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)

This is a communication on the introduction of the first monoclonal marker at Graz University Medical School. Human peripheral blood mononuclear cells were used for immunisation of BALB/c mice by injecting 4,5 X 10(6) cells s. c. Boosting consisted of i.p. injection of 5 X 10(6) cells 4 times in monthly intervals. Spleen cells were taken 4 days after the last boost, fused with NS-1 myeloma cells, using PEG as fusogenic agent. After growth in HAT selective medium, antibody secreting clones were identified by testing the supernatants. Cultures with activity against lymphocytes were closed on normal BALB/C peritoneal cell feeder layers. One of them secreted IgG 1 with strong activity against all lymphoid cells and was named HLy D 1. Further testing showed activity with band cells, polymorphs, eosinophils, macrophages but not with tissue sections from anaplastic undifferentiated cancers and erythroid leukaemias. Since he was named H Le D 1 and introduced for differentiating rare undifferentiated carcinomas from malignant tumors of the lymphoid system.
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PMID:[Cell hybridization: a monoclonal marker as a diagnostic help in haematology and oncology (author's transl)]. 727 18

The concept of antigen-directed cell fusions to increase the yield of hybridomas was investigated. To facilitate cell-cell contact, antigen conjugated cells were used in cell fusion studies. Specifically, fluorescyl conjugated murine myeloma cells (Sp 2/0-Ag14) incubated with murine immune (anti-fluorescyl) splenocytes formed aggregates containing fluorescent and non-fluorescent cells. Fusion of these populations with polyethylene glycol resulted in a greater number of anti-fluorescyl hybridomas relative to normal fusions under non-antigen directed condition. Ligand binding data indicated that despite the multi-cellular aggregates the hybridomas resulting from chemically mediated fusions produced only one monoclonal Ig.
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PMID:Modified hybridoma methodology: antigen-directed chemically mediated cell fusion. 743 26

In this study, B-cells isolated from rheumatoid synovial tissue were immortalized, without prior in vitro stimulation, by means of electric-field induced fusion and conventional PEG fusion in order to compare the efficiency of these methods. Two myeloma cell lines were used as fusion partners, the murine myeloma Ag8 and the murine-human heteromyeloma HAB-1. The results of seven fusion experiments performed simultaneously with identical cell populations showed that fusion frequencies obtained by electrofusion were 4 to 35 times higher than by the PEG fusion technique. The morphological and immunohistochemical evaluation of synovial tissues used for fusion showed that only tissues exhibiting a follicular distribution of B-cells with a high percentage of CD 22-positive lymphocytes gave rise to high fusion yields and produced B-cell clones, whereas synovial tissues with the same percentage of plasma cells but lower percentages of CD 22 lymphocytes yielded very low fusion rates. In conclusion, electrofusion is more efficient for immortalizing small amounts of synovial tissue B-lymphocytes than PEG fusion, since high fusion frequencies could be obtained by this technique without the need for prior in vitro stimulation. Synovial tissue exhibiting a follicular distribution of B-lymphocytes with high percentages of CD 22-positive lymphocytes gave rise to high hybridoma yields and therefore an ideal source of human rheumatoid B-cell clones.
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PMID:Efficient immortalization of rheumatoid synovial tissue B-lymphocytes. A comparison between the techniques of electric field-induced and PEG fusion. 749 50

BALB/c mice were immunized with apolipoprotein (apo AI)--high density lipoprotein (HDL) conjugate. By polyethylene glycol-induced fusion of isolated spleen cells with the myeloma cell line P3 X63 Ag8 6.5.3, three different hybridomas were obtained and characterized. Two of them were found to secrete antibodies of the IgG2a subclass, whereas the third produced antibodies of the IgG1 type. Binding capacities to 125I-apo AI and 125I-HDL were higher than 90% in all cases. The isolated antibodies recognize independent epitopes on the apo AI molecule and bind isolated HDL and serum-HDL with different affinities.
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PMID:Monoclonal antibodies to apolipoprotein AI: generation and characterization. 768 98

There have been no reports of monoclonal antibodies reactive with vesicular monoamine transporters from any source. Western blotting and ELISA data obtained using polyclonal serum from a mouse immunized with a highly purified bovine chromaffin granule monoamine transporter preparation yielded data consistent with the presence of antibodies to the transporter. Hybridomas produced by polyethylene glycol fusion of spleen cells from the mouse with X63/Ag8.653 myeloma cells were screened in an ELISA using partially purified transporter as coating agent. Of the 1142 wells containing colonies, 14 were positive in the initial screen. Hybridomas from wells testing positive were transferred to 24-well plates, grown up, and rescreened. Those still testing positive were subcloned, and the resulting positive wells containing single colonies were grown up and stocked. Of the 6 positive clones that tolerated freeze/thaw (0.5% of the wells tested), 1 was IgG1 kappa, 2 were IgG2a kappa, and 3 were IgG2b kappa isotypes. Ascites fluid was generated in pristane-primed BALB/c mice using hybridomas that had been cloned 2-3 times, and antibodies purified on immobilized Protein A. Immunoreactivity with a mixture of these antibodies, or with only one of them, coincided with dihydrotetrabenazine (TBZOH) binding activity in fractions eluted from all columns employed in the transporter purification. Antibody from at least one of the clones was capable of removing [3H]TBZOH binding activity from a partially purified preparation of transporter. Monoclonal antibodies exhibiting these properties have not been reported previously.
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PMID:Monoclonal antibodies reactive with a monoamine transporter preparation purified from bovine adrenal chromaffin granule membranes. 804 34

