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)

Spleen cells from a CBF1 (BALB/c X C57BL/6) mouse immunized with rat tyrosine 3-monooxygenase were fused with NS-1 mouse myeloma cells. From 188 hybrid cells, 2 stable clones secreting anti-tyrosine 3-monooxygenase antibody were obtained. Antibody from one clone was coupled to CNBr-activated Sepharose 4B and the monoclonal antibody-Sepharose was shown to be very useful for isolating rat tyrosine 3-monooxygenase from crude preparations. Analyses by monoclonal antibody chromatography followed by SDS-polyacrylamide gel electrophoresis and by gel filtration revealed that tyrosine 3-monooxygenases from nerve cell bodies, nerve terminals, and adrenal medullae were indistinguishable with respect to their molecular structures. However, there were serious differences in the catalytic properties between the enzymes from the brain tissues and adrenal medullae, although there appeared to be no significant difference between the enzymes from nerve cell bodies and nerve terminals. The possibility that the activity of the enzyme may be strongly suppressed especially at the physiological pH in brain tissues is also discussed.
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PMID:A comparative study of tyrosine 3-monooxygenase from rat adrenal and brainstem. 258 40

After somatic cell fusion between splenocytes of immunized BALB/c mice and NS-1 myeloma cells, a clone was obtained that secreted an anti-nortriptyline antibody of the IgG1 kappa isotype. The association constant of this antibody for pharmacologically active tricyclic antidepressant drugs ranged from 0.6 X 10(7) to 3 X 10(7) M-1. From thermodynamic and binding studies as well as tridimensional structures of tested compounds, the epitope recognized by the monoclonal antibody appeared to include both a hydrophobic tricycle in which the two phenyl rings form an angle of 120 to 130 degrees, and a side chain in which the amino group is separated from the two lateral rings of the tricyclic structure by a distance of approximately 5.9 A and 7.5 A, respectively. This conformation seems to be the one interacting with muscarinic acetylcholine brain receptors.
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PMID:Structural analysis of the epitope recognized by a monoclonal antibody directed against tricyclic antidepressants. 258 44

The effect of phorbol esters and mezerein pretreatment on macrophage (M phi) activation for tumor cytolysis, tumor necrosis factor (TNF) secretion, and TNF-alpha mRNA expression was investigated. Following pretreatment with various concentrations (0.01 to 10 micrograms/ml) of phorbol 12-myristate 13-acetate (PMA), phorbol-12,13-dibutyrate (PDBu), or mezerein for 16 h, murine peritoneal M phi were activated with M phi-activating factor (MAF) or calcium ionophore A23187 and tested for cytotoxicity in a 24-h cytolysis assay against 125-I-UdR-labeled P815 mastocytoma and NS-1 myeloma target cells. It was found that pretreatment with all three protein kinase C (PKc) activators inhibited M phi activation for cytotoxicity against P815 cells in a dose-dependent manner. Fifty percent inhibition was achieved at concentrations less than 0.1 micrograms/ml. The inhibition was partially reversible. In contrast, the pretreatment did not at all inhibit but significantly enhanced M phi activation for cytolysis against NS-1 cells. Furthermore, exposure to PMA augmented M phi activation by MAF and A23187 for TNF secretion upon stimulation with trace amounts of lipopolysaccharide (LPS). Although the pretreatment neither enhanced nor significantly reduced the synergistic effect of MAF and A23187 on TNF-alpha mRNA expression, it did increase the expression stimulated by LPS alone. Finally, the PKc activity in M phi treated with PMA, PDBu, and mezerein was down-regulated to about 10% of control. Taken together, our results suggest that: 1) PKc plays an important role in the transduction of activating signals for M phi activation by MAF and A23187 to mediate cytotoxicity against some (P815) but not other (NS-1) tumor cells, 2) the induction of TNF-alpha mRNA expression and TNF secretion may be achieved via a PKc-independent pathway, and 3) M phi are equipped with more than one signal transduction pathways for affecting distinct functional activities.
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PMID:Effects of pretreatment with protein kinase C activators on macrophage activation for tumor cytotoxicity, secretion of tumor necrosis factor, and its mRNA expression. 261 73

