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)

Cloned hybridoma cell lines were obtained from fusions of murine myeloma cells with lymphocytes of mice immunized against human breast cancer cells. Hybridomas F36/22 and M7/105 produced antibodies whose binding to breast cancer cells could not be inhibited by prior absorptions with fibroblasts, lymphoblastoid cells, or erythrocytes. Results from cell surface binding assays using a panel of tumor cell lines indicated that antibodies F36/22 and M7/105 recognized determinants expressed maximally on breast cancer cells. Antibody F36/22 reacted with normal mammary epithelial membranes and milk fat globule membranes, whereas antibody M7/105 produced no detectable binding to these specimens. Antigens carrying these epitopes each showed reactivity with concanavalin A lectin. The determinant corresponding to antibody F36/22 was detectable in histological sections of a subset of breast tumors obtained at surgery.
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PMID:Monoclonal antibodies (F36/22 and M7/105) to human breast carcinoma. 633 43

A mouse monoclonal antibody (IgM) was obtained by cell hybridization between X63-Ag8.653 myeloma cells and spleen cells from a BALB mouse that was immunized with GRSL leukemia cells of the GR strain. This antibody identified a unique fetal antigen, which is expressed exclusively on embryonic thymocytes of all strains tested. Therefore, the antigen defined was named fetal thymus antigen-1, FT-1. The proportion of FT-1+ fetal thymocytes detected by immunofluorescence assay sharply decreases as gestation time increases, and finally they disappear from the thymus. On the other hand, Thy-1+ cells increase in inverse proportion. The immunofluorescence studies and absorption tests showed that FT-1 antigen is not detectable on brain, liver, kidney, or lymphoid tissue cells of adult mice. However, it is expressed on some leukemia cells of various mouse strains, which demonstrated that this is the first example of an oncofetal antigen of a mouse leukemia. The molecular weight of FT-1 antigen on leukemia cells was estimated to be 130,000 by means of biosynthetic labeling with [3H]galactose and [35S]methionine. The two-dimensional gel electrophoresis pattern of FT-1 antigen shows a family of glycoproteins with extensive charge heterogeneity. It was also shown that the FT-1 antigen molecule carries the receptor for DBA lectin.
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PMID:A new differentiation antigen (FT-1) shared with fetal thymocytes and leukemic cells in the mouse. 660 76

With the aim of obtaining monospecific antibodies against the beta-galactoside-binding lectin of bovine heart muscle, spleen cells from Lou rats immunized with lectin were fused with the rat myeloma line Y3.Ag1.2.3. Two immunoglobulin M (IgM)-producing clones, designated NIBy 142-36/8 and NIBy 143-9/5, derived from separate fusions, were used to generate ascites containing high-titre binding activity against the 13kDa component in preparations of lectin. Direct evidence that haemagglutinating activity is associated with the 13kDa protein was obtained by the specific elution of 13kDa polypeptides with haemagglutinating activity from an immobilized antibody adsorbent. Solid-phase radiobinding assays and immunoblotting of isolated lectins and/or muscle homogenates confirmed the earlier indications with conventional antisera that the beta-galactoside-binding lectins of bovine, human and monkey muscle tissue are antigenically related.
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PMID:Production and characterization of monoclonal antibodies to beta-galactoside-binding lectin of bovine heart muscle. Direct evidence that haemagglutinating activity is associated with a 13kDa protein. 674 65

Spleen cells from mice immunized with the Dolichos biflorus seed lectin were fused with cells from the mouse myeloma Sp2/O-Ag14 cell line to form hybridomas. Those hybridomas producing antibodies against the seed lectin were cloned at least four times and the monoclonal antibodies from clone C11/64-56.28 were characterized and found to be specific for Subunit I of the lectin; they do not react with the structurally similar Subunit II. In previous studies, we have shown that although these two subunits appear to differ only at their COOH-terminal ends, only Subunit I has carbohydrate binding activity. Using a solid phase enzyme immunoassay, the antigenic determinant fr the monoclonal antibody was found to be located on the COOH-terminal cyanogen bromide fragment of this subunit. The monoclonal antibody inhibits the ability of the lectin to agglutinate erythrocytes and N-acetyl-D-galactosamine, the specific hapten for the lectin, inhibits the ability of the antibody to combine with the lectin. These results suggest that the monoclonal antibody recognizes a determinant that is located either at or near the active site of the lectin or that is conformationally interdependent with the active site.
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PMID:Production and characterization of a monoclonal antibody against the seed lectin of the Dolichos biflorus plant. 678 73

