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)

Three monoclonal antibodies were obtained by the fusion of mouse myeloma cells with splenocytes isolated from BALB/c mice that had been immunized with 8-hydroxy-3,4,7,15-tetraacetyl-nivalenol hemiglutarate covalently bound to bovine serum albumin. These anti-nivalenol tetraacetate monoclonal antibodies were of the IgG type and highly specific to nivalenol tetraacetate, with an apparent association constant of about 10(8)M-1. The relative cross-reactivities of one monoclonal antibody with nivalenol tetraacetate, acetyl T-2 toxin, and scirpenol triacetate were found to be 1.0, 0.02 and 0.03, respectively. Other derivatives showed no cross-reactivity at all. An indirect enzyme-linked immunosorbent assay (ELISA) based on the competitive binding principle was developed using the antibody from clone D18.102.59. The sensitivity of the system was about 0.1 ng of nivalenol tetraacetate per assay. Comparison of nivalenol levels detected in naturally contaminated barley samples by competitive indirect ELISA and gas chromatography (GC) showed good agreement, indicating that the antibody is useful for the measurement of nivalenol in naturally contaminated cereals and grains.
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PMID:Production and characterization of monoclonal antibodies to nivalenol tetraacetate and their application to enzyme-linked immunoassay of nivalenol. 232 18

A review of 52 patients with celiac disease showed the development of malignant tumors in eight cases (15%). The following malignomas were diagnosed: one malignant lymphoma, one multiple myeloma, one rhabdomyosarcoma, one carcinoma of the uterus, one carcinoma of the sigmoid colon and three adenocarcinomas of the small bowel. Patients with tumors showed significantly lower hemoglobin, lower serum albumin, and higher sedimentation rates than patients without tumors. The possibility of underlying malignoma must always be considered in all patients with newly diagnosed coeliac disease and in patients where symptoms of a known celiac disease change without alteration of the prescribed diet.
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PMID:[Risk of malignancies in celiac disease--a retrospective study]. 233 21

It has been assumed, but not documented, that hypercalcemia induces an appreciable reduction in the serum anion gap (AG) because it represents an increase in the level of unmeasured cations. To test this question, we retrospectively compared the data of 59 hypercalcemic patients with malignancy [group 1, serum Ca 13.3 +/- SE 0.3 mg/dl] with those of 108 patients whose hypercalcemia was of parathyroid origin (group 2, serum Ca 12.1 +/- 0.1 mg/dl), and those of 51 control subjects (group 3, serum Ca 9.5 +/- 0.1 mg/dl). The AG of group 2 subjects (8.7 +/- 0.3 mEq/l) was significantly lower than that of the other two groups (p less than 0.001 for both) despite their higher serum albumin and lower serum Ca in comparison to group 1. The AGs of group 1 (11.1 +/- 0.4 mEq/l) and group 3 (11.1 +/- 0.3 mEq/l) were identical. There was no statistically significant correlation between the AG and serum Ca in the hypercalcemic patients. The major finding that the association of hypercalcemia with reduced AG is seen in hyperparathyroidism, but not in malignancy-related hypercalcemia, is not explained by differences in serum albumin, renal function, or acid-base status. Overlap of values between groups limits the diagnostic usefulness of the AG in an individual patient. Nevertheless, in the absence of multiple myeloma, the finding of an AG of 5 mEq/l or less in a hypercalcemic patient may be a helpful clue suggesting that malignancy is not the etiology.
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PMID:Effect of hypercalcemia on the anion gap. 236 30

Six hundred twelve eligible, previously untreated patients with active multiple myeloma and at least some data available for analysis were entered into a randomized trial (Southwest Oncology Group [SWOG] Phase III myeloma study 8229/30), in which the prognostic significance of pretreatment serum beta 2 microglobulin levels was evaluated. Because there was no statistically significant survival difference between the alternating and syncopating VMCP/VBAP regimens, it was possible to evaluate serum beta 2 microglobulin for the total population all together. The serum beta 2 microglobulin measurements showed the highest significance of any prognostic factor, both in the bivariate and multivariate regression analyses. The median survival was 36 months for the 322 patients with pretreatment serum beta 2 microglobulin values of less than 6 micrograms/mL, as compared with a median survival of 23 months for the 225 patients with a beta 2 level of greater than or equal to 6 mcg/mL (P less than .0001). The stepwise multiple regression model first contained serum beta 2 microglobulin, followed by serum albumin, serum calcium, age, and serum creatinine. Serum beta 2 microglobulin was highly correlated with stage: median values ranged from 3.7 micrograms/mL for stage IA, to 10.1 for stage IIIB. It was possible to stratify myeloma patients based on combinations of serum beta 2 microglobulin with both albumin and age, producing excellent separation of patients into low-, intermediate-, and high-risk categories. It is concluded that serum beta 2 microglobulin is the most powerful prognostic factor currently available for multiple myeloma and that it can be used alone or in combination with other variables for pretreatment stratification.
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PMID:Prognostic value of pretreatment serum beta 2 microglobulin in myeloma: a Southwest Oncology Group Study. 220 35

