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)

A novel cell surface marker of fetal development was identified in both in vivo and in vitro systems of the mouse using monoclonal antibodies against a glycoprotein of an apparent size of 133,000 Da. Two independent clones of hybridomas were isolated by fusing murine myeloma cells, NS-1, with spleen cells of a rat which was immunized with murine 3T3 fibroblast. The analysis of molecular size and tryptic peptides of the immunoprecipitate indicated that fibroblast and putative parietal endoderm cells, which were derived by induced differentiation of F9 embryonal carcinoma cells with retinoic acid and cyclic AMP, expressed apparently the same protein. Undifferentiated F9 cells and F9 cells which were treated with retinoic acid or cyclic AMP alone had little or no immunoprecipitable proteins. Analogously, parietal endoderm of in vivo embryos tested positive for this protein but visceral endoderm and embryonic ectoderm did not. The amount of this surface protein was increased in fibroblast and differentiated F9 cells by elevation of intracellular cyclic AMP concentrations. These results are consonant with a hypothesis that this surface protein plays a role in fetal development via a quantitative modulation by cyclic AMP.
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PMID:Fetomodulin: marker surface protein of fetal development which is modulatable by cyclic AMP. 303 32

A monoclonal antibody (MAb), BLT-1, with specificity for bovine mature T cells was prepared by somatic cell hybridization of myeloma NS-1 and spleen cells from BALB/c mice hyperimmunized with bovine T lymphocytes. The MAb reacted with over 92% of nylon wool-nonadherent lymphocytes (T cells) but not with nylon wool-adherent EAC-positive lymphocytes (B cells) in the indirect immunofluorescence assay. It is an IgM, with kappa-light chains, which fixed complement well and killed over 95% of mature T cells in complement-mediated cytotoxicity assays. It reacted with the same proportions of peripheral lymphoid cells (peripheral blood, lymph nodes, and spleen) as the polyclonal goat anti-bovine thymocyte serum (GABTS), but only with 25% of GABTS-positive thymocytes. Immunoperoxidase staining of frozen tissue sections showed that the BLT-1-positive cells were located in the medulla of the thymus and in the T lymphocyte areas of lymph nodes. Western immunoblotting assays showed that the BLT-1-reactive membrane antigen is a 22,000 m.w. protein which was inducible in bovine thymocytes with bovine thymic hormones, thymosin fraction 5, thymosin alpha 1, and thymopentin ORF-18150, indicating that it is a mature T lymphocyte differentiation antigen. The thymosin alpha 1 and thymopentin were found to show additive effects on mature T cell antigen expression by bovine thymocytes.
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PMID:Production and characterization of a bovine T cell-specific monoclonal antibody identifying a mature differentiation antigen. 307 88

Production of human monoclonal antibodies reactive to stomach cancer was attempted by the hybridoma technique using splenic lymphocytes from stomach cancer patients. The parental cells used were NS-1 mouse myeloma line and three human lines including RPMI-1788 6TGR, which was established in our laboratories. Ten mouse-human and two human-human (from the fusion with RPMI-1788 6TGR) hybridomas have been producing IgM antibody for over 18 months, and all the heterohybridomas yielded ascites when transplanted into nude mice. Four antibodies produced by the heterohybridomas were selected and analyzed. These 4 antibodies, 3F6, 4A10, 3H5 and 1F9, reacted predominantly to cytoplasmic antigens of stomach and other epithelial cancer lines. The reactivity against human tumors transplantable in nude mice showed that all antibodies but 3F6 were reactive with stomach and lung cancers. Smears prepared from normal and cancer tissues were also tested, and these 4 antibodies showed positive reactions not only to stomach cancer, but also to normal stomach and colon. The reactivity against fetal tissues demonstrated that 3H5 antibody was reactive with epithelium of the stomach, and 1F9 antibody was positive with epithelium of the respiratory tract and bile duct, but the other two were negative. Thus, the serological analysis showed that the antigens detected are not tumor-specific, but are differentiation antigens. Chromosome analysis of these 4 mouse-human hybridomas and another one, which seems to produce an antibody against keratin, showed that three retained human chromosome 14 on which immunoglobulin heavy chain (Ig H) gene is located, but two did not. Southern blot analysis, however, revealed that all 5 hybridomas had a human Ig H gene.
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PMID:Human monoclonal antibody reactive to stomach cancer produced by mouse-human hybridoma technique. 309 22

