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)

Anionic amphiphiles such as long chain unsaturated fatty acids and SDS were shown to activate the superoxide (O2-) producing NADPH oxidase in a cell-free system derived from sonically disrupted phagocytes (macrophages and granulocytes). O2- production required the cooperation of a membrane associated component sedimenting at 48,000 X g (pi) and a cytosolic factor (sigma). The purpose of the present investigation was to find out whether components pi and sigma were also present in non-phagocytic cells that do not produce O2- when stimulated. It was found that the 48,000 X g pellets of guinea pig lymph node and thymus cell sonicates contained significant amounts of component pi, as shown by their ability to support SDS-elicited NADPH-dependent O2- production when supplemented with macrophage cytosol. Lymph node and thymus pi could be extracted from the membrane by 30 mM octyl glucoside, just as its macrophage-derived equivalent. Combining lymph node and thymus 48,000 X g pellet with autologous cytosol did not yield an active enzyme preparation. Also, cytosol from lymph node and thymus cells could not cooperate with macrophage 48,000 X g pellet, indicating that component sigma was lacking in lymphoid cells. Neither pi nor sigma could be detected in guinea pig kidney, the mouse myeloma cell line MOPC 315 and the canine cell line Cf2Th. The 48,000 X g pellet of all nonphagocytic cells examined contained a b-cytochrome that resembled, by its spectral characteristics, the cytochrome b559 thought to be characteristic of phagocytes. In macrophages, cytochrome b559 represented 80% of b-cytochrome content of the 48,000 X g pellet, whereas in non-phagocytic cells, the equivalent material represented only 50 to 60%. There was no correlation between the presence and quantity of the cytochrome b559-like chromophore in the 48,000 X g pellet of a particular cell type and its ability to cooperate with macrophage cytosol in SDS-elicited O2- production.
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PMID:Certain lymphoid cells contain the membrane-associated component of the phagocyte-specific NADPH oxidase. 283 Dec 70

A T helper clone (clone 9), isolated from a H-2d anti-H-2b mixed lymphocyte culture, was previously found to produce an antigen-specific helper factor (ASHF) that could be specifically absorbed out with BIO.A(2R) (KkAkEkDb), but not B10.A (KkAkEkDd), spleen cells. In order to characterize this ASHF further, we have constructed T-cell hybridoma lines by fusing clone 9 cells with the AKR thymoma, BW5147. One of these hybridoma clones, referred to as clone 25, produced an ASHF that was specific for the Db alloantigen. Immunization of allogeneic C57BL/6 mice with clone 9 cells and subsequent fusion of these immune spleen cells with non-secreting myeloma cells led to the isolation of a monoclonal antibody (mAb) (clone 30 IgM) that was capable of neutralizing the helper activity of clone 25 ASHF. Clone 30 IgM affinity column was found to retain clone 25 ASHF; clone 30 IgM column eluates augmented the cytotoxic responses of CBA/J thymocytes to B6(H-2b), but not D2(H-2d), alloantigens. Preabsorption of clone 25 ASHF with Db-bearing spleen cells prior to affinity purification over a clone 30 IgM column resulted in the abrogation of Db-specific helper activity as well as the loss of a 50,000 molecular weight (MW) band in SDS-polyacrylamide gels run under reducing conditions. Clone 25 ASHF was also retained by immunoadsorbents made with an IgG2a mAb (F23.1) the reactivity of which is against the beta chain of the T-cell receptor. Furthermore, affinity purification of clone 25 ASHF over a F23.1 affinity column, but not an irrelevant mAb column, also yielded a 50,000 MW molecule. These findings suggest that this particular ASHF may be intimately related to the T-cell antigen receptor.
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PMID:Characterization of a Db-specific helper factor required for the induction of cytotoxic responses to alloantigens with the use of monoclonal antibodies specific for the helper factor or the T-cell antigen receptor. 295 97

Monoclonal antibody against 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) was generated by fusing mouse myeloma cells with spleen cells from BALB/c mice immunized with delipidated white matter from rat corpus callosum. The antibody was characterized by solid-phase radioimmunoassay, immunoblot of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), immunoprecipitation from C6 glioma cells, and indirect immunofluorescence staining of monolayer cultures containing oligodendrocytes. The monoclonal antibody bound specifically to an intracellular antigen of oligodendrocytes, but not to Schwann cells, astrocytes, neurons, or fibroblast cytoplasm. The immunoblot of SDS-PAGE of CNS myelin showed that the antibody identified two protein bands at 48,000 and 50,000 molecular weight. These proteins were not identified in peripheral nervous system myelin. The monoclonal antibody immunoprecipitated CNP enzyme activity from extracts of C6 glioma cells. This monoclonal antibody should prove useful in further study of this myelin-specific enzyme in CNS myelin and in cells responsible for myelin production.
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PMID:A monoclonal antibody raised to corpus callosum extract reacts with 2',3'-cyclic nucleotide 3'-phosphohydrolase. 299 39

