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)

We have identified a region of the beta-globin gene that is attached constitutively to histone-depleted murine erythroleukemia cell nuclei. This region spans 800 bp and is located at -300 to -1100 bp upstream from the site of transcriptional initiation. Attachment is not altered by transcriptional activation of the beta-globin gene during induction to terminal differentiation, and the same region of the beta-globin gene is attached to histone-depleted myeloma cell nuclei (NS-1). The attached region contains an A/T-rich section, in addition to a sequence closely related to the Drosophila topoisomerase II consensus cleavage sequence. No comparable site of attachment of the alpha 1-globin gene was detected when a region spanning 1.5 kb 5' to 0.5 kb 3' of the region of transcription was studied.
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PMID:Constitutive attachment of murine erythroleukemia cell histone-depleted DNA loops to nuclear scaffolding is found in the beta-major but not the alpha 1-globin gene. 322 84

Human embryonal carcinoma cells sometimes display the developmental potential of early embryonic stem cells. While available data do not clearly identify a counterpart of these tumor cells in normal development, previous comparisons of human embryonal carcinoma and yolk sac carcinomas indicated that these cell types are closely related, and suggested that embryonal carcinoma cells might resemble the progenitors of extraembryonic endoderm. To analyse further cell-differentiation lineage in these tumors, we produced monoclonal antibodies to cytostructurally associated antigens of human embryonal carcinoma cells. Spleen cells from mice immunized with a detergent-insoluble extract of cultured human embryonal carcinoma cells were fused to NS-1 myeloma cells, and hybridoma supernatants were screened by indirect immunofluorescence on the immunizing cell line, then on a panel of cell lines derived from human embryonal carcinomas, yolk sac carcinomas, and a range of neoplastic and normal tissues. Monoclonal antibody GCTM-1 stained the nuclei of all human cells tested and served as a positive control; this antibody immunoprecipitated proteins of 85 and 66 k Da from human embryonal carcinoma cells. GCTM-2 recognized an epitope on a 200-k Da extracellular protein present on the surface of embryonal carcinoma cells, and stained the surface of visceral yolk sac-type carcinoma and colorectal carcinoma cells as well. Enzymatic analysis of carbohydrate residues on the GCTM-2 antigen revealed that it was a keratan sulphate proteoglycan, and suggested that the epitope recognized by the antibody lies on the core protein. In immunoblots, antibody GCTM-3 bound to a 57-k Da cytoskeletal protein expressed in human embryonal carcinoma. This antibody decorated filamentous arrays in cell lines from human embryonal carcinoma, visceral yolk sac carcinoma, parietal yolk sac carcinoma (endodermal sinus tumour), and adenocarcinoma and large cell carcinoma of the lung. Antibody GCTM-4 recognized a determinant present on a 69-k Da polypeptide, associated with a component of the lysosomal compartment, which was expressed in embryonal carcinoma cells, but no other cell type tested. The results with this antibody panel thus allow distinction between human embryonal carcinoma and yolk sac carcinoma, but provide further evidence of a close relationship between these cell types.
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PMID:Analysis of cell-differentiation lineage in human teratomas using new monoclonal antibodies to cytostructural antigens of embryonal carcinoma cells. 324 84

Production of monoclonal antibodies against human chorionic gonadotropin (hCG) has been studied using hCG as an immunogen. Spleen cells of BALB/c mice immunized with hCG were fused with NS-1 mouse myeloma cells. This study reports the successful isolation of a hybrid clone secreting a monoclonal antibody specific for hCG. By using PEG 4,000 as a fusion agent, the fusion rates were between 42.0 and 50.2%. In total 842 hybridomas were produced. Among them, 403 hybridomas had hCG antibody production. After cloning twice by limiting dilution and alternately screening by enzyme immunoassay and by radioimmunoassay, there were 39 cell lines having specific antibody production. Among them, the No. 57-42-2 had the highest reactivity. By Ouchterlony test, the monoclonal antibody was shown to be IgG1. The affinity constant of the antibody to hCG was 0.6 x 10(9) 1/mole. In radioimmunoassay, the cross reactivity of the antibody to human luteinizing hormone (LH) and human follicle-stimulating hormone (FSH) was 1.5% and 0.7%, respectively. There was no cross reaction with human thyrotropin-stimulating hormone (TSH).
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PMID:Production of monoclonal antibodies to human chorionic gonadotropin. 324 19

