Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019204 (hepatocellular carcinoma)
 71,386 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

By means of the reaction of specific inhibition of precipitation in agarose gel and using the rabbit immune sera against nuclear nonhistone proteins (NHP) in the NHP-DNA complexes isolated from the rat kidney it is shown that the single intraperitoneal injection of hepatocarcinogens, 4-dimethylaminoazobenzene (DAB) or N-nitrosodiethylamine (DEN) induces the appearance of hetero-organic antigens of the kidney nature in the NHP pattern of the liver. These antigens identical, as it proved to be, to the same NHP-antigens from the cells of transplantable rat hepatoma 27 and ascitic Zajdela hepatoma could be found in the NHP pattern of the rat liver during 1 to 12 and 1 to 64 days after the DAB and DEN injection, respectively. In all cases when the hetero-organic NHP-antigens were found the profiles of proper phosphoprotein kinase activity of the fractions of NHP eluted by 0.4-0.5 M NaCl using gradient chromatography on phosphocellulose contained peaks that were not characteristic to the liver NHP but were typical of NHP from the intact rat kidney. In the SDS-PAAG electrophoresis the mentioned fractions form one line with the molecular weight 15000-20000.
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PMID:[Detection of the common features in the antigenic structure and the spectra of the phosphoprotein kinase activity proper of the water-soluble fractions of DNA-free nuclear nonhistone proteins from hepatomas and the liver in rats following a single administration of hepatocarcinogens]. 393 50

The nuclear matrix of Zajdela hepatoma cells, in which DNA synthesis was blocked by novobiocin, contained 2.5-3.0 times more DNA and protein not dissociating in 2 M NaCl than the nuclear matrix of control cells. Chromatography of nuclear matrix preparations on Sepharose 2B-CL resulted in isolation of tightly bound DNA-protein complexes which did not dissociate in 8 M urea or 0.1% SDS. Subsequent elution of DNA-protein complexes on a hydroxylapatite column with a buffer containing 4 M guanidine hydrochloride and 5 M urea caused partial dissociation of the complexes. Electrophoretic analysis revealed essential changes in the composition of proteins DNA-protein complexes of hepatoma cells nuclear matrix during inhibition of DNA synthesis.
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PMID:[Reorganization of the protein composition of the nuclear matrix of hepatoma cells after inhibition of DNA synthesis with novobiocin]. 407 85

A new method to purify papain- or detergent-solubilized form (papain or detergent form) of gamma-glutamyltransferase from rat hepatomas as well as from rat kidney by immuno-affinity column chromatography is presented. The antibody-column was prepared by coupling the anti-kidney papain form antibody, which had been purified by using a kidney papain form-Sepharose column, to CNBr-activated Sepharose 4B. The enzyme bound to the antibody-column was eluted with 0.04 M NH4OH. By this method, detergent forms were purified 300 and 1600-fold in approx. 50% yields from rat kidney and rat ascites hepatoma AH 13, respectively, and the papain form was also purified 16 000-fold in a similar yield from primary hepatoma which has a very low activity of this enzyme. Preparations thus obtained apparently did not contain any peptide other than heavy and light subunit peptides of this enzyme on SDS-polyacrylamide gel electrophoresis. The detergent form of kidney enzyme was preferentially absorbed to a hydrophobic column of aminooctyl-Sepharose, while the papain form was not, suggesting that the detergent form might be adsorbed to the column through hydrophobic interaction of the membrane-binding domain. The domain peptide was also purified by the hydrophobic column after release from the detergent form by papain treatment. The molecular weight of the peptide was estimated to be about 16 000 on SDS-polyacrylamide gel electrophoresis. On double immunodiffusion, the domain peptide reacted with anti-detergent form antibody but not with anti-papain form antibody. The domain-specific antibody was also purified from the anti-detergent form antibody.
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PMID:Purification of detergent-solubilized form and membrane-binding domain of rat gamma-glutamyltransferase by immuno-affinity and hydrophobic chromatography. 613 98

Some regularities of [3H]triamcinolone acetonide (TA)binding to glucocorticoid-sensitive Morris hepatoma cell nuclei were studied. It was shown that part of the hormone incorporated into the nuclei form highly stable complexes with nuclear structures that are not destroyed during nuclei lysis with 0.25% SDS. Such complex formation is not practically suppressed by a 500-fold excess of non-labeled TA. As the time of incubation of Morris hepatoma cells with the hormone rises from 10 min to 24 hours, the specific binding of TA to the nuclei decreases, while the specific radioactivity of the [3H]TA-nuclei complexes resistant to 0.25% SDS increases. The stable complexes are eluted from Sepharose 6B together with the bulk of the nuclear proteins and do not contain DNA. Actinomycin D extrudes, to some extent, the [3H]TA from the complexes having specific binding sites that are localized in the nuclei and induces the accumulation of the steroid in the firmly bound nuclear complexes resistant to 0.25% SDS. The ability to suppress hormonal induction of tyrosine aminotransferase was detected only in the antibiotics with a high affinity for the GC-pairs of DNA. i.e., actinomycin D and mitramycin. It was assumed that high concentrations of TA specifically bound to the nuclei are necessary only at initial steps of hormonal induction. At later stages, gradual dissociation of the complexes takes place and the hormone is accumulation within the composition of the SDS-resistant firmly bound complexes.
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PMID:[Interaction of triamcinolone acetonide with Morris hepatoma cells in the presence antibiotics--inhibitors of RNA synthesis]. 615 1

