Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An epitope common to all classes of murine leukemia viruses (MuLVs) was detected by reactivity of MuLVs with a rat monoclonal antibody (MAb) termed 83A25. The antibody is of the immunoglobulin G2a isotype and was derived after fusion of NS-1 myeloma cells with spleen cells from a Fischer rat immunized with a Friend polytropic MuLV. The antibody reacted with nearly all members of the ecotropic, polytropic, xenotropic, and amphotropic classes of MuLVs. Unreactive viruses were limited to the Friend ecotropic MuLV, Rauscher MuLV, and certain recombinant derivatives of Friend ecotropic MuLV. The presence of an epitope common to nearly all MuLVs facilitated a direct quantitative focal immunofluorescence assay for MuLVs, including the amphotropic MuLVs for which no direct assay has been previously available. Previously described MAbs which react with all classes of MuLVs have been limited to those which react with virion core or transmembrane proteins. In contrast, protein immunoblot and immunoprecipitation analyses established that the epitope reactive with MAb 83A25 resides in the envelope glycoproteins of the viruses. Structural comparisons of reactive and nonreactive Friend polytropic viruses localized the epitope near the carboxyl terminus of the glycoprotein. The epitope served as a target for neutralization of all classes of MuLV with MAb 83A25. The efficiency of neutralization varied with different MuLV isolates but did not correlate with MuLV interference groups.
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PMID:A neutralizable epitope common to the envelope glycoproteins of ecotropic, polytropic, xenotropic, and amphotropic murine leukemia viruses. 170 Aug 32

Six monoclonal antibody-producing hybridoma cell lines were generated by fusion of NS-1 myeloma cells with BALB/c immune splenocytes. Monoclonal antibodies (MCA) specific to Machupo virus NP protein were used to study cross-reactivity between pathogenic and nonpathogenic arenaviruses. It was shown that 3140 MCA cross-reacted in IFA with Lassa, Tacaribe, and Tamiami arenaviruses whereas 3101 MCA reacted with Machupo virus alone. It was assumed that these 3101 MCA could be used for differentiation of Machupo virus in IFA.
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PMID:[Monoclonal antibodies to the Machupo virus: their isolation and preliminary characteristics]. 172 22

Peptides corresponding to sequences from the amino-terminal "head" regions of the low, middle, and high molecular weight neurofilament proteins (NF-L, NF-M, and NF-H) were synthesized by a modification of the Merrifield solid-phase method, and a panel of polyclonal antibodies to these epitopes were prepared in rabbits by the injection of synthetic peptides conjugated to the carrier protein keyhole limpet hemocyanin (KLH). An additional, monoclonal antibody recognizing both glial fibrillary acidic protein (GFAP) and vimentin was also produced, by fusion of cells of the mouse myeloma line NS-1 with spleen cells from a mouse immunized with cytoskeletal extracts. Antibody specificities were confirmed by a combination of Western blotting against cytoskeletal extracts and immunofluorescence using both rat brain sections and fibroblasts transfected with fully encoding cDNAs for each neurofilament protein, driven by viral promoters.
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PMID:Characterization of a panel of neurofilament antibodies recognizing N-terminal epitopes. 172 86

A radioimmunoassay (RIA) for the determination of human group-II phospholipase A2 (M-PLA2) has been developed. M-PLA2 was purified from human spleen. Monoclonal antibody (IgG) was prepared by fusion of splenic cells from immunized mice with M-PLA2 and the mouse myeloma cell line NS-1. The RIA was carried out by a single antibody method. The assay is sensitive (0.78 micrograms/l), reproducible and specific. In healthy individuals, the serum M-PLA2 concentration ranges from 1.4 to 4.2 micrograms/l, the average being 2.2 +/- 0.1 micrograms/l (mean +/- SE). Using the RIA, we found increased serum M-PLA2 in patients with various infections and malignant tumors. We also showed the postoperative transient elevation of serum M-PLA2 in cases without any infectious complications. The elevation was independent of the surgical procedure or site. The maximum serum M-PLA2 level was seen on the 2nd to 4th postoperative day. In these patients, the serum M-PLA2 and C-reactive protein levels were significantly correlated. The present study indicated that serum M-PLA2 is an acute phase reactant.
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PMID:Development of a radioimmunoassay for human group-II phospholipase A2 and demonstration of postoperative elevation. 172 81

