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)

Hybridomas secreting monoclonal antibodies with haemagglutination-inhibition (HI) activity to the Skalica strain of tick-borne encephalitis (TBE) complex were prepared by the fusion of P3-NS1-Ag4-1 myeloma cell line with spleen cells of BALB/c mice immunized with the purified Skalica strain. The highest titres of monoclonal antibodies obtained from the hybridomas S-9, S-15 and S-16 ranged from 512 to 10,240, respectively; the ascitic fluid contained as many as 4.6 mg/ml of monoclonal antibodies. Its analysis by Ouchterlony's double immunodiffusion, agarose electrophoresis, and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed the presence of monoclonal antibodies with mu isotype of the heavy and kappa isotype of the light chain. The specificity of the monoclonal antibodies was proved using 11 different antigens from family Togaviridae in the HI test.
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PMID:Production of monoclonal antibodies with haemagglutination-inhibition activity to the Skalica strain from the tick-borne encephalitis complex. 613 29

Hybridomas secreting monoclonal antibodies directed against intact colonization factor antigen I pili have been produced by the fusion of spleen cells from immunized BALB/c mice with NS1/SP2 myeloma cells. The four monoclones with the highest antibody titer, as detected by enzyme-linked immunosorbant assay (ELISA), were chosen for antibody amplification by production of mouse ascitic fluid. These four were examined for antibody specificity by ELISA and immunoblot assays, using six different pilus types. Three of the four monoclonal isolates were specific for only colonization factor antigen I pili in both assays, whereas the remaining isolate showed a distinct cross-reactivity with K99 pili in the ELISA assay but not in immunoblot analysis. These results indicate that this monoclone may be recognizing a common structural element between the two adhesive pilus types.
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PMID:Monoclonal antibodies against colonization factor antigen I pili from enterotoxigenic Escherichia coli. 613 63

We have isolated three clones of hybrid cells which synthesize antibodies specific for determinants on simian virus 40 (SV40) T antigens. Mouse myeloma NS1 cells were fused with spleen cells from mice that had been immunized with SV40-transformed mouse cells. Hybrid cells were selected in HAT medium and cloned in soft agar. We used an enzyme-linked immunosorbent assay for detection and quantification of mouse antibodies against SV40 T antigens. Monoclonal antibodies from 3 of the 24 clones that scored as positive in the enzyme-linked immunosorbent assay were verified by immunoprecipitation to be specific for SV40 T antigens. Two clones (7 and 412) produced antibodies that recognized denaturation-sensitive antigenic determinants unique to large T antigen. Antibodies from clone 7 appeared to have a low affinity for large T antigen. Antibodies from clone 412 had a higher affinity for large T antigen but did not recognize a subclass of large T antigen that was recognized by tumor serum. Antibodies of the third clone, clone 122, recognized a denaturation-stable antigenic determinant of the 53,000-dalton mouse nonviral T antigen in SV40-transformed cells. Antibodies from clone 122 also recognized similar (51,000- to 56,000-dalton) nonviral T antigens in SV40-transormed or lytically infected cells from five mammalian species and in four uninfected mouse lines. From these observations, we have concluded that (i) the 94,000-dalton SV40 large T antigen may exist as immunologically distinguishable subclasses, and (ii) the nonviral T antigens of five mammalian species share at least one antigenic determinant.
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PMID:Monoclonal antibodies against simian virus 40 T antigens: evidence for distinct sublcasses of large T antigen and for similarities among nonviral T antigens. 615 77

Hybrid cell lines have been derived from a fusion between mouse myeloma cells, NS1, and spleen cells from mice immunized with freshly resected osteosarcoma cells from an untreated patient. Of the 276 hybrids obtained, five secreted antibodies which bound to osteosarcoma tissues but not to autologous skin fibroblasts. The antibodies from three of these five hybrids, OST6, OST7, and OST15, reacted with all of five osteosarcoma tissues and with one chondrosarcoma tissue but not with other malignant or benign tumors. Tests of various normal tissues were negative, except for weak binding to a subpopulation of chondrocytes in articular cartilage. The reciprocal binding inhibition test showed that OST6, OST7, and OST15 antibodies were directed against different antigenic determinants.
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PMID:Detection of human osteosarcoma-associated antigen(s) by monoclonal antibodies. 617 16

Three monoclonal antibodies reactive with a purified extractable Mr 34,000 prostate antigen (PA) have been prepared by fusing splenocytes of BALB/c mice preimmunized with purified PA with the NS1 mouse myeloma cell line. The three antibodies were all of the IgG-1 subclass. The antibodies defined two noncross-blocking unique determinants on PA; each present as one site per molecule. IF3 defined one antigenic site and 2G7 and 1C5 defined another antigenic determinant. All of the antibodies reacted with PA in a solid-phase radioimmunoassay and immunoprecipitated 125I-labeled PA. Absorption and sandwich radioimmunoassays showed PA in prostate tissues but not in tonsil, liver, or kidney. Immunoperoxidase staining of formalin-fixed paraffin-embedded sections of benign prostatic hyperplasia and prostatic carcinoma revealed strong prostate epithelial reactivity. None of the antibodies showed reactivity with prostate membrane preparations. A sandwich radioimmunoassay used 2G7 as a plate coat. 125I-labeled 1F3 was used to detect 5 ng PA per ml in sera of patients with prostate cancer. These results confirm previous observations regarding the specificity of PA and shed new evidence for its intracellular localization.
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PMID:Monoclonal antibodies to a human prostate antigen. 617 8

