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)

Isolated variable region light chain 315 (VL-315), the VL domain of a myeloma protein of BALB/c origin, induces T cells of BALB/c (H-2d) mice that help the adoptive secondary anti-4-hydroxy-3-iodo-5-nitrophenylacetyl (NIP) antibody response to NIP-Fab315. The location of the epitope recognized by helper cells was examined with two fragments of VL-315, obtained by cleavage with cyanogen bromide at Met 87. Both N-terminal fragment 1-86 and C-terminal fragment 88-114/117 elicited BALB/c antibodies that bound to the respective fragments and to VL-315. By contrast, only fragment 88-114/117, which consists of the third hypervariable region, J region, and 5-7 amino acids of the C region, induced helper cells that augmented the anti-NIP response to NIP-Fab 315.
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PMID:T helper cells recognize an idiotope located on peptide 88-114/117 of the light chain variable domain of an isologous myeloma protein (315). 622 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

Hybridomas were prepared by fusion of mouse myeloma cell line Sp2/0 with lymphocytes from mice immunized with avian myeloblastosis virus (AMV). The specificity of each monoclonal antibody was characterized by radioimmunoassay (RIA) using purified viral core proteins, immunoprecipitation of radioactively labeled virus (35S-methionine-labeled AMV, 125J-labeled AMV) and immunoblotting. One monoclonal antibody (IC11) which is of IgG1 subclass, and two other monoclonal antibodies (IF9 and IB8), both of IgG3 subclass, were directed against the p19 protein of AMV. The remaining eight monoclonal antibodies (most of them of IgM class) did not precipitate viral proteins under the experimental conditions used, except IIG12 hybridoma antibody which irregularly precipitated glycoprotein gp85. Since most of them (seven, including IIG12) gave positive reactions in RIA with antigenically unrelated influenza virus, these monoclonal antibodies were directed against virus components specified by chick cells (host cell antigen).
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PMID:Production and characterization of monoclonal antibodies against avian myeloblastosis virus. 631 35

The capacity of Plasmodia to synthesize sialic acids was investigated by adding radioactive acetate to short-term in vitro cultures of the intraerythrocytic asexual forms of three malaria parasites (the human malaria Plasmodium falciparum in Aotus trivirgatus erythrocytes; the simian malaria P. knowlesi in rhesus monkey erythrocytes; the rodent malaria P. berghei in mouse erythrocytes) and to cultures of extracellular zygotes of the avian malaria P. gallinaceum. Radioactive acetate was added to normal rhesus monkey erythrocytes and to cells of the murine myeloma NS-1 for comparison. Although [1-14C]-acetate labeled many proteins with each malaria parasite and the NS-1 cells, analysis of purified sialic acids revealed that only with the NS-1 cells was radioactivity incorporated into sialic acids. Furthermore, N-acetyl[6-3H]mannosamine was not incorporated into sialic acids or malarial glycoproteins when added to P. knowlesi cultures. All of the malaria parasites underwent growth or differentiation during these experiments as measured by [35S]methionine uptake into protein and by light microscopy. Extracellular parasites largely free of erythrocyte membranes were prepared to determine whether Plasmodia contain sialic acids that are not labeled by exogenous precursors. Purified merozoites of P. knowlesi and zygotes of P. gallinaceum did not contain detectable amounts of sialic acids on chemical analysis. Thus, although we could show that Plasmodia can incorporate radioactive sugars such as glucosamine, galactose and mannose into proteins, presumably glycoproteins, they do not synthesize sialic acids or sialo-glycoproteins, nor do they contain sialo-glycoconjugates of host origin.
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PMID:Malaria parasites do not contain or synthesize sialic acids. 637 Aug 20

The authors established the amino acid substitutions determining G3m(s) and G3m(t) specificities, which characterize Mongoloid populations, by sequence analysis of the Fc region of a myeloma protein (Jir). By comparing the amino acid sequences of the IgG3 (Jir) and the other IgG subclasses analyzed to date, it was found that G3m(s) was an isoallotype specified by an amino acid substitution at position 435; i.e., whereas the subclasses IgG1, IgG2, and IgG4 had histidine in common, G3m(s-) had arginine in this position. This was also confirmed by the observation that the Fc fragment in question bound to protein A. It was also established that the amino acid at position 379 of G3m(t-) IgG3 and the other subclasses was valine, whereas methionine in this position was specific for G3m(t+). In addition, the amino acids at position 339 of G3m(u-) IgG3 Jir was threonine, and at position 296 of G3m(g-) IgG3 Jir was tyrosine. These findings are not in accord with the hitherto postulated relations of alanine and phenylalanine to G3m(u-) and G3m(g-), respectively. Finally, this study showed that a large number of substitutions occurred at positions 384 through 389, which suggests that many specificities of the G3m(b) group occur on IgG3 proteins.
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PMID:Structural studies of a human gamma 3 myeloma protein (Jir) bearing the allotypic marker Gm(st). 641 81

