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)

Fusion of P3/X63-Ag8 mouse myeloma cells with splenocytes obtained from mice hyperimmunized with a BHK hamster fibroblast line transformed by an env-strain of Rous sarcoma virus (RSV) resulted in the production of antibody-secreting hybridomas. Seven hybrid clones secreted antibodies binding to RSV-transformed BHK fibroblasts but not to the parental control non-transformed line. The antibodies produced by three of these clones did identify antigenic determinants expressed also on BHK cells transformed by SV 40. The antibodies produced by four other clones reacted specifically with cells transformed by RSV but not with cells productively infected by the transformation-defective Rous-associated virus-1; one of these reacted with RSV-transformed hamster cells only, three others identified antigenic determinants common to RSV-transformed cells of different animal species. These data give further support to the idea that RSV-transformed cells express a cell-surface antigen, specific for transformation, the expression of which is controlled by the transforming src gene, and that the specificities carried on it follow a complex pattern, arising from the interaction between antigenic determinants of cellular and viral origin.
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PMID:Dissection of the antigenic determinants expressed on the cell surface of RSV-transformed fibroblasts by monoclonal antibodies. 617 48

Transformation of cells by Rous sarcoma virus is mediated by the product of the viral src gene, pp60src. A hybridoma cell line producing an immunoglobulin G3 antibody to pp60src was isolated after lymph node cells from immune mice were fused with mouse myeloma cells (P3-NS1-1). Mice were immunized with p60src purified from Escherichia coli cells expressing the src gene product. The monoclonal antibody immunoprecipitated pp60src from Rous sarcoma virus-transformed cells and recognized an antigenic determinant located in the amino-terminal third of the pp60src protein.
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PMID:Isolation and partial characterization of a monoclonal antibody to the Rous sarcoma virus transforming protein pp60src. 618 41

The major component of the core structure of avian sarcoma leukosis viruses is a 27 kD molecular weight polypeptide, p27. Spleen cells from mice immunized with the Schmidt-Ruppin strain of Rous sarcoma virus (RSV) were fused with mouse myeloma cells (SP2/0), and hybridoma cell lines producing monoclonal antibodies to p27 were isolated. The monoclonal antibodies were all of the IgG1 subclass with kappa light chains. These antibodies immunoprecipitated p27 and its precursor proteins from extracts of RSV-transformed cells. Reciprocal competitive binding experiments defined five nonoverlapping antigenic determinants within p27. The monoclonal antibodies also immunoprecipitated the transforming protein, p110gag-myc, from avian myelocytomatosis virus transformed cells. Their usefulness in studies of virion maturation and viral oncogenesis is discussed.
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PMID:Monoclonal antibodies specific for the virion polypeptide, p27, of avian retroviruses. 620 83

Hybrid cell lines were prepared by the fusion of BALB/c myeloma P3U-1 cells with the lymphocytes of BALB/c mice that were immunized with syngeneic Rous sarcoma virus (RSV)-induced tumor CSA1M cells. Three clones of the hybrid progeny (3.4B2, 3.4C6, and 3.5C11) produced cytotoxic IgM antibodies against CSA1M cells. One of the clones, 3.5C11, was chosen for analysis of the detailed specificity. Both direct cytotoxicity assays and absorption tests revealed that monoclonal antibody from 3.5C11 was positive only with CSA1M cells and that it failed to react with other tumors, including 20 RSV-induced mouse tumors, and normal cells. The 3.5C11 monoclonal antibody alone, with or without exogenous complement, was suppressive in the therapy of ip injected CSA1M tumor in syngeneic hosts, and significant prolongation in survival was seen in the treated mice. These results clearly showed presence of an individually distinct tumor-specific cell surface antigen on an RSV-induced mouse tumor.
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PMID:Individually distinct tumor-specific cell surface antigen identified by monoclonal antibody on a Rous sarcoma virus-induced mouse tumor. 628 79