Murine immunocytoma cell line, NS-1, was fused with spleen cells of Balb/C mice which had been stimulated by tolerogenic disaggregated human gamma globulin and immunized by purified serum IgM from the patient with chronic B cell leukemia (B-CLL). 10 hybridoma cell lines secreting monoclonal anti-idiotype (anti-Id) antibodies to human CLL were obtained. The McAbs were subclasses belonging to IgM and of IgG mouse. Specificity and biologic characters of the monoclonal anti-Id antibodies from culture fluid or ascites were assayed by ELISA, indirect mixed ELISA sandwich, ELISA inhibition, immunofluorescence (IF) and IF inhibition. The study also proved that monoclonal anti-Id antibodies could react with homologous IgM, but not with Ig from normal donors or a panel of patients with myeloma. The results of IF and IF inhibition assay showed that monoclonal anti-Id antibodies were bound to lymphocytes of patient with B-CLL. Their reactivity was inhibited by homologous IgM, but not by lymphocytes of patients with ALL or lymphoma. Monoclonal anti-Id antibodies were heterogenous reactive patterns with cell lines in vitro.
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PMID:Studies on monoclonal anti-idiotypic antibodies to human B cell leukemia. 263 Jun 54

Hybrid cell lines were prepared by the fusion of BALB/c myeloma NS-1 cells with the lymphocytes of BALB/c mice that were immunized with partially purified androgen receptor (AR) from human prostates. Nine clones of the hybrid progeny were determined for the production of antibodies against AR by immunoprecipitation assay. One of the clones, referred to as "5F4", was chosen for analysis of the detailed specificity. The clone "5F4" secreted IgM class antibodies against AR. Competition study demonstrated that "5F4" antibody inhibited androgen binding of AR, suggesting that the antibody identifies androgen binding site of AR. Immunoblotting analysis showed that the antibody identified the ARs as two proteins, 95 kD and 41 kD proteins, on a sodium dodecyl sulfate polyacrylamide gel. It is suspected that a 95 kD protein should be a monomeric AR and a 41 kD protein is a proteolytic fragment of AR. Immunohistochemical analysis demonstrated that androgen-dependent tissues--human prostatic hypertrophy tissues, an AR abundant prostatic cancer tissue and fibroblast cells from human genital skin--were stained intensely with "5F4" monoclonal antibody, while androgen-independent tissues--fibroblast cells from lymph nodes, an AR deficient prostatic cancer tissue and human prostatic cancer cell line, PC-3--showed no staining. These results also support the specificity of the antibody for AR.
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PMID:Establishment and characterization of monoclonal antibody against androgen receptor. 268 92

Mice were immunized against duck hepatitis B virus core (DHBc) particles isolated from the liver of asymptomatic carrier ducks of duck hepatitis B virus (DHBV) by ultracentrifugation. Their spleen cells were fused with mouse myeloma (NS-1) cells, and 12 clones of hybridoma cells secreting antibodies against DHBc (anti-DHBc) were isolated. According to the reactivity to core particles and core peptide obtained from DHBc particles treated with SDS-2ME, the 12 antibodies were classified into two groups. Two monoclonal antibodies reacted against both core particles and core peptide (B-type), the other ten monoclonal antibodies reacted against core particles but did not react against core peptide obtained from DHBc particles treated with SDS-2 ME. (A-type). Solid phase enzyme immuno assay (EIA) using these two types of antibodies could detect core antigenisity not only in the liver homogenate but also in the DHBV infected serum. Sucrose gradient analysis and gel filtration analysis revealed this DHBc antigenisity in the serum is not carried by core particles but carried by core peptide, equivalent to HBe antigen in the serum of Hepatitis B virus (HBV) carrier. This EIA may provide sensitive test monitoring both serum DHBe antigen levels and DHBc antigen levels in the liver during DHBV infection.
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PMID:[Preparation of monoclonal antibodies against duck hepatitis B core antigen and analysis of the monoclonal antibodies]. 269 Apr 59

