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)

Immunoglobulin kappa-chain mRNA was hybridized with DNA in order to assess the kappa-gene frequency. Kappa-mRNA was purified from membrane-bound ribosomes of mouse myeloma MOPC-41 by poly (U) chromatography and isolation of a 13S RNA by successive sucrose density gradient centrifugations. The RNA coded for kappa-chain precursor molecules in cell-free protein synthesis and essentially no other proteins. MOPC-41 kappa-mRNA hybridized with MOPC-41, MPC-11, and Krebs DNA with the same kinetics: the majority of the hybrids was formed with rare or unique DNA sequences (Cot/2 450 to 900), a small portion with highly repetitive sequences (Cot/2 5--6). The slow hybrids were well matched and the rapid hybrids were mismatched by about 4%, regardless of the DNA used. It was further investigated whether the rapid hybrids contained translatable kappa-mRNA or were due to impurities in the RNA preparations. Kappa-mRNA and globin-mRNA (as an internal standard for a unique transcript) were hybridized with DNA to Cot 20 or 48, the hybridized and unhybridized RNA were isolated by hydroxyopatite-urea chromatography and, after removal of the DNA, translated in a cell-free system. The cell-free products were analyzed by SDS-polyacrylamide gel electrophoresis and immunoprecipitation. It was found that approximately equal quantities of translatable kappa- and globin-mRNA were hybridized maximally 1.7%). The results do not support the hypothesis that kappa-mRNA is a transcript of both repetitive and unique DNA sequences.
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PMID:Analysis of immunoglobulin genes: DNA/RNA hybridization with immunoglobulin kappa-chain mRNA and isolation and translation of hybridized RNA. 81 83

An analysis of red cell membrane proteins in acute and chronic lymphatic leukaemia, Hodgkin's disease, lymphosarcoma, and myeloma was carried out. The electrophoretic pattern after solubilisation in urea or SDS was examined, along with migration on cellulose acetate or acrylamide in different buffers. Protein acid, basic and neutral amino acid percentages were also determined. An increase in low molecular weight and faster anodic migration proteins was noted in the lymphoblastoses, whereas the amino acid spectrum of these proteins showed percent changes in the case of some amino acids, particularly glutamic acid, phosphoserine, lysine and histidine. The alterations observed were compared with those noted previously in other haemoblastoses, congenital haemolytic and anhaemolytic blood diseases, and endoglobular or acquired metabolic defects in a closer assessment of their significance.
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PMID:[Changes in membrane proteins in the erythrocytes of patients with hemolymphoblastosis not directly involving the erythroblastic line]. 106 86

The proteins precipitated with ammonium sulfate from the urine of a patient (Mat) with multiple myeloma were separated into three components by ion-exchange and gel chromatographies. Sodium dodecyl sulfate polyacrylamide gel electrophoresis, amino acid analyses, immunochemical tests, and measurement of circular dichroism showed that these components were a dimer with a disulfide bond, a stable monomer, and a variable fragment, respectively. All three protein components reacted with 5,5'-dithiobis-(2-nitrobenzoic acid) in Tris-HCl buffer at pH 8.0, indicating that they contained free sulhydryl groups. Partial reduction with dithiothreitol in the absence of denaturants yielded two SH groups per molecule from both the monomer and the dimer, and one SH group per molecule from the fragment. This indicates that the monomer of Mat protein contains a cysteinyl residue in the variable region in addition to a cysteinyl residue at the COOH terminus. The reactivities of the two SH groups of the partially reduced monomer toward iodoacetamide and iodoacetic acid were studied by polyacrylamide gel electrophoresis. The two SH groups had similar reactivities with iodacetamide, but the SH group at the COOH terminus was more reactive with iodoacetic acid than that in the variable region. The extrinsic Cotton effects of an azobenzene-2-sulfenyl group introduced into the SH group in the variable region were different from those of dye attached to the COOH terminal SH group, indicating that the two SH groups had different environments. The states of the SH groups of the intact monomer are discussed on the basis of these findings.
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PMID:A type kappa Bence Jones protein containing a cysteinyl residue in the variable region. 115 Jun 31