A hybridoma cell line which secretes antibody to the Rous sarcoma virus (RSV) structural protein p27 has been established. The hybrid resulted from the fusion of NS-1 myeloma cells with spleen cells from a Balb/c mouse which was immunized with RSV-transformed mouse cells. Antibodies produced by the hybrid clone immunoprecipitated p27 and gag precursor proteins (Pr180gag,pol, Pr76gag and Pr66gag) from [35S]methionine-labelled chicken embryo fibroblasts transformed by the Schmidt-Ruppin strain of RSV. When Schmidt-Ruppin virus was radioactively labelled with [35S]methionine, p27 was the only virus structural protein immunoprecipitated. Antibody production by the hybrid clone (designated 7-29-D6) has remained stable for longer than 12 months at a level of 50 micrograms IgG/ml medium. A highly sensitive method to determine the subclass specificity of monoclonal antibodies is described. In this procedure, the clone is incubated with [35S]-methionine, and radiolabelled antibody is precipitated with affinity-purified, subclass-specific rabbit anti-mouse serum and Staphylococcus aureus. The advantages of this procedure are discussed.
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PMID:Monoclonal antibody specific for avian sarcoma virus structural protein p27. 629 57

Thirteen clones of hybrid cells which synthesize antibodies directed against the Rous sarcoma virus (RSV) transforming protein, pp60src, were isolated. Mouse myeloma cells were fused with spleen cells from mice that had been immunized with purified pp60src from bacterial recombinants which direct the synthesis of the RSV src gene. The hybridomas which survived the selection medium were screened by immunoprecipitation of pp60src from 32P-labeled lysates of RSV-transformed cells. Monoclonal antibodies produced by subclones derived from 13 hybridomas recognized pp60src encoded by the Schmidt-Ruppin and Prague strains of RSV and the cellular homolog of pp60src. Antibody from clone 261 had a high affinity for the viral yes gene product, and antibodies from clones 443 and 463 recognized the transforming proteins encoded by viruses containing the related transforming genes fps and ros. Several other clones had a low affinity for the viral yes, fps, and ros gene products which could be detected by in vitro phosphorylation of the transforming proteins after immunoprecipitation with the monoclonal antibody. All of the monoclonal antibodies allowed phosphorylation of pp60src and casein in an immune complex-bound reaction.
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PMID:Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. 631 92

Spleen cells from BALB/c mice, previously immunized with rat cerebellar tissue, were fused to the mouse myeloma cell line SP2/0-Ag14 and the cerebellar cell type specificity of the resultant hybridomas determined. In this report we describe the specificity of one hybridoma, C4/12. Monoclonal antibodies secreted by this hybridoma recognize granule cell neurons in adult cerebellar frozen sections, and in primary cultures started from 3 to 5-day-old newborn rats. In addition, C4/12 recognizes a subclass of astrocytes when screened on primary cultures but not adult cerebellar tissue. Two temperature sensitive Rous sarcoma virus transformed cerebellar cell lines, previously shown to be either neuronal or glial, were screened for the presence of the antigen. Both cell lines are positive at the temperature permissive for transformation, whereas the glial line but not the neuronal line exhibits the antigen at the nonpermissive temperature. These results are discussed in light of the cell lines being representative of precursor cells.
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PMID:Immunological identification of cerebellar cell lines. 704 26

To investigate the mechanism of myoblast fusion using quail myoblasts transformed with a temperature-sensitive mutant of Rous sarcoma virus (QM-RSV cells), we prepared monoclonal antibodies against a cell surface antigen involved in myogenic differentiation. For this, a Balb/c mouse was immunized with the membrane fraction of QM-RSV cells, and hybridomas producing monoclonal antibodies were raised by fusion of spleen cells from the immunized mouse with myeloma cells. By analysis of the hybridoma supernatants, we obtained a monoclonal antibody, termed H-145, that strongly inhibited myoblast fusion. H-145 inhibited myoblast fusion dose-dependently, and its effect was readily reversed by its removal. H-145 promoted biochemical differentiation of the cells until 48 h. It did not affect a fusion-commitment step to differentiation, but inhibited a later step. Indirect immunofluorescence and immunoblot analyses showed that the antigen reacting with H-145 was a glycoprotein with a molecular weight of approximately 116 kDa. This antigen is present throughout differentiation, but as differentiation progresses, its expression increases and its distribution on the cell surface changes. The antigen purified by H-145 affinity chromatography failed to react with beta 1-integrin, alpha 5-integrin, NCAM, or N-cadherin on immunoblotting. Thus, H-145 antigen differs from these components that are known to be associated with myogenic differentiation. Consequently, the results suggest that H-145 antigen may be a new cell surface antigen associated with cell differentiation.
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PMID:Preparation and characterization of a monoclonal antibody that inhibits myoblast fusion of avian skeletal myoblasts. 817 34