Monoclonal antibodies against SDS-disrupted bovine papillomavirus type 1 (BPV1) were obtained from hybridomas prepared by fusing mouse myeloma cell line P3X63Ag8U1 with spleen cells from immunized BALB/c mice. Six hybridoma cell lines were obtained after testing supernatant fluids for positivity by the enzyme-linked immunosorbent assay using the immunogen as antigen and by indirect immunofluorescence (IF) on frozen sections of BPV1-induced bovine fibropapillomas. Monoclonal antibodies (AU1-AU6) from these hybridomas were then tested for reactivity by IF tests on BPV2-induced fibropapillomas and on human plantar warts and vulvar condylomas and by avidin-biotin complex tests on sections of formalin-fixed cervical dysplasias. One monoclonal antibody (AU1) was reactive with all tissues, four (AU3-AU6) were reactive with both BPV1 and BPV2 fibropapillomas, and the remaining antibody (AU2) was only reactive with BPV1-induced fibropapillomas. All monoclonal antibodies reacted with the major capsid protein (mol. wt. 54,000) of BPV1, whereas five (AU1, AU3-AU6) reacted with the major capsid protein of BPV2. These results indicate that papillomavirus genus-specific, cross-reactive, and type-specific antigenic determinants are located on the major capsid protein of BPV1.
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PMID:Monoclonal antibodies to genus- and type-specific papillomavirus structural antigens. 300 51

The presence of aberrant lambda 1 light (L) chain fragment (lambda 1 F) on the secreted myeloma protein of MOPC-315 has been demonstrated by serological and immunochemical methods. We developed a highly sensitive radioimmunoassay that utilizes exquisitely specific xenogeneic anti-lambda 1 antibodies to detect the minute amounts of lambda 1 F on lambda 2-bearing MOPC-315 myeloma proteins. In addition, structural evidence that lambda 1 F is present on MOPC-315 myeloma protein was demonstrated by subjecting 125I-labeled MOPC-315 myeloma protein to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions followed by autoradiography. The relative amounts of lambda 1 F and lambda 2-chain on MOPC-315 myeloma were measured by two independent methods. The molar ratio of lambda 1 F to lambda 2 was calculated to be 1:68 by radioimmunoassay and 1:80 by analytical SDS-PAGE. This represents the first demonstration that an aberrant L-chain fragment combines with a heavy chain and is secreted in association with antigen-binding myeloma proteins. The implications of these results on L-chain isotype exclusion are discussed.
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PMID:Lack of isotype exclusion and expression of aberrant lambda light chain on secreted MOPC-315 myeloma proteins. 308 41

Eight human IgA1 myeloma proteins were analysed by SDS-PAGE. These experiments showed that purified IgA1 proteins comprise both fully S-S bonded and partly S-S bonded molecules. Pepsin digestion of the IgA1 proteins yielded three four-chain and two two-chain fragments. The four-chain fragments are likely to be derived from intact IgA through cleavage of its alpha chains at different sites: between the CH2 and CH3 domains or in the hinge region. The occurrence of F(abc) (ab') fragments, with alpha chains of different lengths, showed that the alpha chains of IgA can be cleaved independently at the hinge region site. The two-chain pepsin fragments must originate from IgA molecules, which lack inter-assay-chain disulphide linkages. The fragments F(abc)2 and Fabc tended to form dimers, probably through non-covalent interactions of their CH2 domains. An immunoblotting method was used to identify Fd-, CH2- and CH3-specific anti-IgA antibodies. The CH2-specific antibodies could be subdivided into antibodies recognizing an isotype present on both four-chain and two-chain molecules or on two-chain molecules only.
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PMID:Production and characterization of pepsin fragments of human IgA1 to determine domain-specificity of monoclonal anti-IgA antibodies. 309 70

