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)

The host range of the C particle produced by FLOPC-1 myeloma cells, FLOPC-1 murine myeloma-associated virus (FL-MuMAV), was assessed in terms of its ability to productively infect and/or induce new viral antigens in a variety of different cell lines. Production of C particle-like structures by cells exposed to FL-MuMAV) was determined by incorporation of [3H]uridine into particles with a density of 1.16 g/ml and/or measurement of RNA-dependent DNA polymerase activity in concentrated culture medium. to FL-MuMAV was capable of infecting NIH/3T3, normal rat kidney (NRK) cell, BALB/c 3T3, and the A31 clone of BALB/3T3 cells but not rabbit cell line, SIRC. Thus, it is an N, B-tropic murine virus as replication in NRK cells has been shown not to delineate a group of murine viruses with a separate host range (M. M. Lieber, C. J. Sherr, and G. J. Todero, 1974). Further neoantigens, reactive with anti-FL-MuMAV serum, were detected on infected cells. Production of the MuMAV-like particle and MuMAV-associated cell antigens in infected NIH/3T3 and NRK cells persisted for three subcultures. The limited production could not be explained by the lack of an RNA-dependent DNA polymerase or high-molecular-weight RNA as the particles possessed both of these properties. The particles produced by infected NIH/3T3 or NRK cells were antigenically and physicochemically similar to FL-MuMAV and not K-MuLV. The MuMAV-like particles produced by infected NIH/3T3 were capable of limited replication in NIH/3T3 and and BALB/3T3 cells, whereas NRK-MuMAV replicated for a limited period in NIH/3T3, NRK, and SIRC cells; i.e., they had a different host range than FL-MuMAV. The particles produced by infected BALB/3T3 and A31 cells had the same host range as FL-MuMAV. In certain situations, isotopically labeled particles with a density of 1.16 g/ml were produced which appeared to lack RNA-dependent DNA polymerase.
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PMID:Host range studies of FLOPC-1 murine myeloma C particles. 5 24

A high molecular weight RNA-reverse transcriptase complex in the culture media of peripheral leukocytes obtained from two Japanese patients with myeloma-leukemia was detected by demonstration of a 3H-uridine peak and a peak of DNA polymerizing activity banding at a density of 1.15-1.19g/ml. The enzyme in the complex was able to utilize poly(rA)-d(pT)10 or poly (rC)-d(pG) 12-18, but not poly (dA)-d(pT) 10 or (dT) 12-18 as template-primers. The sucrose density sedimentation analysis revealed that RNA in the complex sedimented at a location of approximately 50s and 20-30s.
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PMID:RNA-reverse transcriptase complex from cultured human myeloma-leukemia cells. 7 Dec 70

The retrovirus designated RPMI8226V (isolated from human myeloma cells RPMI8226) has been characterized with respect to its morphological, biochemical and immunological properties as well as its propagation in various animal and human cells. The myeloma cells RPMI8226 produce intracytoplasmatic A-type particles and extracellular particles. The extracellular particles have been classified as immature particles with translucent core center, typical mammalian C-type virus particles and C-type particles with intermediate membrane. However, the budded particles in secondarily infected human neoplastic cells contained complete doughnut-shaped nucleoids. This type of budding is rather characteristic for B-type particles. The 3H-uridine labeled RPMI8226 viral particles have a buoyant density 1.17 g/ml in sucrose gradient containing high molecular weight RNA and the distribution of viral structural proteins in SDS-PAGE is characteristic for oncornaviruses. The internal structural proteins according to MW are ranged from 13 000 to 30 000 daltons. The virus contains a magnesium-dependent reverse transcriptase. The cellular homogenate and viral concentrate from RPMI8226 cultures do not react with antibodies against ALSV, MuLV, FeLV, RD114, MP-MV and SiSLV. The only reaction was scored with anti BLV antibodies. However, anti BLV serum inhibiting the reverse transcriptase activity of BLV to 60% does not cross-react with the reverse transcriptase of RPMI8226V. In contrast to BLV concentrates, neither XC nor KC cells show syncytia formation by RPMI8226V. The RPMI8226V replication is restricted to human tumor and normal human glia-like cells. The possible origin of the virus is discussed.
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PMID:The retrovirus particles in human myeloma cells RPMI8226: morphological, biochemical, immunological and infective transmission studies. 8 Jul 55

