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)

An IgG2a hybridoma antibody (BC-10) was obtained by a myeloma fusion with lymphocytes from B10.RIII mice immunized against native bovine type II collagen. This anti-collagen monoclonal exhibited extensive cross-reactivity with several type II collagen species. BC-10 was found to have self-associating properties, but not the specificity of a typical IgG rheumatoid factor, inasmuch as this mAb bound to F(ab')2 fragments of itself and of normal mouse IgG. Self binding was inhibited by the association of BC-10 with type II collagen, and inhibition assays indicated that antibodies with the capacity to inhibit BC-10 binding to collagen were present in the sera from B10.RIII arthritic mice, but not from DBA/1 LacJ arthritic mice. Joint inflammation and histopathologic features consistent with arthritis were observed in mice injected with the BC-10 hybridoma.
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PMID:A monoclonal anti-type II collagen antibody with cross-reactive anti-Ig activity specific for the F(ab')2 fragment. 326 35

Systemic lupus erythematosus-like graft-versus-host (GVH) disease was induced in 10-week-old male (C57BL/10 X DBA/2) F1 mice by the intravenous injection of spleen and thymus cells (2:1) from 10-week-old male DBA/2 mice. GVH mice were bled at regular intervals 1 month after injection. Antibody to nuclear antigens (ANA) were detected by immunofluorescence using HEp-2 cells as substrate, and antibody to histones and DNA were detected by enzyme-linked immunosorbent assay (ELISA). The titer and frequency of ANA were found to relate directly to the number of donor cells injected. In order to determine the spectrum of ANA in GVH disease, mice were reinjected with optimum cell numbers (120 X 10(6], and splenocytes from two mice with high titer ANA were fused to mouse myeloma cell line P3/X63Ag8.653. Hybridomas were analyzed for ANA by immunofluorescence and ELISA. Sixty-eight clones were found which secreted ANA. Of these, 59% produced antibody to double-stranded DNA, single-stranded DNA, and/or histones and the remainder gave a variety of nuclear immunofluorescence patterns including speckled, homogeneous, nuclear matrix, and nucleolar. This study indicates that GVH disease provides an excellent source of splenocytes for the production of ANA-producing hybridomas as well as a model for the study of autoimmunity.
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PMID:Monoclonal autoantibodies to nuclear antigens from murine graft-versus-host disease. 349 80

Polyclonal IgM obtained by fractionation of a BALB/c serum pool was used as the immunogen for C57BL/6 mice. Draining lymph nodes from selected animals donated cells for fusion with myeloma Sp-2/0. Fifteen hybridomas were productive, and one (RS-3.1) was cloned and the affinity-purified product analyzed for its reactivity pattern by MOPC 104E-enzyme-linked immunosorbent assay inhibition. Among five BALB/c myelomas only TEPC 183 (IgM) was active, not those belonging to other Ig classes. Among normal sera from 8 mouse strains only those of BALB/c, DBA/2J and CBA/J showed inhibition. The recombinant strain BALB-Igh-Va/Igh-Cb did not react, which shows that its C mu stems from parental strain C57BL/6, and that therefore the recombination event had occurred 5' of this gene.
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PMID:Monoclonal anti-allotype antibody towards BALB/c IgM. Analysis of specificity and site of a V-C crossover in recombinant strain BALB-Igh-Va/Igh-Cb. 358 89

