal antibody (H107) inhibiting IgE binding to Fc epsilon R(+) human lymphocytes. 294 2

The presence of Fc receptors for IgE on epidermal Langerhans cells (LC) from patients with atopic dermatitis (AD) was demonstrated by three different types of experiments. Firstly, cell-bound IgE on LC was removed by acid elution and restored by highly purified human myeloma IgE (IgE kappa). Secondly, after pepsin digestion of cell-bound IgE the number of LC staining with anti-human light chain (kappa, lambda) antibodies significantly decreased in contrast to the number of LC staining with anti-human epsilon heavy chain antibody. Thirdly, LC formed rosettes with sheep red blood cells (SRBC) coated with IgE kappa. Epidermal LC from normal non-atopic controls, did not form rosettes with SRBC-IgE. The SRBC-IgE rosette formation could be inhibited by preincubation with IgE kappa and BB10 (MoAb directed against the Fc receptor for IgE on human eosinophils, platelets and macrophages), but also with human IgG, whereas the SRBC-IgG rosette formation could be inhibited neither by IgE kappa nor by BB10. Both the SRBC-IgE and the SRBC-IgG rosette formation could be inhibited by OKT6 (anti-CD1) antibody. The results of inhibition studies with OKT6 antibody on the reconstitution of IgE on epidermal LC after acid elution suggest an associated expression of the CD1 antigen and the Fc receptor for IgE.
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PMID:Associated expression of CD1 antigen and Fc receptor for IgE on epidermal Langerhans cells from patients with atopic dermatitis. 297 37

Modification of a 'sandwich' ELISA assay developed for the determination of serum IgE levels proved to be unsatisfactory for the measurement of IgG4. This was attributed to the limited capacity of the microtitre plate solid phase which required high serum dilutions in order to measure IgG4 levels. To overcome this problem a competitive inhibition assay was developed with monoclonal anti-IgG4 attached to the plate. In this system biotinylated IgG4 myeloma and sample IgG4 compete for the limited antibody binding sites present on the solid phase. The attached biotinylated myeloma is detected by addition of avidin conjugated with peroxidase and following development with substrate, IgG4 levels are calculated by reference to a calibrated inhibition curve. The inhibition ELISA assay has been used clinically to measure IgG4 levels in atopic and normal individuals and the values obtained correlated closely (r = 0.99) with the IgG4 levels determined by radial immunodiffusion. For 43 atopic dermatitis patients investigated the median IgG4 level was 1.1 g/l which was significantly elevated when compared to a median of 0.385 g/l for 60 blood donors (P less than 0.0001, Mann-Whitney U). Among the 47 hay fever patients investigated the median was 0.6 g/l which, although lower than in atopic dermatitis, was again significantly increased (P less than 0.025). Within this latter group, 25 patients were investigated for the effects of desensitization with commercial grass pollen injections. The total IgG4 showed a variable but significant rise between the start and finish of treatment (P less than 0.01 Wilcoxon signed ranks test).
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PMID:Investigation of IgG4 levels in atopic patients using a competitive inhibition assay employing biotinylated IgG4 myeloma and avidin peroxidase. 351 22

We show here an automated (50 samples/h) assay for serum IgG4 having a throughput time of 40 min per sample and a sensitivity of 10 micrograms/ml. The assay procedure is based on the inhibition by sample of the agglutination reaction between monoclonal anti-IgG4 antibodies and latex particles to which IgG4 myeloma protein has been coupled. Assay reliability was ascertained by testing for linearity, analytical recovery (96.4%), interassay precision (less than or equal to 8%), specificity and correlation between the results obtained with monoclonal and polyclonal anti-IgG4 antibodies (n = 84; rs = 0.97). Application of the assay to sera from various groups of patients indicated significantly (p less than 0.00005) higher geometrical means (Gx) in patients suffering from atopy (n = 87; Gx = 617 micrograms/ml), atopic dermatitis (n = 28; Gx = 1,043 micrograms/ml), filariasis with Onchocerca volvulus (n = 48; Gx = 1,681 micrograms/ml) and Brugia malayi (n = 20; Gx = 1,078 micrograms/ml) as compared to nonatopic subjects (n = 103; Gx = 302 micrograms/ml) and randomized paired maternal/cord sera (n = 41; Gx = 276 and 296 micrograms/ml, respectively). IgG4 in the paired maternal/cord sera correlated (r = 0.98; p less than 0.00005). There was no significant influence of age or sex on the IgG4 levels either among the nonatopics or the atopics even though low IgG4 (less than or equal to 30 micrograms/ml) was more common among women. The results suggest that IgG4 and IgE responses are somehow closely related in atopic and parasite-infested patients at the physiological, pathogenic or genetic level.
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PMID:Raised serum IgG4 levels in patients with atopy and filariasis: application of an automated particle-counting immunoassay using monoclonal antibody. 353 90


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