A xenoantiserum to murine B16 melanoma cells was developed by immunizing rabbits with cultured B16 melanoma cells. This antiserum could, after extensive absorption with normal C57BL/6 mouse tissues, react with syngeneic (B16) and allogeneic (HP) melanomas as well as with other murine neoplasms, including syngeneic 75S adenocarcinoma, allogeneic myeloma and leukemic T cell lines. The antiserum also cross-reacted with syngeneic fetal fibroblasts and with an allogeneic fetal fibroblast cell line (SC-1) either uninfected or infected with murine leukemia virus (MuLV). Immunoprecipitated material from B16 melanoma cell-surface glycoproteins that had been labeled with [125I] by lactoperoxidase and purified by a Lentil lectin column was analyzed by one-dimensional SDS- and two-dimensional polyacrylamide gel electrophoresis, which disclosed an acidic glycoprotein with a molecular weight (mol. wt) of 90 K daltons. Absorption studies suggested that the 90 K mol. wt gylcoprotein represented the oncofetal moiety expressed in murine medanoma, carcinoma and fetal tissues. When the amount of this antigen in developing C57BL/6 mouse fetuses was measured by absorption assays, we found that it was expressed strongly in those fetuses just before birth. Binding and absorption studies demonstrated that the 90 K mol. wt glycoprotein, while being expressed on a variety of fetal and neoplastic cells in mice, did not exist at detectable levels in normal tissues of adult C57BL/6 mice, including tissues of the thymus, lymph node, spleen, liver, brain, lung and kidney.
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PMID:Identification of an oncofetal antigen (gp90) on murine B16 melanoma cells. 688 31

A factor in normal serum that selectively and reversibly inhibits proliferation of cells in culture has been enriched 160-fold from calf serum by sequential ammonium sulfate precipitation, gel filtration, and lectin-affinity chromatography. DNA synthesis of normal (but not transformed) rat hepatocytes, human lymphoblast lines, and mitogen-stimulated murine spleen cells is inhibited by greater than 90%, and Vero, murine myeloma, MELC, and a human colon carcinoma cell line to a lesser extent. Growth of other cell lines tested was not affected. Responsive cells are arrested apparently in G1 by this inhibitor, the effect of which is maximal by 24 hr and is spontaneously reversible thereafter unless it is renewed. The active fraction is a protein that migrates with the alpha 2-globulins; it is not a lipoprotein, and it is of high apparent molecular weight.
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PMID:A selective inhibitor of cell proliferation from normal serum. 692 35

Native tetravalent Con A and the divalent acetylated derivative increased the hemolytic titer (i.e., the reciprocal of the antibody dilution required to give an average of one lytic site per sheep erythrocyte) of IgG antibodies against Forssman antigen by up to 225% with guinea pig and human complement. Although the average number of lytic sites generated at each antibody concentration increased, the slope of the titration curve did not change. Other lectins with the same or different sugar specificity either augmented or inhibited hemolysis but were less potent than Con A. Augmentation by Con A was consistent with the ability of lectin on the cell surface to bind but not activate guinea pig C1. Thus it appears that cell-bound Con A and IgG yield a complex that behaves like a doublet of IgG antibody molecules in its ability to fix and activate C1, when activation is dependent on the IgG component. In contrast, the highest dose of Con A inhibited by at least 50% the hemolytic activity of IgG antibodies against either a sugar-free protein (HSA) or a protein reactive with Con A (human myeloma IgE) using cells to which these antigens were coupled with chromic chloride. This suggests that the identity, density, and/or mode of presentation of the antigen on the cell surface may be important determinants of lectin-induced augmentation. Although both the enhancement or inhibition by Con A in the presence of whole C correlated with the number of C1 molecules bound and activated, there was no correlation with the ability of the lectin to agglutinate the cells.
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PMID:Enhancing effect of concanavalin A on the hemolytic activity of anti-Forssman IgG: the role of C1. 710 4