The close relation between rat mast cells and rat basophilic leukemia (RBL) cells with regard to the presence of receptors for IgE and Fc gamma led us to generate monoclonal antibodies directed against cell surface antigens. Hybridomas were obtained by the fusion of NS1 mouse myeloma cells with murine spleen and lymph node cells. The culture supernatants were assayed by two ELISA techniques: a) for the production of mouse immunoglobulin in general and b) for antibodies directed against surface antigens of RBL cells. For this purpose RBL cells were attached to polyvinyl chloride microtitre plates. Eight hybrids produced antibodies directed against surface antigens on RBL cells. Hybrids were cloned and characterized with regard to their isotype and light chains. All eight clones secreted IgM with K light chains. Immunofluorescence studies performed with RBL cells revealed that all eight antibodies were able to show a specific fluorescence. Furthermore, four of these eight antibodies also showed a specific fluorescence with purified rat mast cells. These four antibodies were analyzed as to their ability of interacting with the IgE-receptor on RBL cells and purified rat mast cells. They reduced the binding rate of radiolabelled rat IgE to RBL and rat mast cells. A mutual inhibition of the passive cutaneous anaphylaxis (PCA) reaction in the rat by either mixing mouse reaginic serum directed against 2,4-dinitrophenol bovine serum albumin (DNP-BSA) or by mixing monoclonal mouse anti-DNP IgE with the monoclonal mouse anti-cell surface (rat basophilic leukemia, rat mast cell) IgM was determined.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Interaction of monoclonal antibodies with the IgE-receptor on rat mast cells and rat basophilic leukemia (RBL) cells. 242 99

A hybrid cell line producing monoclonal antibodies recognizing an epitope encoded by the pre-(S)2 region of hepatitis B virus (HBV) genome was obtained by fusion of mouse myeloma cells with lymphocytes from mice immunized with HBV. The monoclonal antibody Mo-F124 secreted from the hybrid line reacted with the pre-S(2) epitope expressed on the surface of both viral and recombinant HBsAg particles--pre-S(2) and S gene product--localised on 34 kD glycoprotein of the viral envelope. The pre-S(2) epitope was sensitive to digestion with V8 protease from Staphylococcus aureus. The enzyme abolished reactivity with Mo-F124 and polymerized human serum albumin (pHSA) binding activity of recombinant particles. Mo-F124 antibody was used to develop highly sensitive radioimmunoassays for determination of pre-S(2) epitope and anti-pre-S(2) antibody in sera of hepatitis B patients. Detection of a pre-S(2) epitope by the monoclonal antibody-based assay in the early phase of acute HBV infection correlated well with the presence of markers of active viral replication (HBeAg, HBV DNA). The appearance of anti-pre-S(2) antibody, usually in the third month after onset of symptoms, was followed by elimination of circulating HBsAg and seroconversion to anti-HBs in all tested cases of uncomplicated acute hepatitis followed by recovery. Anti-pre-S(2) response was not observed in patients with chronic hepatitis B or acute HBV infection progressing to chronic disease. The observed correlation of anti-pre-S(2) response with recovery suggests that the pre-S(2) epitope may represent one of the epitopes inducing antibodies that neutralize the hepatitis B virus.
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PMID:Monoclonal antibody recognizing pre-S(2) epitope of hepatitis B virus: characterization of pre-S(2) epitope and anti-pre-S(2) antibody. 243 50

