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)

Cloned hybrid cells, selected for their ability to secret an IgG 2a immunoglobulin specific for single-stranded (ss) nucleic acids, were obtained by fusion of spleen cells from an unimmunized autoimmune MRL/1 pr male mouse with nonsecreting myeloma cells (MOPC-21, line Sp2/0-Ag 14). Designated MRss-1, this monoclonal antibody was (i) propagated by intraperitoneal injection of hybrid cells to pristane-treated. Balb/c mice, (ii) purified from the bulk of other proteins in ascites extracts by chromatography with DEAE-Sephacel adsorbent, and (iii) radiochemically labeled via reductive methylation using NaB3H4 and formaldehyde. The binding of 3H-labeled antibody to immobilized ssDNA- agarose, calf thymus) or soluble (fd DNA) ssDNA was rapid and dependent upon ssDNA and ionic strength, but not hydrogen ion concentration. Optimal binding occurred in both low and intermediate salt concentration (0.1-0.25 M NaCl), yet was completely abolished above 0.30 M NaCl. The presence of guanine (Gua)-containing mono-, oligo-, and polynucleotides also abolished and/or decreased 3H-labeled antibody binding to ssDNA-agarose. In these competition assays, the amount of Gua-containing mono-and oligonucleotides required to inhibit antibody binding by 50% (0.2-1.0 mg/mL) exceeded those of poly(G), rRNA, and fd DNA (i.e., 0.03-0.1 microgram/mL) by 4 orders of magnitude. In contrast, (deoxy)ribose 5'-phosphate as well as other nucleic acid derivatives devoid of Gua failed to inhibit antibody binding. The above findings were substantiated by the observation that 3H-labeled antibody bound to guanosine (G)- and guanidylate (pG)-conjugated Sepharose, yet not to other nucleoside (A, C, and U)- or nucleotide (pA, pC, and pU)-conjugated adsorbents. Last, the introduction of the methyl group at the N-2, O-6, and N-7 positions in the Gua ring system completely abolished antibody binding. Collectively, these results demonstrate that the MRss-1 antibody recognized single-stranded nucleic acid substrates by virtue of their content of guanidylate residues and, more specificity, by the presence of the Gua base moiety.
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PMID:Antibody-nucleic acid complexes. Identification of antigenic determinant of a murine monoclonal antibody specific for single-stranded nucleic acids. 617 38

Fusion of splenic lymphocytes from Lewis rats, immunized with affinity-purified estrogen receptor from the cytosol of MCF-7 human breast cancer cells, with two different mouse myeloma lines, has provided 13 monoclonal hybridoma lines secreting antiestrophilin antibodies, each of which (with one possible exception) recognizes a different antigenic determinant in the human receptor molecule. Of this library of monoclonal antibodies, some react with estrophilin from all sources tested, some react with mammalian but not avian receptors, whereas one preparation appears specific for estrophilin from primate sources. By proteolytic digestion under controlled conditions with mercury-deactivated papain, chymotrypsin, and trypsin, respectively, it is possible to remove sequentially the determinants recognized by one, two or three of the monoclonal antibodies, leaving the epitopes for the six remaining antibodies investigated on the steroid-binding portion of the receptor. The proteolytic fragment containing the epitope most readily removed (by mercuripapain) also contains the DNA-binding domain of the activated receptor molecule. Immunocytochemical staining, using the peroxidase procedure with various monoclonal antibody preparations, of frozen sections of human breast cancer tissue, fixed in ethanol or in picric acid-formaldehyde reagent, shows clearly that the majority of the native receptor, which appears in the cytosol after tissue homogenization, is actually localized within the nuclear compartment in the intact cell. The immunocytochemical technique also permits the identification of mixed populations of receptor-containing and non-containing cells in human breast cancers.
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PMID:Immunochemical studies of estrogen receptors. 620 Jul

Cryostat sections of human central nervous system (CNS) tissue absorbed sheep erythrocytes (E) sensitized with rabbit IgG antibody (A). The indicator cells bound to the choroid plexus, to the leptomeninges covering the brain and spinal cord, to the arachnoid granulations and to the perivascular tissue of the neural parenchyma. Unsensitized E or E sensitized with F(ab')2 fragments of IgG were not bound. The reactions were inhibited by pooled human IgG, human IgG1 and IgG3 myeloma proteins, and Fc fragments of pooled human IgG. Whole human IgG2 myeloma protein, IgM, IgA, F(ab')2 fragments of pooled human IgG and albumin did not inhibit. Experiments with reduced and alkylated IgG, EDTA, iodoacetamide, 2-mercaptoethanol, various pHs and salt concentrations, formaldehyde, periodic acid and neuraminidase did not reveal any differences between the Fc gamma receptors in the separate anatomical areas. The Fc gamma receptors in human CNS are thus apparently very similar.
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PMID:Properties of Fc gamma receptors in the human central nervous system. 628