A monoclonal antibody, M2, was produced by somatic cell hybridisation of splenocytes, from mice immunised with human fetal brain, with the murine myeloma cell line NS-1. Indirect immuno-peroxidase staining of formalin-fixed, paraffin embedded tissue sections showed that, whilst the monoclonal antibody gave a positive reaction with 32/39 astrocytomas from adult patients and 33/36 of children's astrocytomas of the adult histological type, only 17/39 of juvenile astrocytomas were stained. A Chi-squared test showed that the difference in staining between the two groups (adult versus juvenile) was highly significant (p less than 0.0001). In contrast, using a polyclonal antiserum to GFAP, a significantly larger proportion of juvenile astrocytomas than adult astrocytomas stained positively (p less than 0.05). Thus, whereas the distribution of GFAP accorded with the general finding that the degree of malignancy of a tumour correlates with the loss of cell type specific markers, the distribution of M2 reactivity was similar to that of some oncogene products which increase with malignancy. From the flow cytometry data it is apparent that the antigen recognised by M2 is not cell cycle dependent.
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PMID:A monoclonal antibody which discriminates between sub-types of astrocytoma. 174 99

We have immunized Balb/c mice and rabbits with a minute quantity of a 30 kD neuronotrophic factor which was isolated from the extract of newborn rat tectum (Te) by Phast System gel electrophoresis. Splenic cells from the immunized mice were hybridized with NS-1 mouse myeloma cells. Three clones were selected from 576 wells of hybridomas and were capable of secreting monoclonal antibodies specific to the retinal ganglion neuronotrophic factor (RGNTF-MAbs), namely A1, D3 and E8. Subtyping of the three monoclonal antibodies revealed that A1 and D3 are IgG3 and E8 is IgM. They maintained secreting antibodies even after six months of culturing in vitro. In order to determine the specificities of these antibodies, we have used their ascites fluids containing antibodies at a different dilutions to study their effects on the survival of retinal ganglion cells in vitro. The results indicated that at the dilution ranges of 1:250 to 2000, all three monoclonal antibodies exhibited inhibition on the survival of retinal ganglion cells and the inhibition increased with increases in antibody concentrations; especially at a dilution of 1:250, the E8 monoclonal antibody reaching 70% inhibition and A1 and D3 reaching 66% and 62% inhibition, respectively. Polyclonal antibodies from rabbits exhibited similar but weaker results of inhibition. We can conclude that the monoclonal and polyclonal antibodies can specifically inhibit the activity of the 30 kD retinal ganglion neuronotrophic factor.
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PMID:[Characteristics and inhibitory action of monoclonal and polyclonal antibodies against the retinal ganglion neuronotrophic factor (RGNTF)]. 175 66

Three monoclonal antibodies to mycobacterium tuberculosis were produced and designated Ra1, Ra2 and Ra3. The spleen cells of BALB/C mice were immunized with intact, ultrasonicated M. H37Ra and H37Ra culture filtrate and were fused with NS-1 myeloma cells. The monoclonal antibodies were IgG2a, IgM and IgM respectively. The monoclonal antibodies were characterized by ELISA on 14 mycobacterial species. It showed that they reacted with H37Ra and some of mycobacterial species but did not with BCG. McAb Ral was used to prepare immunoabsorbent, and Ag-Ra1 was isolated from unheated H37Ra culture filtrate by affinity chromatography with the absorbent. Ag-Ral was a glycoprotein with MW. of 66 KDa and produced DTH in guinea pigs.
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PMID:[Production and characterization of 3 mcAbs to Mycobacterium tuberculosis]. 180 31