Monoclonal antibodies were generated against the intermediate filament proteins of different human cells. The reactivity of these antibodies with the different classes of intermediate filament proteins was determined by indirect immunofluorescence on cultured cells, immunologic indentification on SDS polyacrylamide gels ("wester blot" experiments), and immunoperoxidase assays on intact tissues. The following four antibodies are described: (a) an antivimentin antibody generated against human fibroblast cytoskeleton; (b), (c) two antibodies that recognize a 54-kdalton protein in human hepatocellular carcinoma cells; and (d) an antikeratin antibody made to stratum corneum that recognizes proteins of molecular weight 66 kdaltons and 57 kdaltons. The antivimentin antibody reacts with vimentin (58 kdaltons), glial fibrillary acidic protein (GFAP), and keratins from stratum corneum, but does not recognize hepatoma intermediate filaments. In immunofluorescence assays, the antibody reacts with mesenchymal cells and cultured epithelial cells that express vimentin. This antibody decorates the media of blood vessels in tissue sections. One antihepatoma filament antibody reacts only with the 54 kdalton protein of these cells and, in immunofluorescence and immunoperoxidase assays, only recognizes epithelial cells. It reacts with almost all nonsquamous epithelium. The other antihepatoma filament antibody is much less selective, reacting with vimentin, GFAP, and keratin from stratum corneum. This antibody decorates intermediate filaments of both mesenchymal and epithelial cells. The antikeratin antibody recognizes 66-kdalton and 57-kdalton proteins in extracts of stratum corneum and also identifies proteins of similar molecular weights in all cells tested. However, by immunofluorescence, this antibody decorates only the intermediate filaments of epidermoid carcinoma cells. When assayed on tissue sections, the antibody reacts with squamous epithelium and some, but not all, nonsquamous epithelium. Therefore this antistratum corneum antibody and the anti-54-kdalton antibody identify unique epitopes present in the various cytokeratin molecules of epithelial cells. None of the hybridoma antibodies react with neurofilament proteins. The different patterns of reactivity of these antibodies suggest that many of the immunologically distinct intermediate filament proteins contain common antigenic determinants.
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PMID:Monoclonal antibodies to intermediate filament proteins of human cells: unique and cross-reacting antibodies. 618 72

Reuber H-35 hepatoma cells were examined for their ability to synthesize protein in vitro, especially to produce alpha-fetoprotein (AFP). The presence of AFP in the culture supernatant solution was determined immunologically by the micro-Ouchterlony method. Charge heterogeneity of AFP was examined electrophoretically in continuous gradient polyacrylamide microgels. With regard to the duration of culture, there was no remarkable change in the ratio of two peaks of AFP, and which came out as a major combined peak and a similar peak by PAS staining on the condition of added SDS. These findings indicated that Reuber H-35 hepatoma cells had potential to produce two charge variants of AFP in vitro.
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PMID:Characterization of alpha-fetoprotein secreted from cultured reuber H-35 hepatoma cells. 618 63