A human immunoglobulin M (IgM) antibody secreting hybridoma, HMG1, has been established and studied for its reactivity against human gastric cancer cells. Lymphocytes isolated from a regional lymph node of patient with gastric adenocarcinoma were fused with mouse myeloma cells NS-1. Supernatants from the generated human-mouse hybrids were first screened for immunoglobulin production by ELISA. The identified human IgM-secreting hybridomas were expanded and subcloned for further analysis or cryopreservation. The screening for binding of antibodies to a panel of human cancer cell lines and normal fibroblast was carried out with PAP or indirect immunofluorescence stain. The selected hybridoma, HMG1 after being cloned three times, was stable in secreting IgM (about 4 micrograms/1 x 10(6) cells) for more than 9 months. Large amount of ascites was obtained by injecting this hybrid to BALB/C nude mice pretreated with anti-lymphocyte serum and pristane. The ascitic fluid contained 5-19 mg human Ig/ml. Subsequently this IgM was extracted from ascitic fluid by saturated ammonium sulphate solution. This crude extract was further purified with immuno-affinity chromatography. Both this purified ascite-IgM as well as IgM from HMG1 supernatant would react with gastric cancer cell line BGC-823 but not with human normal fibroblasts 350Q by PAP or immunofluorescence analysis. The human HMG1-IgM reacted with gastric cancer cells on paraffin embedded tissue section but did not react with normal gastric mucosa cells. HMG1-IgM had some complement dependent cytotoxicity against BGC-823. These results suggest that the establishment of anticancer human monoclonal antibodies with human-mouse hybridoma technique be feasible. There is a possibility for clinical applications of this human monoclonal antibody in the future.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Study of anticancer human monoclonal antibody--establishment of human monoclonal antibody to gastric cancer by human-mouse hybridoma]. 324 78

Peripheral blood lymphocytes isolated from an infertile woman possessing strong sperm immobilizing and agglutinating antibodies were stimulated by culturing with poke-weed mitogen (PWM) and spermatozoa from a healthy donor for 5 days. The stimulated lymphocytes were fused with mouse myeloma NS-1 by PEG-1000. Fused growing hybrid cells were observed in 58 of 96 wells, and 22 of these showed the production of human immunoglobulin. Among the 22, one hybridoma clone (H6-3C4) was found to produce human IgM (lambda) with strong sperm immobilizing and agglutinating activities. The supernatant from the culture medium contained approximately 1.5 microgram IgM/ml and the antibody titers were 5000 SI50 units on sperm immobilization and 1:1600 dilutions on sperm agglutination. The hybridoma H6-3C4 has continuously produced high titers of antibody exhibiting sperm immobilizing and agglutinating activities over 8 months and contains chromosomes of acrocentric type from mouse and metacentric type from human. The monoclonal antibody (Mab) H6-3C4 reacted specifically to human seminal plasma, ejaculated spermatozoa and male accessory gland but not to testis, any other somatic tissues, or secreted fluids tested. Immunofluorescence staining indicated that the antigen corresponding to Mab H6-3C4 was present over the surface of ejaculated spermatozoa. The binding of Mab H6-3C4 to human spermatozoa was blocked by the serum of the patient from whom the lymphocytes were obtained for cell fusion.
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PMID:Establishment and characterization of a human hybridoma secreting monoclonal antibody with high titers of sperm immobilizing and agglutinating activities against human seminal plasma. 329 32

Three hybridomas producing monoclonal antibodies to bovine brain choline acetyltransferase (ChAT) have been established by fusion of the spleen cells from a mouse immunized with purified enzyme with myeloma NS-1 cells. All three clones produced IgGl antibodies that reacted with enzyme protein denatured with sodium dodecyl sulfate. By using one of the monoclonal antibodies, a rapid and efficient immunoaffinity purification procedure of bovine ChAT has been established. Immunoblot analysis and immunoaffinity purification indicated that bovine ChAT is a single 68-kilodalton protein. The monoclonal antibodies will offer us a good tool to isolate the cDNA clones encoding ChAT.
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PMID:Monoclonal antibodies to and immunoaffinity purification of choline acetyltransferase from bovine brain. 330 7