Some human marrows in culture release particles with oncornavirus-like properties. This study was designed to examine the immunological properties of similar particles in human marrow culture supernates. Leukemic and nonleukemic marrows were cultured for 5-7 days in the presence of [14C]uridine and [3H]leucine or [3H]glucosamine. Labeled supernatant components banding in sucrose gradient densities of 1.20-1.24 g/ml were used as antigen in a double antibody immunoprecipitation assay. The assay was validated by end point titrations and competition with unlabeled antigen; purified myeloma proteins were used as negative controls. Cross-reactivity with mammalian oncornaviruses, as judged by competitive inhibition of precipitation by these viruses, was slight and at the border of the sensitivity of the method. Precipitated antigens analyzed by SDS polyacrylamide gel electrophoresis contained three distinct polypeptides of about 70,000, 45,000 and 30,000 mol wt; these comigrated with the gp 70, pg 45, and p 30 of a murine leukemia virus. Similar polypeptides were obtained from both leukemic and nonleukemic marrow culture supernates. As determined by the radioimmunoprecipitation assay, 32 of 45 leukemic sera (71%), 36 of 45 normal sera (80%), 15 of 19 sera from family contacts of leukemic patients (79%), 14 of 21 cord blood specimens (67%), and 21 of 23 sera (91%) from patients with systemic lupus erythematosus had detectable antibody activity.
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PMID:Antibodies in human sera to oncorna virus-like proteins from normal or leukemia marrow cell cultures. 18 53

Infection of mouse myeloma cells (MPC-11) with vesicular stomatitis (VS) virus resulted in rapid and marked reduction in cellular RNA synthesis considerably before cell viability was compromised. Mouse myeloma cells responded maximally to viral infection at a multiplicity of 1 and were considerably more se;sitive to shut-off of RNA synthesis than were mouse L cells or BHK-21 cells. This inhibition of cellular RNA synthesis was shown not to be caused by differential membrane permeability of infected and uninfected MPC-11 cells to [3H]uridine, nor was it due to greater degradation of previously synthesized RNA. VS viral infection appeared not to impede transport of newly synthesized nuclear RNA to the cytoplasm; moreover, infected cells accumulated polyadenylated mRNA at the same rate as did uninfected cells. Polyacrylamide gel electrophoresis of newly synthesized nuclear RNA demonstrated that the polydisperse nature and size distribution were not affected by VS viral infection. Isolated nuclei of infected MPC-11 cells also inhibited greatly impaired capacity to synthesize RNA despite the absence of cytoplasmic factors. Infected-cell cytosol did not inhibit transcription by uninfected-cell nuclei, nor did uninfected-cell cytosol reverse viral inhibition of nuclear transcription. Studies with alpha-amanitin revealed that VS viral infection inhibited the activity of polymerases I, II, and III, but only polymerase II was affected progressively throughout infection and to a much greater extent. These data suggest that, even at low multiplicities of infection, VS virus rapidly shuts off cellular RNA synthesis at the level of nuclear transcription.
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PMID:Inhibition of RNA synthesis in mouse myeloma cells infected with vesicular stomatitis virus. 20 71

Several human myeloma cell populations were studied using a combination of cytochemical (Unna-Pappenheim and naphthol yellow staining, Feulgen reaction) and autoradiographical (uridine, leucine, thymidine uptake and actinomycin binding) techniques. Progressive differentiation of the myeloma population was associated with: 1. a loss of proliferative activity, 2. decreased transcriptional capacity, 3. decreased RNA and protein synthesis, 4. increased RNA and protein concentrations, 5. greater stability of the protein synthesis template. The existence of a pre-myelomatous compartment is suggested in the light of these results and those of previous kinetic studies in vivo.
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PMID:Biology of the human myeloma cell population. I.Macromolecular characteristics. 70 77