The glutathione (GSH) synthesis inhibitor, buthionine sulfoximine (BSO) was tested for cytotoxicity and thiol depletion in murine and human tumor cells in vitro, and for its antitumor activity and toxicity in vivo. The cell lines used in these studies included murine L-1210 leukemia, human RPMI 8226 myeloma, MCF-7 breast cancer and WiDr colon carcinoma. Soft agar colony forming assays showed that BSO was most effective at reducing tumor colony formation when exposed continuously to cells in vitro. Drug concentrations which inhibited colony formation to 50% of control levels ranged from 2.0-6.2 mM (for 1 hour exposures), 2-100 mM for 24 hour exposures and 0.4-1.40 microM (for continuous BSO exposures). Human myeloma cells proved most sensitive to BSO. In vitro cytotoxicity correlated with depletion of intracellular nonprotein sulfhydryls to less than or equal to 10% of control values in both L-1210 and 8226 cells. This was routinely achieved with prolonged exposures to mM BSO concentrations for greater than 24 hours. Normal mice tolerated high BSO doses (up to 5.0 g/kg) without evidence of acute toxicity. BSO was not active against L-1210 leukemia-bearing DBA/2 mice. When tested in vivo against MOPC-315 plasmacytoma-bearing BALB/c mice, BSO was not active at doses up to 4.0 g/kg. In contrast, the bifunctional alkylating agent melphalan (L-PAM) was active against MOPC-315 and this activity was enhanced by a 24 hour pretreatment of mice with 50 mg/kg of L-BSO.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cytotoxic effects of glutathione synthesis inhibition by L-buthionine-(SR)-sulfoximine on human and murine tumor cells. 358 42

A panel of murine monoclonal antibodies (MAbs) was produced by fusing NS-0 myeloma cells with spleen cells of a BALB/c X DBA/2 F1 mouse hyperimmunized against a highly immunogenic subline of the L1210 leukemia obtained by in vivo treatment of the L1210 parental line with the antitumor drug 5-(3,3'-dimethyl-1-triazeno)imidazole-4-carboxamide (DTIC). Among the 52 MAbs produced 16 (anti-D) were specifically cytotoxic in a complement-dependent cytotoxicity assay for the drug-altered subline and the others (anti-L) also cross-reacted with the L1210 parental leukemia. Six anti-D and three anti-L MAbs were selected for detailed studies of tissue specificity. In quantitative absorption experiments the antigens defined by these antibodies could not be detected on cells from normal mouse tissues (lung, liver, kidney, heart, spleen, and thymus). The reactivities of both anti-D and anti-L MAbs against a panel of L1210/DTIC sublines obtained at different times were assayed. The results showed that the antigenic specificities defined by anti-L MAbs were expressed on almost every L1210/DTIC subline while the anti-D MAbs detected antigenic structures specific for the L1210/DTIC used for the immunization. None of the MAbs tested cross-reacted with the L5178Y lymphoma or with its DTIC-altered sublines. The failure of anti-D MAbs to cross-react with cells from other L1210/DTIC sublines supports the hypothesis that the immunological alterations induced by the DTIC treatment are the consequence of mutagenic activity of the drug. On the other hand the presence of anti-L antigens on the cells of every L1210 subline indicates that the DTIC alteration is not accompanied by a loss of the tumor-associated antigen from the L1210 leukemia.
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PMID:Monoclonal antibodies to the L1210 murine leukemia cell line and to a drug-altered subline. 405 6