Murine tumors contain low molecular weight factors that inhibit macrophage accumulation at inflammatory foci. Certain oncogenic murine leukemia viruses contain similar inhibitory activity and the active component of the retroviruses was shown to be the envelope protein P15E. A number of murine malignant and nonmalignant cell lines, as well as primary tumors, have now been examined to determine whether production of retroviral P15E or a related protein is characteristic of neoplastic cells. Tumor lines examined included the Hep 129 hepatocarcinoma, BP8 fibrosarcoma, RL1 lymphoma, and three variants of the B16 melanoma. Tumor lines were virus negative by electron microscopy. Nonmalignant cells examined included ST0, 3T3/BALB, and 3T3/L1 fibroblasts and unstimulated, as well as mitogen-stimulated murine splenocytes. Cells were pulse-labeled with [35S]methionine, proteins immunoprecipitated with two monoclonal antibodies to P15E and analyzed by SDS-PAGE and gel fluorography. All tumor lines synthesized a approximately 19,000-dalton protein that co-migrated with retroviral P15E on SDS-PAGE. None of the nonmalignant cells synthesized this protein. Two-dimensional gel electrophoresis of the proteins precipitated from two B16 melanoma lines by monoclonal anti-P15E showed them to be physicochemically similar to P15E from Rauscher leukemia virus. A competition ELISA assay for P15E was developed and confirmed the results obtained by metabolic labeling and demonstrated P15E-related antigens in the tumor cell lines and also in the ascites fluid of mice injected with Hep 129 cells. More importantly, P15E antigens were expressed in both a spontaneous mammary adenocarcinoma and in a primary methylcholanthrene-induced fibrosarcoma. Nonmalignant tissues from animals bearing these tumors contained no detectable P15E antigen. Extracts from the primary fibrosarcomas, when injected into the thighs of mice, inhibited the intraperitoneal accumulation of inflammatory macrophages. The inhibitory activity was specifically removed by absorption with monoclonal antibody to P15E. These results suggest that synthesis of the immunosuppressive retroviral protein P15E, or a very similar protein, routinely occurs during the growth of murine neoplastic cells. This P15E-related protein is present in spontaneous murine primary tumors as well as in all murine tumor cell lines tested. The expression of such proteins by transformed cells in vivo could confer a selective advantage for their sustained growth since they would be more likely to escape immune surveillance.
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PMID:Murine malignant cells synthesize a 19,000-dalton protein that is physicochemically and antigenically related to the immunosuppressive retroviral protein, P15E. 619 38

The Con A-peroxidase reaction has demonstrated glycoproteins with molecular masses of 200 and 50 kilodalton on the polyacrylamide gel-SDS electrophoregrams of the molecular matrices isolated from rat liver, hepatoma 27 and Zajdela's ascites hepatoma. Both hepatomas contained an additional band of about 38 kilodalton, whereas Zajdela's hepatoma distinct bands of 54 kilodalton and less demonstrable of over 200 and about 105 and 68 kilodalton. Electron microscopy showed Con A-ferritin staining, more prominent in hepatomas than in the liver, at the periphery of isolated nuclear matrix preparations. Ruthenium red staining characteristic of acidic polysaccharides (glycosaminoglycans), on the contrary, was more pronounced in liver nuclear matrices.
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PMID:[Carbohydrate components of the nuclear matrix in rat liver and hepatoma]. 619 9

A 17-year-old male with previously undiagnosed congenital Factor IX deficiency (13%) presented with gastrointestinal bleeding and a hepatic mass. Prolonged thrombin and Reptilase times, which partially corrected with CaCl2 and a discrepancy between thrombin-clottable and immunoreactive plasma fibrinogen, suggested a dysfibrinogenemia. Laparotomy disclosed metastatic hepatoma. Adequate hemostasis was obtained with clotting factor replacement, but wound healing was delayed. Patient fibrinogen purified with 2.1 M glycine migrated normally on immunoelectrophoresis and 7.5% polyacrylamide-SDS gel electrophoresis. However, fibrin monomers prepared from purified patient fibrinogen displayed impaired aggregation at high and low ionic strengths when compared with fibrin monomers from normal and control Factor IX deficient subjects. Aggregation of normal monomers was delayed when mixed 1:1 with patient monomers. Fibrinopeptide release was normal, and total sialic acid content was similar to that of normal and control fibrinogens. Chemotherapy, consisting of 5-FU given via intra-arterial hepatic infusion, was accompanied by significant transient clinical improvement which coincided with correction of thrombin clotting times and fibrin monomer aggregation. Reappearance of fibrinogen dysfunction occurred with clinical deterioration prior to death from metastatic hepatoma and sepsis. This case is the first to corroborate the postulated tumor marker role of dysfibrinogenemia in a patient with hepatoma by documenting a direct relationship with response to chemotherapy.
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PMID:Acquired dysfibrinogenemia in a hemophiliac with hepatoma: resolution of fibrinogen dysfunction following chemotherapy. 626 56

Alpha 1 protease inhibitor antigen was identified in the culture medium of the human ascites hepatoma cell line SK-HEP-1. Trypsin inhibitory activity and alpha 1 Pl antigen accumulated in serum-free medium concomitantly over a period of several days. Radioactive alpha 1 Pl antigen was detected in conditioned medium from cultures supplemented with 35S-L-methionine, indicating a synthesis and release of the protein. Alpha 1 Pl antigen in conditioned medium appeared to be antigenically identical to that in human plasma, and the newly synthesized (radiolabeled) antigen co-migrated with plasma, alpha 1 Pl after immunoelectrophoresis or SDS-polyacrylamide gel electrophoresis. Moreover, evidence is presented that the synthesized inhibitor exhibits functional activity, since the 35S-labeled alpha 1 Pl in conditioned medium complexes with trypsin. We conclude that SK-HEP-1 cells in culture produce functionally active alpha 1 Pl which may be identical to that in plasma.
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PMID:Functional alpha 1 protease inhibitor produced by a human hepatoma cell line. 627 80


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