Monoclonal antibodies which bind selectively to cancer cells are currently used for tumor localization and for targeting cytotoxic reagents. The success of these approaches depends on the specificity of the antibody and its reactivity to a majority of the tumor samples. Frequently, monoclonal antibodies are generated by immunizing mice with antigenic preparations from a single tumor cell line. Antibodies generated under these conditions often react to a narrow range of tumors. In the present study, mice were immunized with multiple ovarian cancer cell lines in a sequential manner to amplify the immune response against common antigenic determinants expressed in these cell lines. Spleen cells from the immunized mice were then fused with NS-1 myeloma cells to establish hybridomas. Two cell lines were selected on the basis of their selective reactivity to ovarian cancer cells after extensive screening. Monoclonal antibodies OVX1 and OVX2 bound to all 5 ovarian carcinoma cell lines tested and did not bind to normal fibroblast cells. These antibodies recognized a unique antigenic determinant present in ovarian and breast cancer cells. Cross-blocking studies showed that the binding of OVX1 and OVX2 is not displaceable by 10 other previously described anti-ovarian antibodies including OC125. In immunocytochemical studies, OVX1 reacted to a majority of ovarian cancer tissues (17 of 20) and did not bind to normal ovarian tissues. Preliminary results indicate that OVX1 and OVX2 antibodies are directed to a high molecular weight antigen. These antibodies could be used in the preparation of cytotoxic conjugates.
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PMID:Development of two new monoclonal antibodies reactive to a surface antigen present on human ovarian epithelial cancer cells. 185 17

BALB/C mice were immunized with a partially purified M-protein fraction prepared from hot acid-extracts of a type 4, group A streptococcus, strain SS91. Two samples of monoclonal antibodies (MAb) were obtained from hybridoma cells of antibody producing spleen cells fused with NS-1 myeloma cells. Both MAb were of the subclass IgG1 having kappa-type light chains. The MAb agglutinated trypsin-digested cells of type 4 strains, but not of types 1, 2, 18, 28 and 41. This type 4-cell agglutination was inhibited by extracts of type 4 cells; strongly by hot acid-extract and partially by trypsin-extract. Hot acid-extract of type 41 cells had no inhibitory effect. Sandwich-enzyme-linked immunosorbent assay of the MAb and partially purified M-protein preparation combination against commercial T-typing sera showed that only T-type 4 antiserum reacted with the combination system. From these data, we thought that the MAb preparations were not directed to M-protein but to T-protein of type 4, group A streptococci.
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PMID:[Preparation of monoclonal antibodies agglutinating group A, type 4 streptococci]. 191 24

Monoclonal antibodies were raised against Leishmania (Viannia) naiffi, which recently has been characterized as a new species. BALB/c mice were immunized with membrane-enriched fractions of a mixture of L. (V.) naiffi isolates. Subsequent fusion of immunized splenocytes with NS-1 myeloma cells resulted in the production of 5 Mabs (N1-N5). Screening by ELISA and indirect immunofluorescence against an extensive cross-panel of Leishmania strains revealed that N3 was species-specific and could thus be used to identify L. (V.) naiffi. N2 and N5 reacted only with strains of L. (V.) naiffi and Leishmania (Viannia) braziliensis, and therefore could be used in conjunction with N3 to identify L. (V.) braziliensis parasites. These species-specific Mabs will therefore be useful additions to the panel of antibodies already available for the identification of Leishmania species. N1 and N4 were found to recognize a small, glycosylated molecule present on all L. (V.) naiffi and L. (V.) braziliensis isolates that is related to the GIPL family of membrane glycophospholipids previously described for Leishmania (Leishmania) major.
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PMID:Monoclonal antibodies that react with Leishmania (Viannia) naiffi. 191 13


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