The surface anionic site distribution on membranes of a monoclonal antibody-producing hybridoma cell line, and its two parental cells: normal spleen cells of immunized BALB/c mice and cells from a mouse myeloma line (NS-1), were investigated with the aid of the cationized ferritin (CF) labelling method, following glutaraldehyde/formaldehyde fixation of cells. The patch-like CF distribution on the hybridoma cells is similar to that of the NS-1 myeloma cells, but distinct from the even and continuous CF distribution of the immunized and nonimmunized normal spleen lymphocytes. The similarity in the formation of patch-like CF heaps, both on myeloma and hybrid cells is discussed in respect to the surface charge characteristic determined by cell fusion.
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PMID:Distribution of surface anionic sites on mouse hybrid myelomas. 662 23

Hybridomas secreting monoclonal antibodies have been produced by fusion of NS-1 mouse myeloma cells with the spleen cells of mice inoculated with a 60-65,000-mol wt fraction of proteins released from Drosophila embryo nuclei treated with DNase I. The antibodies secreted by the hybridomas were examined with polytene chromosomes of formaldehyde-fixed salivary gland squashes by an immunofluorescence assay. Most of the clonal antibodies obtained resulted in specific staining of the chromosomes relative to the cytoplasmic debris. In the case of clone 28, the antibodies showed a preferential association with sites of gene activity, both puffs and loci identified as puffing at some time during the third instar and prepupal period. In larvae that were heat shocked (exposed to 35 degrees C for 15 min before removal and fixation of the glands), the antibodies of clone 28 stained preferentially the induced heat-shock loci while continuing to stain most of the normal set of loci. The antigen for clone 28 was identified as a single protein of approximately 62,000 mol wt by using the antibodies followed by 125I-rabbit anti-mouse Ig to stain nitrocellulose replicas of SDS polyacrylamide gels of total chromosomal proteins. This study demonstrates that monoclonal antibodies can be used successfully in immunofluorescence staining of formaldehyde-fixed polytene chromosomes. The results verify the hypothesis that a specific nonhistone chromosomal protein is preferentially associated with the set of loci that includes both active sites and those scheduled to be active at some time in this developmental program. Such proteins may play a general role in the mechanisms of cell determination and gene activation.
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PMID:Monoclonal antibodies against a specific nonhistone chromosomal protein of Drosophila associated with active genes. 678 8

A mouse monoclonal antibody, designated NF1, was obtained from a cloned hybridoma isolated from a fusion of mouse myeloma Sp2 cells with spleen cells from a BALB/c mouse immunized with a crude neurofilament preparation from porcine spinal cord. NF1 is an IgG1 and recognizes, in immune blotting procedures, only the 200 K neurofilament triplet component. Its neurofilament-specific nature is further revealed by immunofluorescence microscopy studies on frozen tissue sections and various cultured cells. Immunoelectron microscopy studies on cytoskeletons of cultured neurones emphasize the discontinuous display along each neurofilament previously observed with polyclonal antibodies specific for the 200 K component after appropriate but rather cumbersome cross-absorption steps. Use of NF1 on various neuronal cells strongly supports the previous proposal of the existence of certain subpopulations of neurofilament-free neurones and the observation that certain neuronal arrangements, (e.g., those in dendrites of pyramidal cells of the hippocampus), although rich in neurofilaments, probably lack the normal 200 K triplet component. Since NF1 shows a broad cross-species reactivity and is able to react on formaldehyde-fixed tissue, it should be a useful reagent to study differential neurofilament expression and organization in embryonic, adult and pathological tissues.
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PMID:A monoclonal antibody specific for the 200 K polypeptide of the neurofilament triplet. 682 22

A new multipurpose cell micro-assay has been developed, using the protein dye amido black 10B as an indicator of cell numbers in 96-well plates. The assay is reliable, rapidly performed and can be combined with morphological evaluation and photography of stained cells. It permits investigations of various cell types including the human keratinocyte line HaCaT and subclones, mouse 3T3 fibroblasts and myeloma cells X63-Ag8.653. Briefly, cells are fixed by formaldehyde or glutaraldehyde and, following aspiration of fixative and non-adherent cells, are stained by amido black at pH 3.5. The protein-bound dye is completely eluted by NaOH and is scanned in a microplate reader at 620 nm against 405 nm or 750 nm. Non-adherent and semi-adherent cells are assayed by centrifugation of plates before fixation. The assay revealed a good linear correlation between absorbance of amido black, cell count and DNA content within the range 1000-64,000 HaCaT cells/well. The slope of the regression line varied with different cell types. Experiments with HaCaT cells and its c-Ha-ras oncogene-transfected subclones demonstrated the suitability of the assay for optimizing culture conditions, dose-response studies and for the screening and quantification of cell adhesion to extracellular matrix molecules. The assay was also used to evaluate cytotoxicity of drugs such as hexadecylphosphocholine, target cell killing in co-cultures with interleukin-2-activated lymphocytes, and the testing of hybridoma antibodies for their biological effects on proliferation and adhesion. The assay is highly reproducible, sensitive, independent of cellular aggregation and economic for multiple applications.
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PMID:The amido black assay: a simple and quantitative multipurpose test of adhesion, proliferation, and cytotoxicity in microplate cultures of keratinocytes (HaCaT) and other cell types growing adherently or in suspension. 750 74

