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)

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

Purified GM1 and GM2 gangliosides incorporated into liposomes were injected subcutaneously in BALB/c mice every 3-4 days after pretreatment of the animals with low-dose cyclophosphamide. Serum samples were collected at different intervals and tests by ELISA for the presence of anti-ganglioside antibodies. Four doses (50 micrograms each) were sufficient to raise a measurable primary type of response to GM1, while nine doses were required to obtain measurable IgM antibody titers to GM2. Three monoclonal antibodies (MAbs) wer generated by fusing splenocytes with mouse myeloma cells. The specificity of MAbs was determined by ELISA and HPTLC-immunostaining using a panel of purified glycolipids. The MAb designated E1 showed a high degree of specificity because it reacted only with N-acetyl GM2. Monoclonal antibody A3 reacted predominantly with GM2 and GM1, but also reacted moderately with the GM3 ganglioside. The epitope recognized by this MAb is suggested to be the trisaccharide sequence GalNAc beta 1-4(NeuAc alpha 2-3)Gal. The third MAb (F6) reacted strongly with GM1 but a weak reactivity was also observed with GD1b as well as with asialo-GM1, indicating that the terminal tetrasaccharide Gal beta 1-3GalNAc beta 1-4(NeuAc alpha 2-3)Gal- structure is probably involved in antigenic recognition. Formalin-fixed and paraffin-embedded tissue sections were stained with the E1 and A3 MAbs, using the avidin-biotin complex (ABC) technique. Strong immunoreactivity for E1 appeared in the tumor cells of five primary lung carcinomas and in five malignant melanomas. No immunoreactivity was demonstrated in the parenchyma of a lung without malignancy, or in a metastasis from a colon carcinoma.
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PMID:T cell-independent B cell response to self-monosialogangliosides: primary response monoclonal antibodies. 759 Jul 82

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

To develop a molecular-based assay so that the diagnosis of feline B-cell neoplasia can be facilitated, we have characterized 24 feline immunoglobulin heavy chain variable region (IGH V) complementary DNA (cDNA) transcripts. Structural homology with rearranged human IGH V genes was found, and the sequence information was used to design a feline-specific polymerase chain reaction (PCR)-based assay to amplify the complementarity determining region 3 as a marker for B-cell clonality. Conserved primers derived from the second and third framework regions of V gene segments were used in conjunction with 2 sequence-specific primers and 1 degenerate primer derived from the J gene segments. Each PCR reaction was run in duplicate, and both native and denatured PCR products were evaluated using polyacrylamide gel electrophoresis. Formalin-fixed, paraffin-embedded (FFPE) tissue sections from cats with confirmed B-cell neoplasia (diffuse large B-cell lymphoma, plasmacytoma, and myeloma) were examined, and 15/22 (68.2%) cats produced results indicative of the presence of a monoclonal population of B cells. The evaluation of denatured PCR products (heteroduplex analysis) facilitated a more accurate interpretation in 3/15 (20%) cats. Pseudoclonality was a major reason for the failure to detect monoclonality. Poor DNA quality is a significant concern and was responsible for the removal of 2 cats from the study. Using this assay, FFPE normal feline lymphoid tissues and unfixed peripheral blood mononuclear cells were determined to be composed of polyclonal populations of B cells. This assay represents a useful adjunctive diagnostic tool for the diagnosis and investigation of feline B-cell lymphoproliferative disorders.
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PMID:Characterization of feline immunoglobulin heavy chain variable region genes for the molecular diagnosis of B-cell neoplasia. 1614 6

Protein A of Staphylococcus aureus can be detected on cell walls of intact bacteria by use of radioactively labeled myeloma globulin. Of 156 strains of S. aureus, 141 (90%) contained protein A. None of 47 S. epidermidis strains was positive for protein A. The production of protein A was influenced by incubation temperature but not by differences in incubation time or inoculum size. A medium containing a high concentration of NaCl suppressed the production of protein A by 90%. Formalin treatment of protein A-containing strains caused a decrease in the amount detected, but no further decrease was detected after storage at 4 C. No correlation was found between absence or presence of protein A and phage type or phage group. Sixteen S. aureus strains were studied extensively. There was no correlation between protein A and any of the 26 antigenic characteristics which have been previously described in these strains.
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PMID:Occurrence of protein a in staphylococcal strains: quantitative aspects and correlation to antigenic and bacteriophage types. 1655 23

Anti-melatonin monoclonal antibodies (MAbs) of high titer were prepared by coupling melatonin to bovine serum albumin with formaldehyde and by immunizing BALB/c mice with multifocal intradermal injections and by fusing high titer antibody producing spleen cells with myeloma cells of SP2/0 origin. Five MAbs were selected for further characterization as classes and subclasses. After four successive limiting dilutions, antibodies were produced by these five clones with high affinities ranging from 10(9) to 10(11)/m. These clones were found to be of the immunoglobulin Ig G1 and IgG(2b) subclass with kappa light chain. A systematic study of cross-reactions with seven compounds (indole, aromatic and imidazole derivatives) showed that the antibody had a high specificity for melatonin, low reactivity with 6-hydroxymelatonin and N-acetyl-5-hydroxytryptamine, and no detectable reactivity with tryptamine, l-tryptophan, 5-methoxytryptamine and N-acetyl-L-tryptophan. The roles of the indole nucleus and the side chain in the determination of the antigenic properties of the molecule are discussed. One of the MAbs, 4C9D7, was used to establish a competitive enzyme-linked immunosorbent assay for the detection of melatonin in supernatant.
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PMID:Preparation and identification of anti-melatonin monoclonal antibodies. 1663 23


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