Hybridomas that produce monoclonal antibodies to bovine hydroxyindole O-methyltransferase have been established by immunizing a mouse with hydroxyindole O-methyltransferase partially purified from bovine pineal glands followed by fusion of the spleen cells with myeloma NS-1 cells. Twenty-three clones have been isolated by screening the medium by two different methods. These clones produced various antibodies with different binding properties. Most of the antibodies belonged to IgG1 subtype, while 7 clones produced IgG2 alpha or IgG2 beta antibodies. Three antibodies inhibited enzymatic activity, whereas others did not. Antibodies of 7 clones recognized enzyme protein denatured with sodium dodecyl sulfate, while other antibodies reacted only with native enzyme protein. Thus a variety of monoclonal antibodies will offer us a good tool for immunohistochemical localization of the enzyme, immunoaffinity purification of hydroxyindole O-methyltransferase, and isolation of the cDNA clones encoding it. We also report here on the immunohistochemical demonstration of hydroxyindole O-methyltransferase in bovine pineal gland and a new immunoaffinity procedure to purify the enzyme to homogeneity by use of monoclonal antibodies.
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PMID:Monoclonal antibodies to hydroxyindole O-methyltransferase from bovine pineal gland. 311 61

A monoclonal IgE antibody was prepared by fusion of NS-1 myeloma cells with spleen cells of C3H/He mice immunized with an extract of adult worms of Schistosoma japonicum (Sj). The antibody was able to elicit passive cutaneous anaphylaxis in the rat skin against Sj with the highest titer of 1/256,000 in an ascitic form but did not cross-react with any of antigens extracted from S. mansoni, Fasciola hepatica, Paragoniumus westermani, or Trichinella spiralis. Western blot analysis indicated that the monoclonal IgE antibody recognized epitopes on molecules of 82 kDa, 97 kDa, 160 kDa, and 200 kDa, at least some of which were recognized by IgG antibodies of patients with chronic schistosomiasis japonica. The IgE antibody also recognized a 97-kDa antigen expressed on the surface of mechanically transformed schistosomula. Passive transfer of the antibody into mice in an early stage of challenge infection resulted in a partial but significant reduction of recovery of adult worms. However, similar treatment was not effective for the protection if the antibody was given in the postlung stage of the infection. Moreover, eosinophil-mediated damage to schistosomula was observed in vitro in the presence of the monoclonal anti-Sj IgE antibody, whereas the damage was not observed in the presence of another monoclonal IgE antibody with dinitrophenyl specificity.
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PMID:Production and properties of a mouse monoclonal IgE antibody to Schistosoma japonicum. 311 84

Human tyrosinase was partially purified from the lysate of a melanoma cell line and used to immunize BALB/c mice. Spleen cells from the immunized mice were fused with a murine myeloma cell line (NS-1), yielding a hybridoma (5C12) that produced monoclonal antibody directed against tyrosinase. 5C12 antibody reacted with normal human melanocytes, neval cells, primary cultures of melanoma biopsies, and most melanoma cell lines, including amelanotic lines with very low levels of enzyme activity. No reaction was found with keratinocytes, lymphoid cells, fibroblasts, and nonmelanoma cell lines. The 5C12 antibody was used to affinity-purify tyrosinase directly from a cell lysate, giving a single protein of 60,000 daltons, electrophoretically identical with enzyme activity and immunoreactivity with 5C12 antibody. Treatment of melanoma cells with periodate significantly reduced antigenicity. It can be inferred from these results that 5C12 antibody is directed against a carbohydrate moiety present in active and inactive tyrosinase, and that amelanotic melanoma cells may contain significant levels of the latter protein.
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PMID:Monoclonal antibody against human tyrosinase and reactive with melanotic and amelanotic melanoma cells. 312 79

Monoclonal antibodies to human fibrin have been prepared from stable hybridomas, obtained by fusion of a mouse myeloma cell line (NS-1) and spleen cells of Balb/c mice immunized with a suspension of human fibrin. One cell line, DG1, producing a monoclonal antibody of the IgG1, kappa subclass, reacted specifically with human fibrin (KD = 1.2 nM). Western blotting analysis indicates that DG1 crossreacts with the fibrin fragment D-dimer. Using both a chromogenic and an 125I-fibrin release assay it was illustrated that in the presence of the fibrin specific antibody the t-PA mediated generation of plasmin was significantly inhibited. An animal model system, developed to monitor thrombosis and induced reactive fibrinolysis, was used to investigate the interference of plasminogen activation, by the antibody, in vivo. This fibrin specific antibody prolonged the onset of reactive fibrinolysis in a dose dependent manner.
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PMID:A fibrin specific monoclonal antibody which interferes with the fibrinolytic effect of tissue plasminogen activator. 314 80