A substantial body of literature now exists on the carcinogenic hazards of firefighting. The authors discuss in detail the data on the carcinogens benzene, asbestos, PAHS, formaldehyde, and diesel exhaust, and they go on to examine the prevalent cancers in firefighters, including leukemia, non-Hodgkin's lymphoma, multiple myeloma, and cancer of the brain and bladder.
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PMID:The risk of cancer in firefighters. 890 50

Interest in Mannich bases of 8-hydroxyquinoline stems from reports of their high potency against human cancer cells. In the search for potential anticancer drug candidates, Mannich bases of 8-hydroxyquinoline (7-pyrrolidinomethyl-8-hydroxyquinoline, 7-morpholinomethyl-8-hydroxyquinoline, 7-piperidinomethyl-8-hydroxyquinoline and 7-diethylaminomethyl-8-hydroxyquinoline) were synthesised by reaction with various secondary amines and formaldehyde. They were prepared as hydrochlorides. The cytotoxic activity of 7-pyrrolidinomethyl-8-hydroxyquinoline, 7-morpholinomethyl-8-hydroxyquinoline and 7-diethylaminomethyl-8-hydroxyquinoline compounds in the National Cancer Institute in-vitro cancer cell line panel was determined. It was found that they exhibited substantial cytotoxic activity against leukaemia. The log concentration of 7-pyrrolidinomethyl-8-hydroxyquinoline, 7-morpholinomethyl-8-hydroxyquinoline and 7-diethylaminomethyl-8-hydroxyquinoline that inhibited 50% of 60 cell lines' growth were -4.81 M, -5.09 M and -5.35 M, respectively. Compound 7-pyrrolidinomethyl-8-hydroxyquinoline was selected for further in-vivo testing. The electrophysiological effect of 7-pyrrolidinomethyl-8-hydroxyquinoline also was tested in human myeloma cells (RPMI 8226). The outward current was voltage dependent, activating at -40 mV and believed to be the voltage-activated K+ current I(K(V)). 7-Pyrrolidinomethyl-8-hydroxyquinoline (1-30 microM) caused the inhibition of I(K(V)) in a concentration-dependent manner. The IC50 value of 7-pyrrolidinomethyl-8-hydroxyquinoline-induced inhibition of I(K(V)) is 23 microM. The GI50 value of 7-pyrrolidinomethyl-8-hydroxyquinoline-induced inhibition of cell growth is 14 microM. The results suggest that at least part of the cytotoxicity effect of 7-pyrrolidinomethyl-8-hydroxyquinoline on myeloma cells could be related to blockade of voltage-activated K+ channels.
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PMID:Synthesis and cytotoxicity evaluation of some 8-hydroxyquinoline derivatives. 1041 Dec 13

Protein kinase 2 (CK2) is a ubiquitous and constitutively active serine/threonine protein kinase with various cell functions. It typically forms tetrameric complexes consisting of two catalytic (alpha and/or (alpha') and two regulatory (beta) subunits. The aim of this study was to produce monoclonal antibodies (MAbs) against the CK2beta subunit and to characterize their suitability for Western blotting, immunoprecipitation, and immunohistochemical applications. Bacterially expressed CK2beta-6His-GST recombinant protein has been used as an antigen. Balb/c mice were immunized and given a final boost, and their spleen cells were collected and fused with SP2/0 myeloma cells using PEG 2000. The fused cells were then selected in the HAT-RPMI medium. Anti- CK2beta high-titer antibody-producing hybridoma cell lines were identified by enzyme-linked immunosorbent assay (ELISA) and then subcloned by limiting dilution in HT-RPMI medium supplemented with 20% fetal bovine serum (FBS). A total of 10 IgG-producing cell lines were selected and further tested for their reactivity with the CK2beta subunit using ELISA, Western blots, immunoprecipitation, and immunostaining of formaldehyde-fixed paraffin-embedded tissue sections. The results obtained clearly indicate that several clones produce antibodies that recognize specifically recombinant and endogenous CK2beta subunit in Western blotting and immunoprecipitation, and are suitable for immunohistochemical analysis. In summary, the produced antibodies will be useful for researchers investigating signaling pathways involving CK2 kinase and their deregulation in human pathologies.
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PMID:Generation and characterization of monoclonal antibodies to protein kinase 2 (CK2) beta subunit. 1612 27


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