We constructed a recombinant gene encoding an immunoglobulin (Ig) heavy chain consisting of the variable region from the phosphorylcholine (PC)-specific secreting myeloma MOPC167 and the epsilon constant region from SJL mice. This gene, cloned into the shuttle vector pSV2gpt, was transfected into J558L myeloma cells, and stable transformants that expressed the epsilon gene were cloned. The IgE heavy chain in these transformants is associated with the endogenous lambda light chain and is secreted as an intact IgE molecule. However, the secreted IgE does not bind to PC conjugated to bovine serum albumin (PC-BSA). The MOPC167 kappa chain gene was cloned into the shuttle vector pSV2neo and was transfected into the epsilon heavy-chain transformant. Stable transformants were cloned that expressed both the epsilon heavy chain and the kappa light chain. IgE secreted from such a transformant was shown to bind to PC-BSA. Both types of secreted recombinant IgE bound to rat basophilic leukemia (RBL) cells, but only the IgE produced by the cell line transformed with the MOPC167 kappa gene could be cross-linked with PC-BSA to cause serotonin release.
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PMID:Expression of a recombinant murine IgE in transfected myeloma cells. 243 Oct 59

A panel of monoclonal antibodies was raised against human serum albumin from fusions of BALB/c splenocytes and SP2/0-Ag14 murine myeloma cells. This panel was screened against purified albumins from 21 species including chimpanzee, gorilla, and orangutan. A monoclonal antibody (HSA-1) specific for human albumin was identified. The epitope recognized by HSA-1 was shown to be conserved in all human blood samples tested. A double antibody ELISA assay was developed using biotinylated HSA-1 as the specific probe for human albumin. This assay was capable of detecting as little as 30 nanograms or less albumin/ml. This assay was used to verify the presence of human albumin in blood, tissue extracts, and other body fluids. These results show that the HSA-1 monoclonal antibody can be used in determining the human origin of blood, tissue, and a variety of other body fluids.
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PMID:A unique epitope on human serum albumin recognized by monoclonal antibody HSA-1: a probe for identification of the human origin of blood or tissue. 243 11

The tissue sites of monomeric IgA (mIgA) catabolism were determined in a BALB/c mouse model. Mouse mIgA myeloma proteins were labeled either by direct iodination or by coupling the residualizing label, dilactitol-125I-tyramine (125I-DLT) to the proteins; catabolites from protein labeled with 125I-DLT accumulate at the site of protein degradation, allowing identification of the tissue and cellular sites involved in catabolism of the protein. The circulating half-lives of 125I- and 125I-DLT-mIgA were the same. The distribution of radioactivity in tissues was measured at 1, 3, 24, and 96 h after iv. injection of 125I-DLT-labeled mIgA, dimeric IgA (dIgA), IgG, or mouse serum albumin. The greatest uptake of 125I-DLT-mIgA was attributable to the liver. This organ accounted for more internal catabolism of mIgA than all other tissues combined. In contrast, 125I-DLT-IgG was catabolized equally in skin, muscle, and liver. These data indicate that, in mice, the liver is the major site of mIgA catabolism. To determine the cell types involved, collagenase digestion was used to isolate parenchymal and non-parenchymal cells from perfused liver of animals injected with 125-DLT-mIgA. Most of the radioactivity was associated with the hepatocyte fraction, even though both cell types showed uptake of 125I-DLT-mIgA. Inhibition studies, with asialofetuin and mouse IgA demonstrated that the uptake of mIgA by liver cells was mediated primarily by the asialoglycoprotein receptor.
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PMID:The sites of catabolism of murine monomeric IgA. 245 58

By comparison, it was shown that ascaris protein as carrier was far more effective than BSA and mouse serum albumin to make human c-peptide (HCP) immunogenicity in mice. Twelve monoclonal antibodies (McAb) were obtained after fusion of NS-1 myeloma cells with spleen cells from two BALB/c mice immunized with HCP-ascaris protein conjugate. Eight McAb were characterized and all of them were of IgG1 subclass. Affinities of the McAb for HCP were in the range of 0.03-0.85 X 10(9) mol-1. Although all 8 McAb reacted with both HCP and human proinsulin (HPI), they could specifically recognize human insulin from HPI and were highly species specific without cross-reaction with proinsulin, insulin and c-peptide of other species tested. Through analysis of binding with different HCP fragments, their antigenic determinants were located at either N or C terminal of HCP. The results of plasma HCP radioimmunoassay in 20 normal fasting human adults showed that the value (0.47 +/- 0.16 pmol/ml) determined by rabbit PcAb (R2303) against BSA-HCP was significantly higher than that (0.29 +/- 0.13 pmol/ml) determined by McAb-1.
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PMID:[Studies on monoclonal antibodies directed against human C-peptide]. 247 69


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