We have used the cholesterol auxotrophy of NS-1 mouse myeloma cells as the basis for selecting NS-1 hybridomas. The outgrowth of nascent NS-1 hybridomas in cholesterol-free serum-free medium was 3- to 9-fold more efficient than that in HAT medium and resulted in 3- to 13-times as many antigen-reactive hybridoma wells. This method of hybridoma selection can be applied with any sterol-dependent parent cell line. Hybridomas established under serum-free culture conditions were growth inhibited by fetal calf serum.
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PMID:An alternative method for the isolation of NS-1 hybridomas using cholesterol auxotrophy of NS-1 mouse myeloma cells. 273 3

Monoclonal antibodies (MAb) against A cantonensis were produced through fusion of immunised spleen cells from BALB/c mice with NS-1 myeloma cells at a ratio of 10:1. The successful fusion rate on the 3rd day of fusion was 90.1%. Ten MAb were characterised, six of which were IgG1 and the remaining four were IgG2a, IgG2b, IgM and IgA respectively. Among 6 IgG1 MAb, four were A. cantonensis-specific, of which three reacted to adult worm antigen only and one reacted to both adult worm and juvenile worm antigens. Two other IgG1 MAb showed cross-reaction with other helminthic antigens of Toxocara canis. Ascaris suum. Paragonimus westermani, Dirofilaria immitis, Anisakis Spp, Gnatostoma Spinigerum and Clonorchis sinensis.
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PMID:Preparation of monoclonal antibody against Angiostrongylus cantonensis antigen. 277 97

Two monoclonal antibodies, designated 4C4 and 4G1, were produced by immunization of BALB/c mice with a human esophageal carcinoma cell line, CE69T/VGH, followed by fusion of the spleen cells from an immunized mouse with myeloma cells NS-1. 4C4 showed strong binding activity to three human esophageal carcinoma cell lines and one human hepatoma cell line, but not to any other cell lines tested. 4G1 reacted with three human esophageal carcinoma cell lines and four other cell lines. By peroxidase-antiperoxidase staining, 4C4 and 4G1 detected antigens of the epithelial cells on 10 pairs of esophageal carcinoma and normal esophageal specimens. 4G1 recognized a CE69T/VGH antigen with a molecular weight of 180K. Since 4G1 also reacted with purified carcinoembryonic antigen (CEA) and immunoprecipitated 125I-CEA, 4G1 seems to be an antibody recognizing CEA produced by CE69T/VGH cells. Since 4C4 also bound to the epithelial cells of normal uterine, vaginal, breast and liver tissues, it seems to recognize an epithelial antigen, and can be used to characterize the antigen in the specialization or differentiation of epithelial cells.
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PMID:Monoclonal antibodies against human esophageal carcinoma cell lines. 282 67

Lymph node lymphocytes from patients with primary lung cancer were immortalized with Epstein-Barr virus, and culture supernatants were screened for cell-surface reactivity against allogeneic cancer cell lines. The percentage of wells containing detectable antibodies in initial screening ranged from 1 to 17%, but the vast majority of the cultures lost antibody activity on subsequent expansion. Two antibody-secreting clones, J309 and D579, derived from separate individuals and reactive with anaplastic lung cancer cell lines, were successfully expanded and fused with the NS-1 mouse myeloma cell line. The antibodies produced by these clones exhibited identical restricted serologic reactivity against cultured cell lines and detected a carbohydrate antigen present in the neutral glycolipid fraction of MCF-7 breast cancer cells. Serologic, immunochemical, and chemical analyses revealed that the antigen recognized by antibodies J309 and D579 is galactosylgloboside [Gal(beta 1----3)GalNAc(beta 1----3)Gal(alpha 1----4)Gal(beta 1----4)- GlcCer]. Conclusions regarding the significance of these findings with respect to the biology of lung cancer await further information concerning the distribution of galactosylgloboside in normal and malignant tissues and the frequency of antibodies to this structure in normal and tumor-bearing individuals.
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PMID:Recognition of galactosylgloboside by monoclonal antibodies derived from patients with primary lung cancer. 283 67


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