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)

Two monoclonal antibodies with pre-selected submolecular binding specificities to sperm whale myoglobin (Mb) were obtained by hybridizing Fa/0 mouse myeloma cells with spleen cells derived from mice which had been immunized with free (not coupled to any carrier) Mb synthetic peptides 132-153 or 145-151 (antigenic site 5). Both monoclonal antibodies were IgG1 (k). Their homogeneity was confirmed by analytical isoelectric focusing electrophoresis. According to competitive inhibition studies in which Mb, the five synthetic antigenic sites of Mb, Mb peptide 132-153, bovine serum albumin (BSA), and lysozyme were used as inhibitors, the binding specificities of both monoclonal antibodies were restricted to determinants present in the peptides used for immunizations. The results of direct binding studies confirmed this conclusion and suggested that monoclonal antibodies with pre-selected submolecular binding specificities can be readily obtained by the techniques of somatic cell hybridization when the corresponding free synthetic determinants are used as immunogens.
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PMID:Production of monoclonal antibodies with pre-selected submolecular binding specificities to protein determinants: demonstration with sperm whale myoglobin. 618 11

The ability of human IgE-anti-IgE (mouse hybridoma anti-Fc) immune complexes (IC) to generate suppressor T cells for human myeloma IgE synthesis in vitro was tested. T cells incubated with 0.1 micrograms/ml of IC that had an IgE to anti-IgE ratio of 1:1 inhibited myeloma IgE synthesis by 16% more than the control (p less than 0.01). Inhibition was also seen with IC in which the IgE to anti-IgE ratio was higher (2:1 and 4:1), but these differences in synthesis were smaller and were not statistically significant (8 and 3%, respectively, p greater than 0.05). Thymidine incorporation by T cells incubated 3 days with 0.1 microgram/ml of IC at the 1:1 or 2:1 ratio was consistently greater (p less than 0.0025 and less than 0.0125, respectively) than by controls. The IC lost their ability to generate suppressor T cells when the cytophilic site on the IgE molecule was destroyed with heat treatment (0% inhibition with IC at 1:1 and 4% inhibition with IC at 2:1). The activation of T cells with IC showed isotype specificity because the activated T cells failed to suppress IgG and IgA synthesis by the lymphoblastoid cell lines GM-1500 and GM-1056, respectively. T cells were fractionated by incubation with IC and then were panned on plates coated with goat anti-mouse IgG. The adherent cells spontaneously suppressed IgE by 25% when compared to controls (p less than 0.005). These cells failed to suppress IgG and IgA. The activation of the T cells was not due to the panning process itself because activation did not occur with cells that adhered to plates coated with bovine serum albumin (p greater than 0.05) when compared to untreated T cell controls or the IC nonadherent population. These experiments extend previous findings that isotype-specific suppressor T cells for IgE synthesis can be generated in vitro.
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PMID:Isotype-specific human suppressor T cells for IgE synthesis activated by IgE-anti-IgE immune complexes. 623 63

The plasma cell alloantigen PC-1 was isolated from C1.18 myeloma cells by immunoprecipitation and was analyzed by polyacrylamide gel electrophoresis. It was found to consist of two similar or identical disulfide-bonded polypeptide chains, each of Mr 115,000. The mobility of PC-1 in nonequilibrium pH gradient electrophoresis was similar to that of bovine serum albumin (pI 4.9). The PC-1 antigen is therefore similar to the transferrin receptor in Mr, charge, subunit composition, disulfide bonding, and developmental regulation. Similarities can also be detected by peptide mapping with subtilisin, but not with staphylococcal V8 protease. It is suggested that the PC-1 protein and the transferrin receptor may have had a common evolutionary origin, and may have similar functions.
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PMID:Structure of the murine plasma cell alloantigen PC-1: comparison with the receptor for transferrin. 629 94

