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)

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

Our trial to produce human monoclonal antibodies with human-mouse hybridomas is described. Human spleen cells, in comparison with peripheral blood lymphocytes, bone marrow cells and lymphnode lymphocytes, seem to be the best partner to fuse with myeloma line NS-1 to obtain hybridomas. About sixty percent of hybridomas derived from human spleen cells at first produce human Ig which in most cases belong to either IgG or IgM. Fifty percent of hybridomas which had initially produced human Ig continued to do so after 4 months. One of the clones of human monoclonal antibodies reacted with a cell surface antigen expressed on three out of 5 B cell lines, 14 out of 38 Epstein-Barr virus transformed B cell lines and null cell type lymphocytic leukemia cells obtained from one patient out of 34 tested. Other normal or malignant cells, hematopoietic or nonhematopoietic cells examined were negative. The antigen does not seem to be related to EBNA, early antigen and VCA of EB virus, or certain haplotype specificity of HLA-A, B, C, and DR loci. Reports by others on production of monoclonal antibodies with similar approaches were also reviewed.
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PMID:[Human monoclonal antibodies with human-mouse hybridomas]. 660 96

This study describes the monoclonal antibody 5E9 and the cell surface antigen it defines. The hybridoma cell line T3-5E9 was derived from fusion of P3 X 63/Ag8 myeloma cells and spleen cells from BALB/c mice immunized with HSB-2 cells, a human T cell line. Although binding to only 1 to 5% of peripheral blood (PB) and spleen mononuclear cells, 5E9 antibody bound to 40 to 80% of Con A-, PHA-, or PWM-activated PB cells. Moreover, 5E9 antibody bound to variable numbers of Sezary, acute myelogenous leukemia, and ALL PB leukemia cells. 5E9 antibody bound to all hematopoietic and nonhematopoietic cell lines tested, to 11 +/- 1% of thymocytes, and 40% of nucleated bone marrow cells. Under reducing conditions, immunoprecipitation studies using 5E9 antibody demonstrated 5E9 antigen to be an 90,000 m.w. glycoprotein. Under nonreducing conditions, antigen 5E9 is a disulfide-linked dimer of approximately 190,000 daltons. Sequential precipitation experiments using antibody 5E9, alpha OD heteroantiserum (raised against T ALL cells), and monoclonal antibody OKT9 demonstrated that the 3 antibody preparations recognized the same 90,000 m.w. glycoprotein. Thus, antibody 5E9 defines an 90,000 m.w. human cell surface antigen that is absent on the majority of PB mononuclear cells and is expressed on rapidly dividing normal and malignant human cells. This monoclonal antibody should be a useful marker of human cell activation.
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PMID:Characterization of a monoclonal antibody (5E9) that defines a human cell surface antigen of cell activation. 678 29

Hybridomas were generated by fusing SP2/0 mouse myeloma cells with spleen cells from mice that had been immunized with cultured human melanoma cells. One of the hybridomas secreted a monoclonal IgG1 antibody, 48.7, which binds to a cell surface antigen of cells from human melanomas and compound nevi. The presence of the target antigen in vivo was demonstrated immunohistologically by staining frozen sections of primary and metastatic melanoma by the peroxidase anti-peroxidase technique. Weak staining of some blood vessel cells was also seen, but other normal cells, including skin melanocytes, were unstained, as were cells from other tumor types. Antibody 48.7 immunoprecipitated polypeptides with apparent m.w. on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 250,000 and greater than 400,000.
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PMID:Studies of a high molecular weight human melanoma-associated antigen. 682 41

This study represents an initial attempt to analyze the humoral immune reactions of patients with malignant melanoma by hybridoma methodology. Using lymphocytes from regional lymph nodes, peripheral blood and tumor infiltrates, 158 fusions were performed with SKO-007 (human myeloma line), LICR-LON-HMy2 (LICR-2), GM 4672 (human lymphoblastoid lines), or NS-1 (mouse myeloma line). Fusion of lymph node lymphocytes with NS-1 resulted in a 3-4 times higher frequency of clones than fusion with LICR-2, and a 10 times higher frequency than fusion with SKO-007 or GM 4672. In the case of peripheral blood lymphocytes, fusion with NS-1 gave greater than 25 times higher frequency of clones than fusion with LICR-2 or SKO-007. Production of human mu, gamma, or alpha heavy chains was detected in 50-80% of wells containing growing clones, and the levels of immunoglobulin ranged from 0.3 micrograms to 40 micrograms/ml. NS-1-derived clones could be easily subcultured, while LICR-2 and SKO-007 clones grew more slowly on subculturing. In this study, Ig secretion appeared to be a more stable property of LICR-2-derived clones than NS-1-derived clones. A panel of 20 human cancer cell lines was used to screen 771 Ig-secreting cultures for antibody to cell surface or intracellular antigens. Reactivity with cell surface antigens was found infrequently (6 cultures), whereas reactivity with intracellular antigens was more common (27 cultures). A new cell surface antigen with properties of a glycolipid was defined with an IgM monoclonal antibody secreted by a tetraploid cell derived from a fusion of LICR-2 with lymphocytes from the axillary lymph node of a patient with melanoma. The hybrid cell line has been subcloned four times and secretes 5 micrograms IgM/ml. The antigen detected by this IgM antibody was found on 5 of 23 melanoma cell lines and 12 of 30 epithelial cancer cell lines. No reactions were found with 11 cultures derived from normal cells. Stable cell lines secreting human antibody that detected nuclei, nucleoli, cytoskeletal elements, Golgi complex, or other cytoplasmic components were also isolated in this study. One of these antibodies detected an intracellular antigen that is restricted to cells of neuroectodermal derivation, and a second antibody reacted primarily with cells of epithelial origin. Using these methods to isolate and analyze human monoclonal antibody, it should now be possible to define the repertoire of the humoral immune response to melanoma.
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PMID:Detection of cell surface and intracellular antigens by human monoclonal antibodies. Hybrid cell lines derived from lymphocytes of patients with malignant melanoma. 686 64