A kinetic study of five human myeloma cell populations before and after chemotherapy using cytochemical and autoradiographical techniques showed: 1. a large number of cells, with a DNA content intermediate between 2c and 4c, that did not incorporate thymidine ('U' cells) and were indicative of ineffective myelomapoiesis; 2. non cell cycle-specific (cyclophosphamide) followed by cell cycle-specific (vincristine) treatment led to an increase in the 3H-thymidine labelling index (LI) and activation of macromolecular synthesis (increased uridine and leucine uptake and actinomycin binding capacity) pointing to early cell recruitment. A high percentage of 'U' cells can be found even after therapy. The LI variations make it clear that recruitment after therapy is overestimated by at least 40% due to ineffective myelomapoiesis. In the light of this and previous personal studies, we propose a kinetic pattern: the myeloma population may be seen as a highly differentiating population whose non-proliferating cells cannot re-enter the cycle. By contrast, the acute leukemia populations are unable to differentiate, and the non-proliferating cells (G0) can be recalled into the cell cycle.
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PMID:Biology of the human myeloma cell population. II. Cytokinetic characteristics. 70 78

The effect of D-glucosamine and D-galactosamine on the content of uridine nucleotides in myeloid tumor (Graffi) and myeloma MOPC-21 of mice was investigated in vivo. After treatment with aminosugars a marked decrease in UTP and UDP-glucose quantity was found. The trapping of uridine phosphates by formation of UDP-sugar derivatives was different in the two tumors and depended on the aminosugar employed. D-glucosamine provoked an increase in the UDP-N-acetylglucosamine pool size in myeloid tumor (Graffi) and myeloma MOPC-21. D-galactosamine administration led to formation of UDP-galactosamine and UDP-N-acetylglucosamine in myeloma MOPC-21, while in myeloid tumor (Graffi) an increase in the content of UDP-N-acetylglucosamine was obtained only.
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PMID:Effect of D-glucosamine and D-galactosamine on the uridine nucleotide concentration in mouse myeloid tumor (Graffi) and myeloma MOPC-21. 115 35

MPC-11 myeloma cells synthesizing IgG were labeled in vitro with 3H-uridine and the cell lysates, or purified polysomes treated with rabbit antiserum against the purified MPC-11 protein. The specificity of the immune precipitation was tested by rabbit anti-egg albumin and by precipitation of polysomes from "non-producer" myeloma and HeLa cells. The specific precipitation was 10 to 15% of the total cytoplasmic RNA for the IgG-producing clone of MPC-11 and about 2% for the non-producer clone or HeLa cells. Up to 20% of the total polysomal and ribosomal RNA were precipitated from the IgG producing clone. This value correlated with the IgG synthesis of these cells which is also about 20% of the total protein produced. The results suggest that myeloma cells produce a relatively large quantity of IgG due to the presence of a large amount of specific m-RNA molecules.
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PMID:Immune precipitation of immunoglobulin producing polysomes from mouse myeloma cells. 116 19

When human myeloma cells are pulsed for one hour with 3H-uridine and chased for six hours in fresh medium containing unlabeled uridine, the processing of 45 S rRNA precursor into the stable 28 S and 18 S rRNA components can be followed. However, when the cells are chased in exogenous adenosine instead of uridine, the accumulation of 18 S rRNA is selectively inhibited. Cells pulsed with 3H-adenosine and chased in the absence of exogenous nucleosides exhibit normal rRNA precursor processing, while cells pulsed simultaneously with 3H-uridine and 3H-adenosine and chased with uridine and adenosine are deficient in labeled 18 S rRNA. Consequently, the inhibition of 18 S rRNA accumulation by adenosine is not an artifact of labeling nor is it relieved by an equal molar concentration of uridine. The wasting of 18 S rRNA in human myeloma cells is similar to that reported to occur in normal lymphocytes during the quiescent state.
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PMID:Wasting of 18 S ribosomal RNA by human myeloma cells cultured in adenosine. 127 May 22


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