Campylobacter rectus is one of the predominant bacteria in the lesions of human periodontitis. The surface antigens of the bacterium contain several components which may play significant roles in colonization and pathogenesis. A high-molecular-weight protein was selectively isolated from the cell surface of C. rectus by acid extraction and purified by DEAE Sepharose. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that the extracted protein was 150 kDa. The protein was not found in Campylobacter curvus ATCC 35224 or Wolinella succinogenes ATCC 29543. Lipopolysaccharide (LPS) was extracted from various C. rectus strains by the hot phenol-water method. SDS-PAGE patterns revealed that C. rectus LPS was the smooth type in nature. Monoclonal antibodies against C. rectus were generated by the fusion of SP2/0 myeloma cells with splenocytes from BALB/c mice immunized with whole cells of C. rectus ATCC 33238 strain. An Immunoglobulin G1 monoclonal antibody reacted with the high-molecular-weight proteins from 4 of 9 C. rectus strains, indicating that the 150 kDa protein exhibits antigenic heterogeneity. Immunoelectron microscopic study revealed that the monoclonal antibody recognized the S-layer of C. rectus cells. An IgM monoclonal antibody reacted with LPSs from C. rectus strains at molecular weights between approximately 20.0 kDa and 24.0 kDa. The monoclonal antibody did not react with any other LPSs from C. curvus ATCC 35224 or W. succinogenes ATCC 29543. The reactivities of this monoclonal antibody indicate that it recognizes an O-specific side chain epitope of C. rectus LPS. Sera from patients with adult periodontitis showed strong reactivity with the 150 kDa protein antigen and LPS from C. rectus strains. As determined by immunoblotting analysis, sera from periodontally healthy individuals, however, showed little or no reactivity. The levels of serum IgG antibodies of patients with periodontitis to the protein antigen and LPS were statistically significantly higher than those of periodontally healthy individuals, as assessed by an enzyme-linked immunosorbent assay.
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PMID:Analysis of cell surface antigens of Campylobacter rectus. 130 24

Monoclonal antibodies (McAb) of hybridomas derived from the fusing of the mouse splenocytes immunized by TuMV with BALB/c mouse myeloma cells (SP2/0-Ag14). Five kinds of hybridoma cell line were produced by indirect-ELISA screening and cloning three times with limiting dilution. Four kinds of hybridoma produced antibodies respectively reactive to TuMV C1, C3, C4 and C5. One kind was reactive to all five strains of TuMV. In indirect-ELISA and sandwich-ELISA tests, TuMV specific monoclonal antibodies did not react with CaMV, CMV, TMV, PVX, and PVY. Antibody titers of ascitic fluids were about 1:256,000 to 2,048,000 in indirect-ELISA. The biological, physical, and chemical properties of the hybridoma cell lines and McAb were identified. The identification of TuMV strains, the specificity and stability of McAb, the coat proteins, and the antigenic site of TuMV were discussed and analyzed with SDS-PAGE and western-blotting.
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PMID:Establishment of hybridoma cell line secreting specific monoclonal antibodies against turnip mosaic virus and analysis of properties of the McAb. 134 28

Protective human monoclonal antibodies (HuMAbs) are superior to hyperimmune sera and murine monoclonal antibodies as far as human immunotherapy is concerned. In this report, we describe the successful generation of triomas secreting HuMAbs to tetanus toxin (tt). Lymphoblastoid cell lines secreting anti-tt antibodies were stabilized by back-fusion with a mouse x human heterohybrid myeloma partner, SBC-H20. One of the antibodies so produced, confers total protection of mice from tetanus, unlike a few recent reports where only partial protection (delay in the onset of tetanus) was achieved with single HuMAbs. Experiments to localize the neutralizing epitope(s) of the toxin using the protective monoclonal antibodies revealed that the antibody recognizes a conformational determinant that is destroyed on SDS-treatment. Preliminary studies show that Fab preparations of the protective antibody are capable of neutralizing tetanus toxin, suggesting that it might be possible to clone and express the Fab in a stable vector for large scale production.
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PMID:A single human monoclonal antibody that confers total protection from tetanus. 137 15