After human IgG binds to antigen, it attains biological functions that are not properties of monomeric, uncomplexed IgG, including the ability to activate complement and to bind to cellular receptors. Associated with antigen binding, we have recently demonstrated that IgG itself has neoantigenic epitopes. Antibodies to these neoantigens on immune-complexed IgG may represent a significant proportion of circulating anti-human IgG in rabbits immunized with immune complexes. In contrast, mice immunized in an identical fashion have very little circulating anti-neoantigen antibody. This is true whether the mice are genetically easy to tolerize to monomeric human IgG (DBA/2 and C57Bl/6) or difficult to tolerize (BALB/c). Fusions were made between the NS-1 myeloma cell line and spleen cells from mice of each strain, which had been made tolerant to monomeric human IgG and then immunized with immune complexes containing IgG. Like the serum antibody, antibodies made by these fusions showed little specificity for immune complexes since 99% of the hybridoma antibodies that recognized IgG in immune complexes also bound to uncomplexed IgG. Only 1 hybridoma produced antibody that preferentially recognized human IgG in immune complexes. This antibody, called CE9, is an IgM that binds to IgG in plate-bound immune complexes with 100-1000-fold greater avidity than it does to plate-bound uncomplexed IgG. Because CE9 will not bind to immune complexes made with F(ab')2 antibody, the epitope it recognizes requires the Fc fragment of IgG. The minimal binding of CE9 to uncomplexed IgG is easily inhibited by soluble aggregates of IgG, but binding to immune complexes is not inhibited by aggregated IgG. CE9 does recognize fluid-phase immune complexes as well as solid-phase immune complexes. We conclude that, while mice produce much less anti-immune complex antibody than rabbits, anti-neoantigen is still a component of their response to immunization with immune complexes. Using hybridoma techniques to amplify these anti-neoantigen antibodies, we have shown that they resemble rheumatoid factors in their isotype and binding properties.
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PMID:A mouse monoclonal antibody that reacts specifically with immune-complexed human IgG. 407 42

Somatic cell hybridization of NS.1 nonsecretor myeloma cells with spleen cells of (DBA/2 X C57BL/6)F1 mice immunized against the myeloma MOPC 70A of BALB/c mice led to the establishment of five hybridoma clones which continuously secrete anti-MOPC 70A cytotoxic antibodies. The respective antigen detected by each of the five monoclonal antibodies is expressed both on plasmacytomas and on antibody-secreting cells as the only normal cell type. The tissue distribution of this new antigen is different from that reported for the alloantigen PC.1, and we have therefore designated it as PC.2. On the basis of immune elimination of direct and indirect plaque-forming cells, all mouse strains tested express PC.2 determinants, identifying PC.2 essentially as an autoantigen. Conventional anti-PC.1 alloantiserum contains antibodies to the PC.2 determinant, and these antibodies are distinguishable from the anti-PC.1 antibodies proper by the fact that only the latter are absorbed by liver cells. Monoclonal anti-PC.2 antibodies are not directed against MuLV-(murine leukemia virus)--associated antigens as over 20 ecotropic, several MCF (mink colony forming recombinant, and xenotropic viruses failed to react in immunofluorescence assays.
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PMID:A new surface antigen (PC.2) expressed exclusively on plasma cells. 615 21

Two monoclonal rat anti-mouse IgM antibodies, Bet 1 and Bet 2, are described in this paper. Bet 1 defines a new allotypic determinant, Igh-6.5, expressed on IgM molecules in serum and on B lymphocytes, whereas Bet 2 recognizes a determinant on IgM molecules of all mouse strains tested. Both reagents bind to the IgM myeloma protein MOPC104E, but not to IgG myeloma proteins, including FLOPC21, MOPC21, and UPC10. Using serum from various mouse strains to inhibit the binding of Bet 1 to MOPC104E, 3 distinct inhibition patterns were found. BALB/c, DBA/2, and CBA sera inhibited strongly, C56BL/6 (B6), SJL, AKR, and NZB sera inhibited weakly, and A and AL sera showed no inhibition of binding of BET 1 to MOPC104E. All sera tested were equivalent in their inhibition of the binding of Bet 2 to MOPC104E. When spleen cells from different mouse strains were reacted with fluorescein-conjugated Bet 1 (F-Bet 1) and subjected to flow microfluorometry analysis, 3 types of staining patterns, corresponding to those obtained with the serum inhibition assay, were also found. The determinant recognized by Bet 1 is controlled by a gene linked to the Igh-C gene complex. C.AL20 behaved like AL, and C.B20 and BAB/14 behaved like B6, both in the serum inhibition assay and in flow microfluorometry analysis of spleen cells stained with F-Bet 1. In addition, the capacity of serum from individual (BALB/c X B6) X B6 backcross progeny to inhibit the binding of Bet 1 to MOPC104E was linked to the expression of the Ig-1a marker.
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PMID:A mouse IgM allotypic determinant (Igh-6.5) recognized by a monoclonal rat antibody. 616 30

