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)

There were 72 patients (19 with hepatic failure, 10 with fulminant hepatitis, eight with paraquat poisoning, eight with rheumatoid arthritis, five with myasthenia gravis, four with hyperlipidemia, four with systemic arteriosclerosis including brain infarction, three with pemphigus vulgaris, two with multiple myeloma, two with systemic lupus erythematosus, two cases non-specific Ig-G antibody, two cases medication with an anticancer drug, one with multiple sclerosis, one with Crohn's disease with amyloid kidney and one with chronic myeloblastic leukemia) treated by plasma exchange in the Kidney Center, Tokai University School of Medicine from Jan. 1983 to Dec. 1986. We performed plasma exchange using fresh frozen plasma in 40 cases and Lactate-Ringer's solution containing albumin (4.0-5.0%) in 20 cases as the replacement fluid. In 17 cases, we performed double filtration plasma exchange with the recycle system and no replacement fluid. Although PE therapy did not constitute a basic therapy for hyperlipidemia, pemphigus vulgaris, rheumatoid arthritis, myasthenia gravis, and systemic lupus erythematosus, it was effective in relieving severe clinical symptoms. At the present time, conventional plasma exchange does not improve the survival rate of patients with hepatic failure and fulminant hepatitis. Developments of a new artificial liver support apparatus and identity of many toxic substances in hepatic failure are necessary. No hypotension, hypovolemic shock or other significant complications were experienced.
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PMID:Clinical reports on plasma exchange in the Kidney Center, Tokai University School of Medicine. 344 83

A serum-free in vitro immunization method for the generation of hybridomas producing specific antibodies to an antigen is described. The method was tested with human thyroglobulin as antigen. The serum-free medium used (Yssel et al., 1984) consisted of Iscove's modification of Dulbecco's modified Eagle's medium, supplemented with albumin, transferrin, insulin, ethanolamine and linoleic, oleic and palmitic acids. An optimal response was obtained when splenocytes from BALB/c mice were cultured for 3 days in the presence of 1.5 nM thyroglobulin and thymocyte-conditioned medium prior to fusion with SP2/0 myeloma cells and seeding of the fused cells in microtitre plates. The frequency of positive wells, defined as the number of wells secreting anti-(thyroglobulin) antibodies/number of viable cells used for the fusion, was 1.6 X 10(-6) +/- 0.25 X 10(-6) (mean +/- SD; n = 4). Eight stable clones producing anti-(thyroglobulin) antibodies were isolated. One clone (3D12) produced antibodies reacting only with human thyroglobulin. The antibodies produced by the other clones reacted with human, murine and porcine thyroglobulins. Seven of the clones produced antibodies of the IgM class and one clone produced IgG. The specificity of 3D12 (IgM) for human thyroglobulin and the absence of any reactivity with murine thyroglobulin provides evidence for a primary response of splenocytes in culture to the presence of an antigen.
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PMID:Production of murine monoclonal antibodies against human thyroglobulin using an in vitro immunization procedure in serum-free medium. 348 50

A serum-free medium was developed for culture of plasmacytomas and hybridomas that are dependent upon or independent of the presence of specific P388D1-derived polypeptide growth factors. Possibly due to the stringency of requirements for culturing such plasmacytomas, a highly advantageous combination of components was developed. The medium, SFM, contains RPMI 1640, beta-mercaptoethanol, Hepes buffer, reduced glutathione (GSH), selenite (Se), pyruvate, transferrin, albumin, soybean lipids, and low density lipoproteins. A cooperative effect of GSH and Se is observed. SFM supports the continuous, prodigious growth of every B cell line tested, including a variety of the plasmacytomas, hybridomas, myeloma fusion partners and lymphoma cell lines, as well as the macrophage-like cell line P388D1. All of the B cell lines grow equally as well in SFM as in serum-containing medium. Hybridoma lines from mouse-mouse and rat-mouse fusions continue to produce monoclonal antibodies which can then be purified in a single-step procedure. The cells can be cloned out and frozen down in SFM. In addition, the medium is highly effective for establishment of plasmacytoma cell lines from some transplantable plasmacytomas, including early generation tumors.
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PMID:Serum-free medium for growth factor-dependent and -independent plasmacytomas and hybridomas. 358 96