The ability of purified human myeloma IgG proteins to interact with human plasma fibronectin was studied by enzyme immunoassays. Seven of eight different myeloma IgG proteins representing all four IgG subclasses bound to solid phase fibronectin in a dose-dependent manner. The binding of myeloma IgG to solid phase fibronectin could be inhibited by soluble fibronectin and gelatin, but not by heparin or bovine serum albumin. Evidence for an antigen-antibody type interaction was not observed by double diffusion analysis. Affinity chromatography of radiolabelled cell culture medium over IgG-Sepharose showed that only fibronectin bound to the IgG-conjugates. The affinity of IgG molecules for fibronectin may play a role in cryoimmunoglobulinaemia associated with certain pathological states.
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PMID:Affinity of myeloma IgG proteins for fibronectin. 634 76

Monoclonal antibodies were obtained after fusion of mouse P3 X 63 Ag8.653 myeloma cells with spleen cells isolated from BALB/cCr mice immunized with either DNA modified by 7 beta, 8 alpha-dihydroxy-9 alpha,10 alpha-epoxy-7,8,9,10-tetrahydrobenzo[a]-pyrene (BPDE-I-DNA) complexed electrostatically to methylated bovine serum albumin or with BPDE-I modified guanosine conjugated with bovine serum albumin, BPDE-I-G-BSA. One monoclonal hybridoma line from each type of immunization was grown as ascites tumors or in defined media and characterized in an enzyme linked immunosorbent assay (ELISA). The antibody produced from the spleen cells of a BPDE-I-DNA immunized mouse, designated 5D11, recognizes BPDE-I-DNA and DNA modified by 7 beta,8 alpha-dihydroxy-9 beta,10 beta-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene (BPDE II) but not unmodified DNA, N-2-acetylaminofluorene (AAF) or 1-nitropyrene (NP) modified DNA, BPDE-II-dG or BPDE-I tetraol. It does recognize BPDE-I-dG but with a much lower affinity than when the adduct is present in DNA. In contrast, antibody 8E11 produced from the spleen cells of a BPDE-I-G-BSA immunized mouse recognizes the monoadduct BPDE-I-dG better than BPDE-I-DNA. It also recognizes BPDE-I tetraol but not BPDE-II-DNA, unmodified DNA, AAF- or NP-DNA or BPDE-II-dG. In a noncompetitive ELISA as little as 3 fmol of BPDE-I-DNA adduct can be detected with either antibody 5D11 or 8E11. The combination of the highly sensitive ELISA and highly specific monoclonal antibodies should be valuable in the detection and quantitation of human exposure to benzo[a]pyrene.
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PMID:Monoclonal antibodies to DNA modified by a benzo[a]pyrene diol epoxide. 642 6

Mouse IgG and IgA, with reactivity to dinitrophenol conjugated to carrier protein, have been isolated from myeloma proteins by means of a variety of affinity techniques. The IgA was predominantly in the dimeric form. The in vitro and in vivo biological activities of IgA-containing immune complexes were assessed in the rat. IgA-containing immune complexes were demonstrated, in a dose-dependent manner in vitro, to activate neutrophils and to generate O.-2. In addition, these immune complexes showed evidence of complement activation in vitro, by the use of immunofixation techniques. When IgA was instilled into the airways of rats and antigen was injected intravenously, acute lung injury occurred, as reflected by increases in lung permeability and morphological changes consisting of blebbing of endothelial cells, intra-alveolar hemorrhage, and fibrin deposition. The lung changes were directly proportional to the amount of IgA instilled into the airways and failed to occur if intravenous injection of antigen was omitted. Lung injury did not occur in animals that received an intravenous injection of antigen in the absence of an airway injection of IgA. Lung injury related to IgA-containing immune complexes was complement dependent but neutrophil independent. In companion studies with mouse IgG-containing immune complexes, acute lung injury also occurred and had morphological features similar to those associated with IgA-induced lung injury except that, in the case of IgG immune complex-induced damage, neutrophils were more evident. Acute lung injury induced by IgG-containing immune complexes, whether of mouse or rabbit origin, was complement and neutrophil dependent. The similarities and differences between IgG- and IgA-associated acute immune complex-induced injury of rat lung were reinforced by the use of morphometry techniques. Studies with another monoclonal IgA antibody-containing antigen-binding activity to phosphorylcholine also demonstrated the ability of IgA antibody to cause acute lung injury in the rat. Neither antibody alone nor antigen (phosphorylcholine linked to bovine serum albumin) alone produced evidence of lung injury. These studies indicate for the first time that immune complexes containing IgA have lung-damaging properties and that the pathogenic mechanisms are different from those associated with IgG-associated immune complex-induced acute lung injury.
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PMID:Acute lung injury in rat caused by immunoglobulin A immune complexes. 643 Sep 58