Changes in the activity and transcription of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4-N-acetylglucosaminyl-transferase III (GnT-III: EC 2.4.1.144) were investigated in haematological malignancies. GnT-III activity was elevated in patients with chronic myelogeneous leukaemia in blast crisis (CML-BC) and patients with multiple myeloma (MM); whereas most of the normal healthy subjects and patients with other haematological malignancies, including CML in its chronic phase, showed negligible activity. The GnT-III transcript of leukaemic cells from various haematological diseases showed a single band with a similar size. The ratio of GnT-III activity per normalized transcript in CML-BC was considerably higher than in the other conditions, which provided the possibility that in CML-BC the transcript or the enzyme protein might be more stable, or that a post-translational modification of the enzyme might enhance its activity. Furthermore, a lectin blot analysis of patient specimens and a lectin fluorescence study of CML cell lines revealed that E4-PHA binding to surface glycoproteins correlated with GnT-III activity, indicating that more bisecting GlcNAc was added to these glycoproteins, catalysed by elevated GnT-III in CML-BC.
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PMID:Changes of beta-1,4-N-acetylglucosaminyltransferase III (GnT-III) in patients with leukaemia. 749 37

The lectin peanut agglutinin (PNA) and CD19 monoclonal antibody have been covalently linked to magnetic beads and utilized in an in vitro purging system for autologous bone marrow in multiple myeloma (MM). An alternative to mechanical purging involves the use of immunotoxins to provide specifically targeted cellular toxicity; however, no studies to date have examined the utility of a lectin-ricin A chain (RCA) combination as a purging agent in MM. Initially, we studied the internalization of PNA by target cells (Raji) using flow cytometry. The surface fluorescence intensity of PNA-treated Raji cells was reduced upon incubation at 37 degrees C, and subsequent studies with fixed cells detected the endocytosed PNA. Complete internalization occurred within 120 minutes, indicating the potential of PNA as a purging agent. We manufactured a novel PNA-RCA conjugate and demonstrated its strong and specific binding to PNA reactive cell targets. Subsequent experiments assessed the toxicity of the conjugate to Raji cells and normal bone marrow progenitor cells. 3H-leucine uptake assays showed that PNA-RCA was capable of reducing protein synthesis in Raji cells and that the toxic effects were specific. In addition, at concentrations of conjugate achieving greater than 99% selective cytotoxicity for Raji cells, adequate CFU-GM were preserved in normal marrow. These studies suggest that PNA-RCA may be of value as an in vitro purging agent for MM.
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PMID:The synthesis of a peanut agglutinin-ricin A chain conjugate: potential as an in vitro purging agent for autologous bone marrow in multiple myeloma. 749 62

A new method of in vitro bone marrow purging using a lectin and monoclonal antibody in combination has been used for the first time in vivo. Two patients with advanced myeloma were treated with high-dose melphalan and total body irradiation and then rescued with autologous bone marrow which had been purged in vitro to remove malignant cells by using a combination of a plasma cell-binding lectin (peanut agglutinin, PNA) and the anti-B lymphocyte monoclonal antibody anti-CD19, bound to magnetised microspheres. Both patients showed rapid engraftment of the purged bone marrow and remain well 36 and 46 months later with normal bone marrow morphology, although one patient still has a low level of circulating paraprotein. This is a promising form of therapy for what has been an invariably fatal condition.
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PMID:Autologous bone marrow transplantation for myeloma patients using PNA- and CD19-purged marrow rescue. 752 27


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