In the present paper we describe the production and characterization of a monoclonal antibody (Mab) recognizing HLA-Aw32 + A25 antigens. NS1 murine myeloma cells were fused with splenocytes from a BALB/c mouse immunized with normal human peripheral blood (PB) lymphocytes of phenotype A1, Aw32; B7,B37,Cw-,Cw-;DR2,DRw10. Supernatants were first screened against Cr51-labeled immunizing cells by complement dependent cytotoxicity 51Cr-CDC). Cultures identified as producing cytotoxic antibodies were subcultured and the supernatants tested against a selected panel of HLA typed cells by the NIH microcytotoxicity method. One culture producing antibody reacting with an HLA polymorphism was detected. This hybrid, designated CATA 1, was cloned twice by limiting dilution and obtained in ascitic form. Specificity of CATA 1 Mab was evaluated against a panel of 120 PB T cells from normal donors. CATA 1 reacted with cells bearing HLA-A25 or HLA-Aw32 antigens. In addition, a reaction was observed with a cell of phenotype A2,Aw31; B17,Bw49. Isoelectric focusing revealed the monoclonal nature of CATA 1, with immunofixation identifying it as an IgG molecule. Absorption studies have demonstrated that CATA 1 recognizes a common determinant on HLA-A25 and HLA-Aw32. The finding that this Mab recognizes the same CREG as alloantisera against HLA-Aw32 suggests that this antigen has no unique epitopes.
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PMID:Monoclonal antibody against HLA-Aw32 + A25. Is HLA-Aw32 an allele with no unique antigenic determinant? 618 19

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

Our previous work using rabbit antibodies to the variable region of MOPC315 myeloma heavy chain (VH) has indicated the existence of framework determinant(s) common to many murine heavy chains. Here we report the characterization of anti-VH monoclonal antibodies (mAb) prepared in an attempt to elucidate the nature of the common VH determinant. We immunized AKR/J mice with a purified VH315 fragment and generated somatic cell hybrids by the fusion of the immune AKR/J splenocytes with the NS1 myeloma cells. Thirty-seven common anti-VH and 57 subgroup VHI-specific hybridomas have been established and characterized. Whereas the anti-subgroup mAb seemed to react with a determinant unique to the MOPC315 (mouse VHI) subgroup, all the anti-VH mAb reacted with myeloma heavy chains of different VH subgroups, class and allotypes. Antibody competition studies revealed that the VH subgroup determinants are distinct from the common VH determinants and that both were also recognized by the rabbit polyclonal antibodies. The common VH determinants were found to be "hidden" determinants on intact immunoglobulin molecules being exposed only on isolated heavy chains. Furthermore, they are sequential determinants since they are preserved on fully denatured heavy chains. The common VH determinants are shared by immunoglobulins of a wide range of vertebrates from amphibia to man and thus represent antigenic structures which were highly conserved throughout evolution.
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PMID:Monoclonal anti-VH antibodies recognize a common VH determinant expressed on immunoglobulin heavy chains from various species. 619 96

A monoclonal antibody against keratins (KL1) from normal human stratum corneum was obtained using hybridoma techniques. Spleen cells from immunized BALB/c mice were fused with NS1, a mouse myeloma cell line, to produce hybrids. Antibody activity to epidermal keratins was tested using an indirect immunofluorescence test on cryostat sections of human epidermis and rabbit lip. A stable clone producing antikeratin antibody was isolated and an ascitic fluid was produced and used as a source of antibody (IgG1 kappa). KL1 was characterized by its immunohistochemical staining of various epithelia and by its recognition of 55-57 kilodalton (kd) keratin polypeptide from normal epidermis using the immunoblot technique. Frozen and deparaffinized sections of normal human epidermis, mucosa, and esophagus were stained by this antibody only in the upper cell layers as demonstrated by both indirect immunofluorescence and immunoperoxidase techniques. Approximatively 80% of normal keratinocytes isolated after trypsinization were labeled by KL1 whereas most negative cells showed basement membrane zone antigens. This confirmed differences in the expression of medium-sized polypeptides between basal and supra-basal cells during the course of human epidermal differentiation. All epithelial cells from other human epithelia (thymus, thyroid, bronchial mucosa, stomach, intestines) were positive with KL1 whereas nonepithelial cells and tissues did not show any staining. In view of these results KL1 promises to be a useful tool in the exploration of human epithelial differentiation.
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PMID:Reactivity pattern of a monoclonal antikeratin antibody (KL1). 619 31

Ten monoclonal antibodies (TN 1-TN 10) directed against different renal antigens of distinct sites of the human nephron were derived from a fusion between P3-NS1/1-Ag4-1 mouse myeloma and spleen cells of a mouse hyperimmunized against isolated human kidney cells. Two of these reagents (TN 1, TN 10) were shown by immunoperoxidase labelling on frozen sections of five normal kidneys and of other selected human organs, as well as by immunofluorescence studies on normal peripheral blood cells and selected lymphohematopoietic cell lines, to detect antigens exclusively expressed on visceral glomerular or proximal tubular epithelial cells. The other eight antibodies were found to react with different determinants shared between renal structures, muscle cells, different epithelia, B-lymphocytes and granulocytes. In heterogeneous cultures of isolated kidney cells these monoclonal reagents could be used to identify distinct cell types of tubular origin. Thus such hybridoma-derived antibodies provide new tools to correlate structural characteristics of various renal epithelial cells with their functional properties and will contribute to the study of their influence on immunologically mediated kidney injuries in different forms of glomerulonephritis in man.
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PMID:Characterisation of renal antigens on distinct parts of the human nephron by monoclonal antibodies. 619 94


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