Fc fragments derived from a human IgG1 myeloma protein potentiate the rat delayed-type hypersensitivity (DTH) reaction to antigen challenge. Lewis rats immunized with heat-killed tubercle bacilli give augmented DTH reactions to the purified protein derivative of tuberculin when Fc fragments are included in the challenge dose. Similar potentiation of DTH by pFc' fragments indicates that the active site is located in the CH3 domain of IgG1. Histologic evaluation of the augmented reaction sites revealed predominantly mononuclear cell infiltrates characteristic of DTH reactions. Skin tests of tubercle bacilli-sensitized rats with an unrelated antigen and/or Fc fragments fail to elicit significant reactions. Augmentation of the DTH reaction to purified protein derivative is restricted to the Fc or pFc' region fragments since intact monomeric IgG1, Fab fragments, and bovine serum albumin were all shown not to be active potentiators. The DTH reaction of ovalbumin-sensitized rats was similarly augmented when Fc fragments were included with a challenge dose of ovalbumin, thus supporting the general nature of the phenomenon. These results support the concept of Ig molecules as multifunctional proteins that can not only serve effector functions but also participate in the regulation of immune responses.
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PMID:Potentiation of the rat delayed-type hypersensitivity reaction by the Fc portion of human IgG1. 643 16

By using an indirect enzyme-linked immunosorbent assay, four monoclonal antibodies were selected after fusion of mouse P3-NS1-Ag4-1 myeloma cells with spleen cells isolated from BALB/c mice that had been immunized with aflatoxin M1 (AFM1) conjugated to bovine serum albumin. Two of these antibodies were found to be specific for AFM1 and were designated AMW-1 and AMW-4. The specificities of AMW-1, which had higher affinity to AFM1, were determined by a competitive direct enzyme-linked immunosorbent assay with peroxidase-AFM1 as the marker. The relative cross-reactivity of each toxin (relative to AFM1) with AMW-1, as determined by the amount of aflatoxin necessary to cause 50% inhibition of enzyme activity, was 12, greater than 40, 12, and greater than 40 for B1, B2, G1, and G2, respectively.
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PMID:Production and characterization of monoclonal antibodies against aflatoxin M1. 644 Apr 84

Total and ionized calcium and other related parameters were measured in 34 patients with multiple myeloma. Hypercalcemia was not a major feature of the group of patients studied with only three patients exhibiting marked increases in total (Ca total) and ionized (Ca++) calcium concentrations. The Ca++/Ca total ratio was also maintained within relatively narrow limits. No major differences were found in the calcium fractions of patients with different types of multiple myeloma. Serum immunoreactive parathyroid hormone showed no consistent relationship with either the total or ionized calcium concentration. There were no correlations between increased total protein or reduced serum albumin concentrations and changes in total and ionized calcium fractions or Ca++/Ca total ratios. These results imply that in this group of myeloma patients, there was no significant binding of calcium by the monoclonal immunoglobulins.
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PMID:Frequency of calcium binding by monoclonal immunoglobulins in multiple myeloma. 646 28

We have shown that NS-1 mouse myeloma cells, but not NS-1 hybridomas, required human low density lipoprotein (LDL) for survival and growth in serum-free cell culture (Kawamoto et al., 1983). Here we have further defined the lipid requirement of NS-1 cells by demonstrating that LDL could be replaced by cholesterol complexed with carrier bovine serum albumin (BSA). Cholesterol was the active component of this complex since BSA alone did not promote NS-1 survival or growth. Cholesterol was an absolute requirement of these cells, and it could not be replaced by mevalonolactone. In contrast to NS-1 cells a related mouse myeloma cell line, Sp2/0, did not require cholesterol or other lipids for growth in vitro. Finally, we propose that cholesterol-deficient medium may be an effective alternative to HAT medium for selecting NS-1 hybridomas.
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PMID:Cholesterol requirement of NS-1 mouse myeloma cells for growth in serum-free medium. 653 17


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