The secretion of immunoglobulin (Ig) from cultured mononuclear cells by lipopolysaccharide (LPS) stimulation is inhibited by monoclonal nonspecific suppressor factor (MNSF), a lymphokine produced by murine T cell hybridoma. In an attempt to develop a murine monoclonal antibody (MAb) with specific reactivity against MNSF, a cell fusion technique that incorporated immune murine splenocytes and HAT-sensitive murine myeloma cells was used. Cross-reactivity experiments confirmed that the MAb (MO6) does not bind to unrelated proteins such as bovine serum albumin, mouse IgG, and murine interferon-gamma (IFN-gamma). There are no effects when anti-IFN-gamma antibodies are used with MNSF. As far as biological activity is concerned, MO6 inhibits in vitro the activity of MNSF in terms of the Ig secretion from cultured lymphocytes. By using MO6, affinity chromatography and immunoblotting were performed. The MNSF on the SDS-PAGE showed a band with m.w. of approximately 70,000, indicating the formation of an aggregate in saline; but after treatment with 0.4 M pyridine-acetic acid buffer, separate bands of 24,000 and 16,000 daltons were evident. Therefore MO6 recognizes 70,000 and both 24,000 and 16,000 daltons. Thus we confirmed by using this MAb and affinity chromatography, the existence of human counterpart, human nonspecific suppressor factor (hNSF), in supernatant from concanavalin A-stimulated T cells. When hNSF was fractionated by high pressure liquid chromatography (HPLC), the activity was found in a region corresponding to 70,000 daltons. However, when fractionated in pyridine-acetic acid buffer, hNSF activity was distributed in a slightly wider range of 15,000 to 30,000 daltons. Physicochemical analysis showed that the purified hNSF is resistant to either heating at 56 degrees C or to 2-mercaptoethanol treatment; however, it is labile to acidification at pH 2.0 and is also sensitive to protease treatment, the characteristics of which were similar to those of murine MNSF. Thus MO6 was confirmed to be a pertinent tool for isolation of hNSF, as well as for murine MNSF.
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PMID:Characterization of monoclonal nonspecific suppressor factor (MNSF) with the use of a monoclonal antibody. 310

Stepwise increments of the concentration of 2-difluoromethylornithine (DFMO), a mechanism-based irreversible inhibitor of mammalian ornithine decarboxylase (ODC), resulted in a selection of cultured human IgG-myeloma cells (Sultan cell line) capable of growing in the presence of up to 3 mM-DFMO. This capacity was associated with 10-fold increase in ODC activity in the dialysed extracts of drug-resistant myeloma cells, markedly enhanced synthesis rate for ODC enzyme molecules, as revealed by a 20 min [35S]methionine labelling of cellular proteins, followed by specific immunoprecipitation and SDS/polyacrylamide-gel electrophoresis, dose-dependently increased expression of ODC mRNA in resistant cells (effective dose causing 50% inhibition), dose-dependent amplification of ODC gene sequences in a 9-kilobase-pairs EcoRI genomic DNA fragment, and (v) a 10-fold increase in the ED50 (effective dose causing 50% inhibition) for the anti-proliferative action of DFMO in these myeloma cells. These results represent one of the few gene amplifications described in cultured human cells.
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PMID:Human myeloma cells acquire resistance to difluoromethylornithine by amplification of ornithine decarboxylase gene. 310 82

Monoclonal antibodies to chicken riboflavin carrier protein have been produced by fusing immunized mouse spleen cells with myeloma SP2/O-Ag 14. The three different monoclonal antibodies specifically bound 125I-labelled chicken riboflavin carrier protein and were characterized with respect to their affinities to bind the antigen, subclass and isotype. These three monoclonal antibodies had similar affinities for holo-, apo- and SDS-denatured riboflavin carrier protein but were unable to recognize the reduced and carboxymethylated protein indicating that they were directed to specific conformational epitopes on the native avian protein. Succinylation of the vitamin carrier protein while still retaining flavin binding characteristics totally abolished the cross-reactivity with all the three monoclonal antibodies indicating that lysine residues were involved at the antigenic sites of the protein. This shows that the antigenic loci may be distinct from the flavin binding sites in the protein. All three antibodies were able to recognize riboflavin carrier protein present in the sera of pregnant rats, monkeys and humans indicating that the epitopes to which they are directed are conserved throughout evolution. These antibodies can therefore be effectively used for radioimmunoassays and further studies on the functional aspects of this protein in higher mammals.
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PMID:Immunological characterization of riboflavin carrier proteins using monoclonal antibodies. 311 15

Rabbit IgA-heavy chain cDNA and germline genes were cloned into prokaryotic and eukaryotic expression vectors, respectively. The Fc alpha encoding portion of six C alpha cDNA clones were cloned into pUC8 and E. coli were transformed. Radioimmunoassay of the molecules synthesized by these clones showed that molecules with Fc alpha antigenic determinants were produced at the level of approximately 0.1 to 1.0 microgram per ml culture. Radiobinding analysis showed that each of the clones encoded heavy chains of the IgA-g subclass. Southern blot analysis of rabbit germline DNA revealed 10 germline C alpha genes. Five of these, isolated from recombinant cosmid libraries, were cloned into a eukaryotic expression vector containing a rearranged murine VDJ gene, the CH enhancer region and the Eco-gpt gene. Murine myeloma cells, J558L, were transfected with each of the heavy chain constructs and stable transfectants was selected with mycophenolic acid. The immunoglobulins produced by each transfectant were analyzed by radiobinding and by SDS-PAGE. Each transfectant were shown to synthesize IgA molecules and thus all five C alpha genes are expressible. The heavy chains from the transfectants ranged in size from 55,000 to 60,000 daltons. Radiobinding analyses indicated that four of the five genes encode molecules of the IgA-f subclass; the serological identity of the fifth gene is not yet established.
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PMID:Expression of rabbit IgA heavy chain genes in E. coli and in murine myeloma cells. 312 39


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