The rat albumin promoter inserted in adenovirus directs transcription in human and rodent hepatoma cells and in rodent hepatocytes (Friedman et al. 1986) and Babiss et al. (1986) but not in HeLa cells or myeloma cells. The nucleotides between -43 and -156 of the RNA start site of the rat albumin gene are required for this cell-specific expression. Protein binding studies (footprints, exonuclease III stops, and gel shifts) all indicate specific interaction in the -80 to -130 region of the gene with factors present in nuclear extracts of hepatocytes and hepatomas, but also from extracts of other cells that do not express the albumin gene. To observe albumin promoter binding, a smaller amount of extract of liver cell nuclei was required compared to extracts of HeLa cell or kidney cell nuclei. In addition, the various tests of DNA-protein interaction did not give qualitatively identical results with extracts from different cells. However, it seems clear that factors are present in several cell types where albumin genes are inactive that will bind to those DNA sequences demonstrated to be necessary for cell-specific expression of this gene. These factors could either be similar but nonidentical factors or the same factors that are modified differently in different cell types.
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PMID:Factors that interact with the rat albumin promoter are present both in hepatocytes and other cell types. 367 23

Spleen cells of Biozzi HL mouse (selection V) immunized with bovine albumin-triiodothyronine conjugate were fused with P3-X63-Ag8.653 mouse myeloma cells. Thirteen monoclonal antibodies, selected by an enzyme-linked immunosorbent assay and a radioimmunoassay, were produced in mouse ascites fluid, purified and analyzed. All of them were IgG1 (kappa). The cross-reactivity of all these monoclonal antibodies with thyroxine (T4) was less than 0.2%. The association constant determined by Scatchard analysis ranged from 1.5 x 10(9) M-1 to 2.7 x 10(10) M-1.
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PMID:Production and partial characterization of monoclonal antibodies against 3,3',5-triiodo-L-thyronine. 367 56

Somatomedin C, also called insulin-like growth factor I (Sm-C/IGF-I), is a highly conserved polypeptide required for the proliferation of many cell types. Since several attempts in our laboratory to recover monoclonal antibody-secreting hybrids to this peptide by the direct fusion of hyperimmunized splenocytes with myeloma cells had been unsuccessful, we modified our approach by coculturing hyperimmunized BALB/c splenocytes and a small amount of the antigen for 5 days prior to fusion with the P3X63Ag.8.653 myeloma cell line. Of 88 microcultures at risk, specific antibody was detected in 24. Two clones were expanded in ascites fluid and characterized as to isotype, affinity, and specificity. Both were IgG1,kappa and bound human Sm-C/IGF-I with affinity constants of 1.09 and 1.01 X 10(10) liter/mol, respectively. Both clones were quite specific for Sm-C/IGF-I with inconsequential binding to insulin-like growth factor II, multiplication-stimulating activity, any of the chymotryptic fragments of Sm-C/IGF-I, insulin preparations, hGH, hTSH, mEGF, or mouse albumin. In vitro boosting after primary in vivo immunization appears to provide monoclones of an IgG isotype in contrast to primary in vitro immunization, which reportedly favors an IgM isotype. The antibodies produced in this study have proved to be extraordinarily useful in defining the physiologic role of Sm-I/IGF-I with immunoneutralization techniques and in the purification of human Sm-C/IGF-I by affinity chromatography.
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PMID:Derivation of monoclonal antibodies to human somatomedin C/insulin-like growth factor I. 368 3

A comparative study of membrane expression of immunoglobin (Fc) receptors on human eosinophils and neutrophils has been undertaken using human IgG-1, IgG-2, IgG-3, IgG-4, IgA-1, IgA-2, IgM, IgD and IgE myeloma proteins. Sheep erythrocytes (E) coated with either human IgG-1, IgG-2, IgG-3 or IgG-4 myeloma proteins formed rosettes with human neutrophils and eosinophils. Proportionally more (1 1/2-2 times) rosettes were observed with neutrophils compared to eosinophils. In contrast, E-IgE bound to eosinophils (but not to neutrophils) to a degree that was comparable to E-IgG-1. Although IgG and IgE rosettes were inhibited by aggregates prepared from their corresponding myeloma protein there was no evidence that eosinophils and neutrophils have distinct receptors for IgG subclasses. Cells from four patients with hypereosinophilia were separated on density (metrizamide) gradients. The percentages of E-IgG-1 and E-IgE rosettes with normal- and light-density eosinophils were similar. Neutrophils, but not eosinophils, also bound significantly more E-IgA-1 and E-IgA-2 than the E-human albumin (E-Alb) control. In contrast, neutrophil and eosinophil rosette formation with E-IgM and E-IgD was not significantly different from E-Alb or E alone. These experiments indicate that human neutrophils and eosinophils bind homologous IgG subclass myeloma proteins, eosinophils, but not neutrophils, bind E-IgE with a similar avidity to that observed with E-IgG1, neutrophils, but not eosinophils, readily express demonstrable receptors for IgA-1 and IgA-2 and neither neutrophils nor eosinophils form E-IgM or E-IgD rosettes in greater numbers than the E-Alb controls.
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PMID:Binding of immunoglobulin classes and subclasses to human neutrophils and eosinophils. 369 41