Rats were immunized with guinea pig T lymphocytes and the spleen cells were fused with cells of a mouse myeloma line. The resulting hybrids were screened for the production of antibodies selectively reacting with guinea pig T cells. The monoclonal antibody (MoAb) H159 was analysed in detail because it bound to T lymphocytes, but not to B lymphocytes or macrophages. Cellular ELISA, cytofluorometry and immunohistology revealed that the antigen detected by H159 is selectively expressed on the majority of peripheral mature T lymphocytes (about 95%). In contrast, it stained only a minor population of thymocytes in FACS analysis. H159 precipitated from NP40 lysate of T cells a protein with a molecular weight of about 90 kDa when separated under non-reducing conditions in SDS-PAGE. Under reducing conditions bands with molecular weights of about 50 kDa were found. After binding to anti-rat Ig coated beads, the MoAb H159 had a mitogenic effect for guinea pig T lymphocytes whereas soluble MoAb H159 in the presence or absence of macrophages was not mitogenic. The cellular expression and molecular characteristics of the H159 antigen together with the mitogenic activity of the antibody for T cells indicate that the MoAb H159 recognizes the guinea pig T-cell receptor for antigen via a constant region determinant.
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PMID:Analysis of mature guinea pig T cells with a monoclonal antibody directed against a framework determinant of the T-cell receptor for antigen. 138 15

Antibody raised in mice was used in attempting to identify proteins responsible for the conductive chloride transport that can be measured in porcine ileal brush border membrane vesicles. Ileal brush-border membrane vesicle protein from pig was separated into five different molecular mass fractions by preparative SDS polyacrylamide disc gel electrophoresis. Separated protein fractions were used to immunize mice. Antibody was screened for reactivity with antigen by Western blotting, and for effects on conductive chloride transport in ileal brush border membrane vesicles. Immunization with brush-border protein from fraction I proteins (> 110 kDa) produced polyclonal antisera which specifically inhibited the conductive component of chloride uptake by ileal brush border vesicle preparations. Western blotting of the antigen showed the presence of several protein species of molecular mass > 100 kDa that were recognized by immune serum. Spleen cells from a mouse producing antiserum that inhibited conductive chloride transport were fused with a myeloma cell line. The resulting hybridoma colonies produced antibody that reacted with at least seven distinct protein bands by Western blot assay and inhibited chloride conductance in brush-border membrane vesicles.
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PMID:Inhibition of ileal brush-border chloride conductance by specific antibody. 143 82

We previously described a novel 68,000 D macrophage-derived protein (MMS-68) that can stimulate mucus-like glycoconjugate (MLGC) secretion from cultured human airways, respiratory epithelial cells, and the ishikawa adenocarcinoma cell line. To better characterize this mucus secretagogue, we generated monoclonal antibodies against MMS-68 by injecting crushed SDS-PAGE gel slices containing this protein into Balb-C mice followed by fusion with SP2/0, a nonsecreting mouse myeloma cell line. A panel of monoclonal antibodies was produced that identified the 68,000 D MMS by immunoblot analysis and immunoprecipitation. The monoclonal antibodies detected MMS-68 in normal peripheral blood monocytes and pulmonary macrophages by cytofluorographic analysis and in human airways as determined by immunohistochemistry. Utilizing the monoclonal antibodies, an antigen-capture ELISA assay was developed. Statistically significant elevations in levels of MMS-68 were detected in bronchoalveolar lavage fluid (BALF) of chronic bronchitic subjects and cigarette smokers and in monocyte culture supernatants from steroid-dependent asthmatic patients compared to normal control subjects. The 68,000 D MMS is a potent secretagogue and may play an important role in the regulation of mucus secretion, especially in chronic bronchitis and steroid-dependent asthma.
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PMID:In vivo detection of a novel macrophage-derived protein involved in the regulation of mucus-like glycoconjugate secretion. 145 80

Soluble interleukin-6 receptor (sIL-6R) was found to be spontaneously released from human myeloma cell line U266 cells into culture supernatant, and was quantitatively measured with a fluorescence sandwich enzyme-linked immunosorbent assay employing antibodies specific to IL-6R. The supernatant IL-6R was generated only from IL-6R-positive cell lines; myeloma cell lines RPMI8226 and PRMI1788, and myelomonocytic cell lines U937, THP-1, and HL-60. In contrast, it was not released from the IL-6R-negative cells; T cell line Molt-4 and Burkitt lymphoma cell line Raji. SDS-PAGE analysis of the soluble IL-6R from U266 cells suggested a molecular weight of approximately 50-55 kDa, 25-30 kDa smaller than the mature cell surface receptor. These results suggest that the generation of soluble IL-6R may be a maker of myeloma cells and myelomonocytic cells.
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PMID:Soluble interleukin-6 receptor is released from receptor-bearing cell lines in vitro. 150 71


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