Spleen cells from a DBA/2 mouse immunized with RL male 1 tumor cells, a radiation induced BALB/c T-cell leukemia, were hybridized with the nonsecretor myeloma line NS.1. Four established hybrid cell lines continuously secreted antibodies that recognized a new alloantigenic specificity, tentatively called Ly-m22. This antigen is detectable on nearly 60% of lymph node cells, and 30% of spleen cells by direct cytotoxicity assay, but did not lyse significant number of cells of thymus and bone marrow. By absorption test, these lymphoid organs, i.e., lymph node, spleen, thymus, and bone marrow, were shown to express Ly-m22 determinant. The newly found antigen is expressed predominantly on T-cells. Analysis of BXD and SWXL recombinant inbred strains revealed close linkage between Ly-m22 and Ltw-4 loci on chromosome 1. The estimated recombination frequency is 0.027 +/- 0.081.
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PMID:Mouse alloantigen system Ly-m22 predominantly expressed on T lymphocytes and controlled by a gene linked to M1s region on chromosome 1. 633 54

The expression of tumor-associated antigens on the DBA/2 lymphoma L1210 and three L1210 sublines, each resistant to a different antileukemic agent [guanazole, methylglyoxal-bis(guanylhydrazone), and 4,4-diacetyldiphenylurea-bis(guanylhydrazone)] was investigated by the use of monoclonal hybridoma antibodies. Hybridomas were produced by the fusion of spleen cells from DBA/2 mice immunized with irradiated L1210 or L1210 subline cells and cells of a non-immunoglobulin-secreting BALB/c myeloma variant. Three clones producing antibodies reacting with L1210 or L1210 subline cells were used to study the antigenic expression of L1210 and L1210 subline cells. Monoclonal antibodies from anti-L1210 and anti-L1210 subline hybridomas exhibited a greater reactivity with L1210 subline cells than with L1210 cells in complement-dependent cytotoxicity, quantitative absorption, and membrane immunofluorescence experiments, thereby demonstrating a tumor-associated antigen shared by L1210 and the L1210 sublines and an increased expression of this antigen on subline cells. Cross-blocking tests of antibody binding demonstrated that monoclonal antibodies from anti-L1210 and anti-L1210 subline hybridomas recognized the same or very closely situated antigenic determinants on the tumor cell surface. Most syngeneic and allogeneic tumor cells used as controls failed to react with the anti-L1210 and anti-L1210 subline hybridoma antibodies. However, two syngeneic tumors, L5178Y and P388-D1, demonstrated a significant reaction with the monoclonal antibodies. In addition, several spontaneous mammary tumors from C3H/St and DBA/2Ha, both high-frequency mammary tumor strains, reacted in various degrees with anti-L1210 or anti-L1210 subline hybridoma antibodies in absorption tests and in immunofluorescence experiments. On the other hand, liver, kidney, and spleen from normal C3H/St mice, as well as mammary tumors from BALB/c and C3Hf, both low-frequency mammary tumor strains, did not demonstrate significant reactivity in similar experiments. Normal lactating mammary glands from high-frequency mammary tumor mouse strains reacted with the monoclonal antibodies, whereas lactating mammary glands from low-frequency mammary tumor mouse strains were negative by this method. Purified murine mammary tumor virus preparations reacted strongly with the monoclonal antibodies in solid-phase radioimmunoassays, whereas a purified murine leukemia virus preparation failed to do so in similar experiments. These results indicate that the tumor-associated antigen(s), differentially expressed on L1210 and L1210 subline cells, is related to an antigen which is associated with the murine mammary tumor virus.
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PMID:Differential antigenic expression of the DBA/2 lymphoma L1210 and its sublines: cross-reactivity with C3H mammary tumors as defined by syngeneic monoclonal antibodies. 634 55


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