The antihemorrhagic factor in opossum (Didelphis virginiana) serum isolated by Sephadex G-200 gel filtration and DEAE A-50 ion exchange chromatography was used as antigen to immunize BALB/c mice. Hybrid cell lines secreting monoclonal antibodies against antihemorrhagic factor were produced by fusion of Sp2/0 myeloma cells with spleen cells of the immunized mice. The ascites fluid was produced in BALB/c mice. The monoclonal antibody in the ascites fluid was partially purified by DEAE A-50 ion exchange and coupled to CNBr-activated isolation of isolation of antihemorrhagic factor. The neutralization capacity of the conventionally isolated antihemorrhagic factor was 14.6 times and the affinity isolated antihemorrhagic factor was 16.8 times that of crude opossum serum. Both antihemorrhagic factors were homogeneous, with one fast migrating band in the area of albumin shown by polyacrylamide gel electrophoresis. However, the antihemorrhagic factor showed one heavy band and one faint band in SDS-polyacrylamide electrophoresis, as well as in isoelectric focusing. The molecular weight of the heavy band was estimated to be 65,000 with a value of p1 4.8 and the faint band was 57,000 with a value of pI 4.1.
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PMID:Isolation of antihemorrhagic factors in opossum (Didelphis virginiana) serum using a monoclonal antibody immunoadsorbent. 375 Mar 45

The results of 24 applications of hemosorption procedure in 19 cases of acute leukemia, chronic myeloleukemia, chronic lymphocytic leukemia and multiple myeloma are discussed. Hemosorption in conjunction with infusions of albumin, hemodesum, rheopolyglucinum, saline and glucose solutions may be recommended for severe and extremely severe toxemia. A high efficiency of the procedure application at different stages of leukemia development in cases of toxemia syndrome, toxico-allergic hepatitis and sepsis was observed.
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PMID:[Hemosorption combined with intensive measures in hemoblastoses]. 386 Oct 25

Mouse myeloma NS1-Ag4 cells were fused with spleen cells from a BALB/c mouse previously immunized with luteinizing hormone releasing hormone (LHRH) conjugated to serum bovine albumin (BSA). Fused cells were grown in HAT restrictive medium which was screened for LHRH binding ability via a primary binding assay employing [125I]LHRH and cold ethanol precipitation. One clone (hy-USASK/DSIL-LHRH-A1) was selected for further study. Cell culture fluid and ascites fluid bound 30% of [125I]LHRH at 1:4000 and 1:400,000 dilution respectively. A competitive inhibition assay using ascites fluid at 1:2,000,000 dilution and LHRH standards at 0.125-32.0 ng/ml was established. Initial studies using rabbit anti-mouse allotype sera in a horseradish peroxidase (HRP)-ELISA system indicate the antibody is IgG1. A dose of 0.5 ml ascites fluid containing LHRH antibody given intravenously (i.v.) on day 9 of gestation was effective in terminating pregnancy in rats. A 1 cm progesterone implant made of elastomer polymer and placed interperitoneally blocked this effect. Ascites fluid (4.5 ml) containing LHRH antibody, when infused i.v. into mature spayed female dogs induced a precipitous decline in mean luteinizing hormone (LH) levels and reduced LH pulsatility over 4 days. It was concluded that the mouse monoclonal antibody is specific for LHRH, and can interrupt reproductive events in vivo.
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PMID:Monoclonal antibodies against LHRH: development and immunoactivity in vivo and in vitro. 388 2


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