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 polyclonal B cell activators, lipopolysaccharide (LPS) and poly I:C, have been used to induce interferon (IFN) production by murine B cell populations. The results show that splenic B cell-enriched fractions, isolated by wheat germ agglutination followed by C-dependent anti-Thy 1.2 cytolysis, respond to treatment with poly I:C + DEAE-dextran by IFN production at levels comparable on a per cell basis to unfractionated spleen cells. By contrast, the LPS-stimulated IFN response of these same B cell fractions is either undetectable or substantially lower than that of spleen cells; although the B cell fractions appear fully capable of LPS-induced proliferation. Consistent with this pattern of splenic B cell IFN responses, two antibody-secreting hybridoma lines and two myeloma cell lines (including the parental myeloma of the hybrid) can be stimulated by poly I:C + DEAE-dextran to produce IFN; yet these same B cell lines do not synthesize IFN in response to LPS at doses from 1-100 micrograms/ml. The level of poly I:C-induced IFN secreted by the hybridomas are approximately 10-fold greater than that produced by the unfused parental myeloma cells. Not only do these results directly demonstrate that murine lymphocytes of the B cell lineage produce IFN in response to the B cell activator poly I:C, but these observations also strongly suggest that the IFN responses of the B cell tumor lines model the IFN producing capacity of splenic B cells. Moreover, since the hybridoma cell lines and one of the myeloma lines synthesize specific antibody molecules, these observations show that the progeny of a single B cell clone can synthesize and secrete both IFN and immunoglobulin.
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PMID:Differences in the B cell interferon responses to lipopolysaccharide and poly I:C. 618 67

Hybridomas have been prepared by fusing mouse myeloma (P3 X 63 Ag8) cells with spleen cells of mice immunized with a yeast fraction enriched with respect to non-ribosomal translational components. Cloned hybridoma lines were grown in the form of ascites tumors, and the monoclonal antibodies produced were purified from the ascites fluid by chromatography on DEAE-Affi-Gel Blue. One of the antibodies, from a hybridoma cell line designated as PSH-1, inhibited the translation of natural mRNA and poly(U) and polysomal chain elongation in a cell-free protein-synthesizing system from yeast. Resolution and partial purification of the elongation factors indicated that the monoclonal antibody from PSH-1 did not interact with EF-1 or EF-2 but reacted with and inactivated EF-3, the 125 000 molecular weight additional elongation factor specifically required with yeast ribosomes. The EF-3 purified from the cytosol by immunoaffinity chromatography was comparable to that prepared by ion-exchange chromatography. Evidence was obtained which indicated that EF-3 was essential for the translation of natural mRNA as well as poly(U), was associated with polysomes but not ribosomal subunits, and was required for every cycle in the elongation phase of protein synthesis.
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PMID:Monoclonal antibody specific for yeast elongation factor 3. 638 May 81

Rats were immunized with the purified BCL1-IgM lambda 3(1) and their spleen cells were fused with Sp2/0 cells. Hybridomas secreting antibodies reactive with lambda 1-, lambda 2-, and lambda 3-containing myeloma proteins were subcloned and propagated in spinner culture. The antibodies were tested in a solid-phase radioimmunoassay and by indirect immunofluorescence using either BCL1 cells or normal mouse spleen cells. One of the monoclonal antibodies was purified to 95% homogeneity on DEAE-Sephadex. The purified anti-lambda anti-body, coupled to Sepharose, was mitogenic for lambda-bearing normal B cells and BCL1 cells, and in the presence of a supernatant from Concanavalin-A (Con A) stimulated these cells to secrete IgM lambda.
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PMID:Induction of proliferation and differentiation of murine B cells bearing surface Ig lambda by rat monoclonal antibody to lambda chain. 643 81

A hybridoma cell line secreting monoclonal antibody specific for glutathione-insulin transhydrogenase has been produced by fusing mouse myeloma cells with spleen cells from mice immunized to purified rat liver glutathione-insulin transhydrogenase. The secreted antibody isotypes were found to be: Ig gamma 1 heavy chains and kappa light chains. This monoclonal antibody has been used to screen glutathione-insulin transhydrogenase in various rat tissue extracts (liver, fat, heart, testis, spleen, lung and kidney) following separation on NaDodSO4/urea polyacrylamide disc-gel electrophoresis and electrophoretic transfer to nitrocellulose. Screening with the monoclonal antibody showed the presence of one immunoreactive protein band equal in molecular weight to that of purified rat liver GIT (Mr 53,000) in extracts of all tissues studied and a second immunoreactive protein band of lower molecular weight (Mr 49,000) in spleen and lung tissue extracts. Separation of these two proteins by HPLC using a TSK-DEAE column demonstrated that both proteins exhibit insulin degrading activity. These data indicate that GIT may occur in multiple forms in some tissues.
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PMID:Production of a monoclonal antibody directed against rat liver glutathione-insulin transhydrogenase. 651 17