Splenocytes from a female, BALB/c mouse immunized with bradykinin conjugated to ovalbumin with toluene diisocyanate were fused with mouse myeloma cells, X63/Ag8.653, using polyethylene glycol. Seventy-nine hybridomas were identified by ELISA to be making kinin reactive antibodies. In preliminary specificity studies it was determined that all of these hybridomas were producing antibodies more reactive with des-Arg9-bradykinin than with bradykinin. ELISAs were developed with the five clones that displayed the highest affinities for des-Arg9-bradykinin. Radioimmunoassays were developed for 3 of these 5 clones as well as with 5 monoclonal antibodies previously described (Odya and Lee 1990). The most sensitive des-Arg9-bradykinin assay developed was a radioimmunoassay in which carboxypeptidase B-treated [Tyr5]-bradykinin was the labeled antigen, clone OLNBK-5 was the antibody, and dextran-coated charcoal was used to separate bound from free radioactivity. The concentration of des-Arg9-bradykinin that inhibited 50% of the radioactive peptide binding was 0.08 +/- 0.03 nM. The relative specificity of this assay (des-Arg9-bradykinin = 100%) was: 29% bradykinin and about 1% with each of the following: lysyl-bradykinin, methionyl-lysyl-bradykinin, des-Arg1-bradykinin and des-Phe8-Arg9-bradykinin.
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PMID:Immunoassays for des-Arg9-bradykinin. 829 67

Splenocytes from mice immunized with homogenous, polyclonal, rabbit kinin antibody (BK21) were fused using polyethylene glycol with the mouse myeloma cell line SP2/o. Eleven monoclonal antibodies, whose binding to BK21 could be inhibited by bradykinin, were obtained from 3 fusions. All of these anti-idiotypic antibodies were of the IgG1k isotype, except for one, which was an IgG2ak. An IgMk, auto-anti-idiotypic antibody, reactive with BK21 was obtained from a fusion of SP2/o cells and splenocytes from a mouse immunized with bradykinin conjugated with carbodiimide to keyhole limpet hemocyanin. Bradykinin could completely inhibit the binding of all of the anti-idiotypic antibodies to BK21 in an enzyme-linked immunosorbent assay. This result is consistent with the anti-idiotypic antibodies being reactive with the ligand binding sites of BK21. It was possible to separate the anti-idiotypic antibodies into 2 groups. The first group, 10 of the 12 antibodies tested, was more sensitive to inhibition by bradykinin than the second group and was not readily inhibited by des-Arg9-bradykinin. The second group was about 7 times more sensitive to inhibition by des-Arg9-bradykinin than by bradykinin. Further experiments will be needed to determine whether or not these monoclonal anti-idiotypic antibodies are "internal image" antibodies.
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PMID:Monoclonal ligand binding site related anti-idiotypic antibodies elicited with a polyclonal kinin antibody. 845 3

We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.
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PMID:Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation. 847 58

L-asparaginase is an enzyme which hydrolyses asparagine. Since the 1960s it has been known that some leukemic cells are deficient in asparagine synthetase and therefore cannot manufacture sufficient quantities of this essential amino acid to maintain cell viability. L-asparaginase is predominantly useful in acute lymphocytic leukemia (ALL) although responses have been noted in patients with acute myeloid leukemia, lymphoma, and rarely other tumors. L-asparaginase has been used in conjunction with methotrexate and ara-C in combination programs in leukemia. The major side-effect limiting the usefulness of L-asparaginase is allergic reactions. In addition, it is probable that neutralizing antibodies develop which shorten the half life of the drug so that the goal of depletion of plasma levels of asparagine cannot be attained or maintained. Polyethylene glycol (M.W. 5000) can be conjugated to L-asparaginase at sites not involving the active site of the enzyme. This enables free access of a small molecule, asparagine, to the active site of the enzyme but prevents uptake by the reticuloendothelial system, greatly decreasing the probability of developing antibodies against the asparaginase and prolongs the circulating half life of the drug. In a phase I/II study conducted at the M.D. Anderson Cancer Center, 37 heavily pretreated patients with refractory hematologic malignancy were treated. The age range from 15 to 73 years, median 49 years. Nineteen patients had ALL, 15 lymphoma, two myeloma, and one Hodgkin's disease. The dose levels of PEG L-asparaginase varied from 250 IU/m2 up to 8000 IU/m2. The pharmacokinetic profile demonstrated a monophasic half life consistent with a one compartment model with a single elimination phase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:L-asparaginase and PEG asparaginase--past, present, and future. 848 65

A large quantity of polyclonal anti-ovalbumin antibodies was obtained from mice by a simple modification of the method described by Kurpisz et al. (1988). In addition, the cells from ascitic fluid were used to produce monoclonal antibodies. Egg ovalbumin hyperimmunized BALB/c mice were injected successively with pristane, antigen and a non-antibody secreting myeloma cell line: the production of ascitic fluid containing antiovalbumin antibody activity was observed after 10-25 days. Cells from ascitic fluid were harvested, washed and fused together with polyethylene glycol to produce monoclonal antibodies. Two fusions were performed and a large number of monoclonal anti-ovalbumin antibodies was obtained. This method is simple, reproducible, allows many fusions to be obtained from one mouse, and allows the use of ascitic B cells rather than the more, frequently used splenic B cells.
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PMID:Mice ascites as a source of polyclonal and monoclonal antibodies. 850 48


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