Monoclonal antibodies to murine lymphocyte differentiation antigens were generated by fusing the mouse myeloma cell line X63-Ag8.653 with spleen cells derived from Lewis rats hyperimmunized with lymphoid cells from nude (C57BL/6) mice. One of these antibodies--designated 3MB1--recognizes a previously undescribed cell surface antigen. This antigen is expressed on 62% of spleen cells, 9% of thymus cells, and 98% of peritoneal macrophages. Virtually all LPS- and Con A-induced lymphoblasts carry this newly found antigen. The 3MB1 determinant is limited in its expression to leukocytes. It is not found in other tissues such as brain, liver, kidney, or on erythrocytes. Biochemical analysis reveals that the 3MB1 target antigen consists of a single chain glycoprotein with an approximate m.w. of 90,000.
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PMID:A new murine cell surface differentiation antigen (Leugp90) defined by a rat monoclonal antibody: cellular distribution and biochemical characterization. 697 11

The cytochemical stain Hoechst 33342 has been used to quantify DNA in viable cells and has been used under nonsaturating conditions to discriminate between lymphoid cell types. In order to correlate the quantitative emission from Hoechst 33342 with cell surface antigens, a fluorescence activated cell sorter was modified to simultaneously detect emission from the UV excited Hoechst dye and fluorescein attached to the cell surface by immunofluorescence techniques. A special set of laser mirrors was installed in an argon ion laser so that all the lines from 351-488 nm could be used to illuminate the cells. Appropriate emission filters were used to separate the light emitted by Hoechst 33342 from the fluorescein. An electronic cross-over circuit was used to compensate for special overlap between the two dyes. Analysis of murine lymph node cells stained both with Hoechst 33342 under nonsaturating conditions and anti-Thy 1.2 indicated that the cells that stained dimly with the Hoechst dye expressed the Thy 1.2 marker while the cells that were brightly stained with Hoechst 33342 lacked this differentiation antigen. The correlation of cell surface myeloma protein with cell cycle on an in vitro cell line indicated that the heterogeneity of cell surface antigen expression could not be accounted for solely by variations occurring during the cell cycle.
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PMID:Simultaneous quantitation of Hoechst 33342 and immunofluorescence on viable cells using a fluorescence activated cell sorter. 702 25

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

Two hybridoma clones have been produced by hybridization of murine myeloma cell line PAI and splenocytes from BALB/c mice immunized with cells from a transplantable sarcoma induced in rat by SR-RSV. The antibody produced by hybridoma clone 2C2 was of subclass IgG3 and recognized a cell surface antigen of 52 kD. It only cross-reacted with cells from SR-RSV-induced sarcoma in hamster, but not with cells from the chicken RSV-induced sarcoma, nor with a number of methylcholanthrene sarcomas and various other tumors of viral or other etiology developed in rats, mouse, hamsters or chickens. The antibody produced by hybridoma clone 5G2 was of subclass IgG2A and recognized an antigen of 28 kD which was located under the plasma membrane, particularly in the cell protrusions and microvilli. Cross-reactions were found with all sarcoma cells tested, indicating that this antigen might represent a common sarcoma antigen of comparatively low molecular mass.
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PMID:Two tumor-associated membrane antigens defined by monoclonal antibodies in a transplantable sarcoma induced by Rous sarcoma virus in rat. 893 54

Many factors involved in the proliferation of myelomas have been reported, and the relationship between these factors and the pathogenesis of multiple myeloma has been discussed. We found that most myeloma cells express Fas antigen/APO-1 (CD95), a cell surface antigen that mediates apoptosis. However only some cells are sensitive to anti-Fas antibody and undergo apoptosis. These data indicate that some multiple myelomas are generated not only by cell proliferation but also by cell immortalization. The mechanism by which myelomas are immortalized is still unclear, but Bcl-2, Bcl-xL, adult T cell leukemia derived factor (ADF), soluble Fas are all candidate factors for this mechanism. The possibility also exists that inducers of apoptosis, e.g. tumor necrosis factor(TNF), interleukin-1 beta-converting enzyme(ICE), Bcl-xS, or Bax, do not have a lethal effect. In this review, we focus on the system that immortalizes myeloma cells, and suggest the possibility that multiple myeloma constitutes one group of cells which cannot undergo apoptosis in the bone marrow.
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PMID:Fas antigen/APO-1 (CD95) expression on myeloma cells. 903 Oct 82


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