Monoclonal antibodies against tetanus toxin were generated by fusion of mouse NS-1 myeloma cells with spleen cells from BALB/C mice immunized with tetanus toxoid. Twenty seven hybridomas against tetanus toxin were obtained. Six hybridoma clones, designated as 1A6B12, 1H7D9, 3A8G9, 3A9F2, 3F9H9, 4A6D11 were selected for further studies. All of them were IgG1, k chain and bound specifically to tetanus toxin and toxoid. All six clones were injected intraperitoneally into pristane-primed BALB/C mice. Antibodies with titer up to 10(6) were obtained in the ascites. Results obtained from in vivo neutralization test showed that 1A6B12, 3A8G9, 3F9H9, 4A6D11 mAbs did have neutralizing activities against tetanus toxin. Monoclonal antibody 4A6D11 had the strongest neutralizing activity. 4A6D11 were purified from ascites by DEAE-52 ion exchange chromatography. Comparing to U.S.A. standard antitetanus toxin antiserum, 50 micrograms purified 4A6D11 mAb had 1 international unit neutralizing activity. The purified 4A6D11 mAb was also coupled to cyanogen bromide-activated sepharose to make an affinity column. Pure tetanus toxin can be obtained by passing crude tetanus toxin through this column and eluting the adsorbed toxin with 4M urea. Large scale purified tetanus toxin could be obtained by this method.
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PMID:Protective murine monoclonal antibodies to tetanus toxin. 315 81

The proximate cholesterol precursors lathosterol, 7-dehydrocholesterol and desmosterol supported the growth of NS-1 and X63 mouse myeloma cells. These cells and X63.653 cells are cholesterol auxotrophs, yet each was able to convert [3H]lathosterol to [3H]cholesterol. These results are consistent with the conclusion that cholesterol auxotrophy in these myeloma cells is due to a deficiency in 3-ketosteroid reductase activity. The steroid hormones testosterone, progesterone and hydrocortisone could not replace cholesterol as a medium supplement. These results provide a greater understanding of the cholesterol auxotrophy characteristic of cell lines clonally-derived from the MOPC 21 myeloma tumor, and they provide a rational basis for the use of sterols in defined culture medium for mouse myeloma cells.
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PMID:Effects of proximate cholesterol precursors and steroid hormones on mouse myeloma growth in serum-free medium. 320 88

A monoclonal antibody cross-reactive with most group A trichothecenes was produced by fusion of P3/NS-1/1-AG4-1 myeloma cells with spleen cells isolated from a BALB/c mouse that had been immunized with 3-acetyl-neosolaniol-hemisuccinate conjugated to bovine serum albumin. One stable clone, H159B1D5, which produced monoclonal antibody that bound with both T-2 toxin and diacetoxyscirpenol (DAS) was obtained after subcloning. Enzyme-linked immunosorbent assay (ELISA) revealed that the antibody belongs to the immunoglobulin G1 (kappa chain) isotype and had binding constants of 2.81 x 10(9), 1.05 x 10(9), and 1.57 x 10(8) liters per mole for T-2 tetraol tetraacetate, T-2 toxin, and DAS, respectively. The relative cross-reactivities of the antibody with T-2 tetraol tetraacetate, T-2 toxin, and DAS were 200, 100, and 20, respectively, with tritiated T-2 toxin as the marker ligand. The relative cross-reactivities for the above toxins were 667, 100, and 73, respectively, with tritiated DAS as the marker ligand. No cross-reaction with HT-2 and deoxynivalenol triacetate was observed in either system. By using this monoclonal antibody, an indirect ELISA for analysis of T-2 toxin was also developed. The linear portion of the standard curve for analysis of T-2 toxin in each analysis by radioimmunoassay and ELISA was in the range of 0.1 to 2 ng and 0.05 to 1.0 ng, respectively.
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PMID:Production and characterization of a monoclonal antibody cross-reactive with most group A trichothecenes. 322 62


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