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)

Eight monoclonal antibodies (MAbs) raised against human prostate cancer cell lines are described. One MAb was derived from the fusion of mouse myeloma P3x63Ag8-653 cells with spleen cells of mice immunized with DU145 prostate cancer cells. The other seven were from the fusion of myeloma lines P3x63Ag8-653 or SP2/0 with spleen cells of mice immunized with PC3, DU145 and 1013L prostate cancer cells. All of the antibodies also reacted with cell lines of other human cancer types, especially carcinomas. Immunoperoxidase staining on fixed tissue revealed strong reactivity only with antibody PrN10. Seven other antibodies seemed to bind to cell surface-associated (glyco)proteins. Antibodies PrL22 and PrO11 showed similar reactivity in radioimmunoassay, and immunoprecipitated a 160 kD molecular weight polypeptide from [125I]lactoperoxidase-labeled cells. Antibodies PrHk an PrQ12 bound to molecules with apparent MW of 115 kD and 100 kD, respectively; antibodies PrM24 and PrP14 revealed a more complex picture in immunoprecipitation of surface-labeled cells.
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PMID:Shared antigens of human prostate cancer cell lines as defined by monoclonal antibodies. 388 36

Mouse myeloma NS1-Ag4 cells were fused with spleen cells from a BALB/c mouse previously immunized with luteinizing hormone releasing hormone (LHRH) conjugated to serum bovine albumin (BSA). Fused cells were grown in HAT restrictive medium which was screened for LHRH binding ability via a primary binding assay employing [125I]LHRH and cold ethanol precipitation. One clone (hy-USASK/DSIL-LHRH-A1) was selected for further study. Cell culture fluid and ascites fluid bound 30% of [125I]LHRH at 1:4000 and 1:400,000 dilution respectively. A competitive inhibition assay using ascites fluid at 1:2,000,000 dilution and LHRH standards at 0.125-32.0 ng/ml was established. Initial studies using rabbit anti-mouse allotype sera in a horseradish peroxidase (HRP)-ELISA system indicate the antibody is IgG1. A dose of 0.5 ml ascites fluid containing LHRH antibody given intravenously (i.v.) on day 9 of gestation was effective in terminating pregnancy in rats. A 1 cm progesterone implant made of elastomer polymer and placed interperitoneally blocked this effect. Ascites fluid (4.5 ml) containing LHRH antibody, when infused i.v. into mature spayed female dogs induced a precipitous decline in mean luteinizing hormone (LH) levels and reduced LH pulsatility over 4 days. It was concluded that the mouse monoclonal antibody is specific for LHRH, and can interrupt reproductive events in vivo.
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PMID:Monoclonal antibodies against LHRH: development and immunoactivity in vivo and in vitro. 388 2

An enzyme-linked immunosorbent assay (ELISA) for determination of antibodies against the zona pellucida was developed and compared with the already available indirect immunofluorescence (IIF) technique. Sera from 100 women with explained and unexplained infertility were screened for the presence of autoantibodies to the zona pellucida by ELISA and IIF techniques. Porcine/goat zonae immobilized on activated microtitre plates or solubilized zona pellucida antigens adsorbed on poly-L-lysine-coated microtitre plates were used as a solid phase in an ELISA. Assay of anti-zona pellucida antibodies in xenogeneic and allogeneic sera was performed by incubation of test samples with the solid phase against human serum supplied by WHO as a reference positive control, followed by incubation with staphylococcal protein A conjugated to horseradish peroxidase. The ELISA was effectively used to screen the production of monoclonal antibodies from mouse myeloma X mouse splenocyte hybridomas. The sensitivity of the ELISA was more than 2500-fold greater than that of the IIF technique. Significantly high titres of autoantibodies to zona pellucida were found in patients with unexplained infertility as compared with patients with a known cause of infertility, and their normal counterparts.
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PMID:Enzyme-linked immunosorbent determination of autoantibodies to zona pellucida as a possible cause of infertility in women. 388 60

After a brief examination of the recent literature on non-secretory multiple myeloma, the Authors describe the immunohistologic study (peroxidase-antiperoxidase method) of a case of truly non producing plasmacytoma, interesting because of the presence of a small polyclonal plasma cell population within the neoplastic clone. Several possible explanations are considered.
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PMID:[Non-secretory plasmacytoma. Bibliographic review and immunohistochemical study of a case]. 389 70

A monoclonal antibody, designated NAT-9 II:3F-6F (IgM), was generated by hybridization of mouse myeloma cells with spleen cell from mice immunized with normal human bone marrow cells. The antibody reacted with 40-60% of bone marrow cells as analysed on samples from 40 normal individuals and only with a subpopulation of human acute myeloid leukemia (AML) cells of the M2 class (20/20 tested) and M4 class (12/12 tested) (subclasses of the French-American-British (FAB) classification), but not with leukemic cells of the M1 (0/12 tested) and M5 (0/12 tested) FAB subclasses. This is in contrast to many other myeloid-specific monoclonal antibodies. Fluorescence-activated cell sorter (FACS) analyses and morphological examination of cells stained with peroxidase as based on the NAT-9 II:3F-6F monoclonal antibody showed that this antibody reacted with a distant differentiation antigen which is absent on myeloblasts, but expressed on promyelocytes, myelocytes, metamyelocytes, band neutrophils, and on a minority of mature granulocytes. NAT-9 II:3F-6F did not bind to circulating monocytes, T and B cells, erythrocytes and a variety of different human cell culture lines. Immunoblotting demonstrated that the antibody bind to a cellular component with a Mr approximately 97.400 dalton. The antibody may be useful in immunological subclassification of non-lymphoid leukemias and in studies on hematopoiesis.
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PMID:A monoclonal antibody (NAT-9 II:3F-6F) that identifies a differentiation antigen on human myeloid cells. 390 84