Monoclonal antibodies against murine immune interferon (IFN-gamma) were produced by fusing the murine nonsecreting myeloma cell line P3.X63.Ag8.653 with spleen cells from rats immunized with IFN-gamma-containing supernatants obtained by stimulating a T-cell lymphoma, L12-R4, with phorbol 12-myristate 13-acetate. Supernatants from a twice-cloned hybridoma (AN-18.17.24) were found to neutralize and to adsorb in depletion experiments up to 27 units of mouse IFN-gamma but not equivalent amounts of mouse leukocyte or fibroblast IFNs. The AN-18.17.24 monoclonal antibody neutralized to the same extent mouse IFN-gamma from different sources--namely, (i) concanavalin A-stimulated spleen cells, (ii) alloantigen-stimulated spleen cells, and (iii) monkey fibroblasts transfected with the cloned gene of murine IFN-gamma. Moreover, the monoclonal antibody displayed species specificity, since it did not neutralize IFN-gamma of human origin. Binding inhibition experiments with murine IFN-gamma preparations exposed to enzymatic or physicochemical degradation demonstrated that the protein moiety and not the carbohydrate residues were responsible for the binding to the AN-18.17.24 monoclonal antibody. Finally, this monoclonal antibody immunoprecipitated two molecular species of IFN-gamma of about 16.8 and 17.8 kilodaltons, respectively, from [35S]methionine- or [3H]glucosamine-labeled supernatants of stimulated L12-R4 cells.
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PMID:Monoclonal antibodies against murine gamma interferon. 643 8

Monoclonal antibody HBCA-12 obtained by hybridoma procedure after immunization with human mammary adenocarcinoma cell line MDA-MB-231 immunoprecipitated a cell surface sialoglycoprotein gp80 (apparent molecular weight 80 000) from MDA-MB-231 cells and a glycoprotein gp78 from human myeloma cell line ARH 77. A protein of a similar electrophoretic mobility was immunoprecipitated also from 35S-methionine metabolically radiolabeled human melanoma cell line VUP 1. The expression of the antigen recognized by HBCA-12 monoclonal antibody could be detected neither on PHA-induced nor on EBV-transformed peripheral blood mononuclear cells from healthy donors.
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PMID:Biochemical and histochemical characteristics of target antigen detected by monoclonal antibody HBCA-12 against a membrane component of human mammary carcinoma cell line. 652 96

Antibodies to molybdate-stabilized chicken oviduct progesterone receptor were raised in a Wistar rat and detected by interaction with homogeneous radioiodinated progesterone receptor. Spleen cells of this rat were then fused with mouse Sp2/0-Ag14 myeloma cells and the antibodies produced by the hybrid cells were detected by double immunoprecipitation using the 125I-labeled receptor. Cells of one of the positive cultures were then cloned by limiting dilution and one hybridoma cell line was studied. The monoclonal antibody produced was an IgG2b, and it reacted with the molybdate-stabilized "8-9S" form of the chicken oviduct progesterone receptor, labeled with either [3H]progesterone or [3H]ORG 2058 (a high-affinity synthetic progestin). Kd for the 8-9S progesterone receptor was approximately equal to 1 nM. Progesterone receptor-monoclonal antibody complexes were labeled with radioactive progesterone, suggesting that antibody does not prevent hormone binding. By using a [35S]methionine-labeled antibody, we were able to detect the progesterone receptor independently of its characteristic function of binding radioactive hormone. No crossreaction with human progesterone receptor was detected.
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PMID:Monoclonal antibody to chicken oviduct progesterone receptor. 657 54

To investigate the role of the leader peptide in modulating secretion from living cells, we injected a synthetic peptide into Xenopus oocytes. The peptide consisted of the NH2-terminal leader sequence of mouse immunoglobulin light chain precursor. We found that the leader peptide has two different roles in regulating secretion from the oocytes. First, it competitively inhibits the synthesis of secretory and membrane proteins but not of cytoplasmic proteins. The inhibition occurs both with oocyte proteins and with proteins directed by coinjected myeloma mRNA. The inhibition reaches a maximum 2 hr after injection and decays within 3 hr. It appears to be mediated through the cell membrane, because 125I-labeled leader peptide segregates into the membrane fraction of microinjected oocytes simultaneously with the interference with methionine incorporation. A second role of the microinjected leader peptide is to induce a rapid acceleration in the rate of export of secretory proteins from the oocyte. The maximal enhancement effect is obtained upon injection of 50 ng of leader peptide per oocyte. It is not merely due to the small size, negative charge, or hydrophobicity of the peptide, because enhanced secretion does not occur when glucagon, poly-L-glutamic acid, or Triton X-100 is injected. Furthermore, immunoreaction of the peptide with specific antibodies prior to microinjection prevents the accelerated export. Our observations indicate that in Xenopus oocytes, the leader peptide is involved in both translocation and later step(s) in the secretory pathway.
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PMID:Synthetic leader peptide modulates secretion of proteins from microinjected Xenopus oocytes. 658 Jun 39

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


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