A method is described for the isolation of subclasses of human IgG. Two myeloma proteins, after isolation by DEAE-Sephadex chromatography, were further purified on subclass-specific anti-IgG1 and 2 Sepharose 4B columns. Contaminating IgG1 and 2 were removed from the isolated myeloma proteins.
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PMID:Isolation of subclasses of human IgG with affinity chromatography. 743 Jun 63

Three hybridoma cell lines producing monoclonal antibodies (McAbs) against porcine serum E receptor (PSER) were established by fusing mouse myeloma SP2/o cells with spleen cells of BALB/c mouse immunized with PSER. The ascites McAbs were purified by ammonium sulfate precipitation and DEAE-cellulose chromatography. The McAbs were found to belong to the IgG1 and IgG2b subclasses, respectively. These McAbs inhibited reverse E-rosette formation and enhanced or depressed lymphocyte proliferation induced by PHA or ConA. The specificity of these McAbs was proved by immuno-dot blot and Western blot assay. The potential application of these McAbs in the study of structure and biological function of the E-receptor is discussed.
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PMID:[Study on monoclonal antibodies against porcine serum E receptor]. 790 18

Culture supernatants of lipopolysaccharide-stimulated P388D1 macrophage-like tumor cells showed a growth inhibitory effect on plasmacytoma MOPC-315, MPC-11 and myeloma FO cells, but had no effect on J558 plasmacytoma cells. Based on the results of trypan blue staining and a 51Cr release assay, the supernatant had both cytotoxic and cytostatic activity for MOPC-315 plasmacytoma cells. The inhibitory activity was trypsin-sensitive, heat-stable at 100 degrees C for 20 min., but sensitive to 2-mercaptoethanol and cystein HCl. At least 6 hrs of exposure period were required for the P388D1 culture supernatant to show an inhibitory effect on plasmacytoma cells. Since the inhibitory activity could not be blocked by protease inhibitor or neutralized by antibodies to mouse IL-1 beta, IL-6 and TNF-alpha, the inhibitory factor(s) was distinct from the defined cytotoxic factors. After partial purification with DEAE-Sephacel and Sephacryl S-300 chromatography, four major active peaks with the molecular mass of 874-KDa (near the void volume), 112-KDa, 45-KDa and 18-KDa were obtained.
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PMID:Inhibitory effect of lipopolysaccharide-stimulated P388D1 macrophage-like cells on plasmacytoma cells. 835 65

A Monoclonal antibody (MAb II-T) specific for serotypes II and V Group E streptococci (GES) was prepared by fusing myeloma cells with spleen cells of mice immunized with whole cells of a serotype II strain. MAb II-T reacted in an enzyme immunoassay (EIA) with whole cells of both serotypes and reacted in gel diffusion test with autoclaved-saline extraction of serotypes II and V. The extract was purified by DEAE-Sephadex A-25, followed by treatment with proteinase K, and further by chromatography with a Sephadex G-200 column. The purified polysaccharide (PS) antigen contained 98.6% carbohydrate and 1.4% protein, but no detectable phosphorus. In hapten inhibition tests using various sugars, D-mannosamine markedly inhibited the precipitin reaction. These results indicated that the antigenic determinant might have a structure similar to D-mannosamine.
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PMID:Characterization of serotype II polysaccharide antigen of group E streptococci using a monoclonal antibody. 926 65

Spleen cells from BALB/c mice immunized with human breast cancer serum antigen were fused with murine myeloma SP 2/0 cells. After screening with ELISA and limited-dilution cloning, one hybridoma which could stably secrete specific antibody was obtained and designated McAbGB2. The titer of McAbGB2 was up to 1.2 x 10(6) after purified by ammonium sulfate and DEAE-cellulose. The McAbGB2 was defined as murine IgG1 by agarose double immunodiffusiong. Immunoblotting analysis revealed that the antigens with molecular weights of 116 kd and 45 kd recognized by McAbGB2 were distributed in human breast cancer tissue and serum.
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PMID:[Preparation and identification of monoclonal antibody GB2 directed against human breast cancer serum antigen]. 938 24

This paper describes an attempt to find a difference between the patterns of methylation of E. coli tRNA by extracts of two mouse tissues. Two samples of tRNAs, methylated in two separate experiments with extracts of myeloma and of liver in presence of either 14C or 3H S-Adenosyl-L-Methionine, were pooled and fractionated together on a RPC column. The results show a difference in the specificities of the two extracts. Chromatography on DEAE Sephadex suggests that the tRNA Met is methylated by the enzymes on the myeloma, while enzymes from liver react very little, if at all, with that particular tRNA species. Studies have been undertaken in order to find out whether similar differences can also be demonstrated in homologous systems.
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PMID:??? 1194 21


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