A subglottic primary extramedullary plasmacytoma (typ IgA-Lambda) of the larynx is reported. These tumours are very rare. The diagnosis is made more difficult by unspecific symptoms and can only be confirmed by histopathology. Early diagnosis and differentiation between primary extramedullary plasmacytoma and metastasis from a multiple myeloma are very important for the prognosis of the disease. Whether immunology can help to solve this problem is still doubtful: few cases have so far been examined by this method. Paraproteins are often not secreted in extramedullary plasmacytoma; the peroxidase-anti-peroxidase method is therefore helpful for classification of the tumour.
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PMID:[Subglottic plasmacytoma: diagnosis and prognosis]. 392 27

kappa-Myeloma antigen (KMA) was immunoprecipitated from lactoperoxidase-radioiodinated HMy2 lymphoblastoid cells by using monoclonal antibody K-1-21 and was analyzed by SDS-PAGE. Under reducing conditions, two major subunits of Mr approximately 26,000 and Mr approximately 42,000, and minor components of Mr approximately 28,000, 31,000, and 36,000 were observed. The Mr approximately 26,000 subunit was identical to kappa-light chains from HMy2 surface IgG in apparent m.w., isoelectric point, and staphylococcal V-8 protease peptide map, but was not precipitated in association with Ig heavy chain. The Mr approximately 42,000 component was homologous to rabbit skeletal muscle actin by peptide mapping with staphylococcal V-8 protease. The cell surface origin of the immunoprecipitated antigen was confirmed by demonstrating lactoperoxidase dependence of iodination and complete removal from the cell surface after pronase treatment of viable cells. Thus, cell surface expression of KMA is the result of membrane association of non-heavy chain-linked kappa-light chains, possibly in noncovalent association with actin.
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PMID:Structural analysis of the myeloma-associated membrane antigen KMA. 392 6

Rats were immunized with cultured cells from chemically induced transitional cell carcinomas of the mouse urinary bladder, and their spleen cells were hybridized with NS-1 mouse myeloma cells. Following initial screening of antibodies made by hybridoma clones, the tissue distribution of antigens defined by the antibodies was established by using a peroxidase-antiperoxidase technique with frozen sections of a variety of mouse tumors, as well as normal adult and embryonic tissues. Two antibodies were identified which detected antigens with bladder carcinoma specificity. One antibody (3B12) reacted weakly with epithelial cells from several sources, including normal bladder, while the second antibody (6.10), which bound strongly to bladder carcinoma cells, was negative on bladder epithelium and bound (weakly) to only a small fraction of all epithelial cells tested except for epidermal cells and periosteum from embryos. Both antibodies should be useful to assess the immunotherapeutic and immunoprophylactic effects of monoclonal antibodies to tumor-type specific oncofetal antigens.
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PMID:Monoclonal antibodies to cell surface antigens shared by chemically induced mouse bladder carcinomas. 398 70

About 2,000 antibody-producing hybrids were obtained by fusion of lymphocytes harvested from mice hyperimmunized with the human carcinoma line A 431 and P3-X63-Ag8-653 myeloma cells. Antibody specificity was screened in a radiobinding assay performed on glutaraldehyde-fixed cultured cells, and on paraffin-embedded sections stained with the method of avidin-biotin-peroxidase. Among the clones, 16 produced antibodies reacting with a variety of tumor lines but not with human fetal fibroblasts or peripheral blood leukocytes. On the basis of their specificity, monoclonal antibodies were classified into three groups. Some reacted only with the A431 line used as immunogen: One antibody reacted with an antigen preferentially expressed on cancer of the gastrointestinal tract and ovary; A group of monoclonal antibodies displayed a broader spectrum of reactivity defining a panel of antigens that could be tentatively classified as epithelial specific.
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PMID:Monoclonal antibodies against the human epidermoid carcinoma A 431. 406 36

Polymeric IgA (pIgA) is transported by liver parenchymal cells (hepatocytes) from blood to bile via a receptor-mediated process. We have studied the intracellular pathway taken by a TEPC15 mouse myeloma pIgA. When from 1 microgram to 1 mg 125I-pIgA was injected into the saphenous vein of a rat, 36% was transported as intact protein into the bile over a 3-h period. The concentration of transported 125I-pIgA was maximal in bile 30-60 min after injection, and approximately 80% of the total 125I-pIgA ultimately transported had been secreted into bile by 90 min. A horseradish peroxidase-pIgA conjugate (125I-pIgA-HRP) was transported to a similar extent and with kinetics similar to that of unconjugated 125I-pIgA and was therefore used to visualize the transport pathway. Peroxidase cytochemistry of livers fixed in situ 2.5 to 10 min after 125I-pIgA-HRP injection demonstrated a progressive redistribution of labeled structures from the sinusoidal area to intermediate and bile canalicular regions of the hepatocyte cytoplasm. Although conjugate-containing structures began accumulating in the bile canalicular region at these early times, no conjugate was present in bile until 20 min. From 7.5 to 45 min after injection approximately 30% of the labeled structures were in regions that contained Golgi complexes and lysosomes; however, we found no evidence that either organelle contained 125I-pIgA-HRP. At least 85% of all positive structures in the hepatocyte were vesicles of 110-160-nm median diameters, with the remaining structures accounted for by tubules and multivesicular bodies. Vesicles in the bile canalicular region tended to be larger than those in the sinusoidal region. Serial sectioning showed that the 125I-pIgA-HRP-containing structures were relatively simple (predominantly vesicular) and that extensive interconnections did not exist between structures in the sinusoidal and bile canalicular regions.
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PMID:Transcellular transport of polymeric IgA in the rat hepatocyte: biochemical and morphological characterization of the transport pathway. 406 52


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