Hybridoma antibodies against bovine collagenase inhibitor were produced by fusion of myeloma cells NS-1 (P3-NS1-1) with spleen cells from mice hyperimmunized with collagenase inhibitor purified from the explant medium of bovine dental pulps. Hybridomas positive by an enzyme-linked immunosorbent assay (ELISA) for bovine collagenase inhibitor were cloned by the dilution method. Seventeen hybridomas producing antibodies were isolated, four of which also recognized purified human collagenase inhibitor in the ELISA. Using a monoclonal antibody-Sepharose affinity column, we easily purified both bovine and human collagenase inhibitors to homogeneity. They showed the same mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, corresponding to a molecular mass of 32,000 daltons.
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PMID:Monoclonal antibodies to bovine collagenase inhibitor. 331 76

Nine hybridoma cell lines secreting monoclonal antibodies specific for Nematospiroides dubius were produced by fusion of the mouse myeloma cell line NS-1 to either spleen cells or mesenteric lymph node cells from mice repeatedly infected with N. dubius. Seven of the antibodies were identified as IgM and two as IgG1. Each monoclonal antibody bound to polypeptide epitopes on both infective larvae (L3) and adult worms. However, five antibodies bound preferentially to L3 and three to adult worms. All nine antibodies reacted with high molecular weight protein antigens. Passive protective immunity in Balb/c mice was demonstrated with monoclonal antibodies Nd2 and Nd3 in ascites fluid which stunted both male and female worms and reduced parasite fecundity.
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PMID:Nematospiroides dubius: passive transfer of protective immunity to mice with monoclonal antibodies. 336 16

A 65-kDa estrogen receptor (ER) protein has been demonstrated both by sucrose gradient analysis and by immunoblot, using anti-ER monoclonal antibodies (MAbs). Since the ER is denatured in many experimental situations, such as formaldehyde fixing of samples for histochemistry and electroimmunoblotting studies, in this work we used a denatured 60-70-kDa ER-rich protein preparation as antigen for mice immunization in order to raise anti-ER MAbs. That material was obtained by affinity purification on an allyl-estradiol matrix of the MCF-7 cytosolic ER, followed by further isolation and enrichment by PAGE. NS-1 myeloma cells and spleen lymphocytes from the immunized mice were fused, and resultant hybridoma colonies were screened by [125I]-estradiol-labelled nuclear ER immunoprecipitation. The isolated MAb, E476, shows a moderate ability to precipitate ER and reacts strongly with a 46-kDa antigen in Western blot assay. The 46-kDa antigen was not detectable in native cytosol but became reactive after 50% ammonium sulfate precipitation of cytosolic proteins. The 46-kDa antigen appeared concentrated in the NaSCN plus estradiol eluate of the affinity column used for cytosolic ER purification. Freshly prepared 60-70-kDa material from the preparative gel electrophoresis did not show any E476 reactivity. However, when the 60-70-kDa proteins were frozen, thawed and speed vacuum concentrated, the 46-kDa antigen became detectable. Storage increased the reactivity of the 60-70-kDa material with the E476 MAb. The 46-kDa antigen was present only in the ER positive cell lines, and was absent in all negative cell lines tested. The 46-kDa protein is also present in the ER positive human breast cancer specimens. We conclude that the 46-kDa protein identified with the E476 MAb in human breast cancer is probably a naturally occurring ER fragment.
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PMID:A 46-kDa antigen associated with estrogen receptor in human breast cancer. 338 60

The in vitro effect of the heat-labile toxin (HLT) of Bordetella parapertussis on HeLa, baby hamster kidney (BHK), chinese hamster ovary (CHO), myeloma (Pa-NS-1), human embryonic lung (HEL-R66) cells, erythrocytes, adipocytes and lymphocytes from guinea pigs, mice or rats, or aortic smooth muscle cells from pigs or guinea pigs was examined. Within 8, 6, 4, 2, and 2 hr after the exposure to 1, 3, 10, 30, and 100 MNDs/ml of HLT, respectively, the cultured smooth muscle cells only showed a cytopathic change. When the cells exposed to HLT were washed out within 60 min post-exposure, the change could be induced with an extend period of lag. Histamine, KCl or norepinephrine caused similar change in the cells, but the period of lag was within 30 min. The HLT activity was neutralized by an anti-B. parapertussis- or B. bronchiseptica-HLT guinea pig IgG. HLT had no effects on any other cells tested.
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PMID:Cytopathic effect of heat-labile toxin of Bordetella parapertussis on aortic smooth muscle cells from pigs or guinea pigs. 339


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