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)

DNA-dependent ATPase IV has been purified to near homogeneity from the Novikoff rat hepatoma. The enzyme is devoid of DNA polymerase, RNA polymerase, exonuclease, endonuclease, phosphomonoesterase, 3'- or 5'-phosphodiesterase, polynucleotide kinase, protein kinase, topoisomerase, helicase or DNA reannealing activities at a detection level of 10(-5) to 10(-7) relative to the ATPase activity. The enzyme is a monomer of Mr 110,000, has a sedimentation coefficient of 5.9 S, a Stokes radius of 40 A and a frictional coefficient of 1.32. In the presence of Mg2+ ion and a polynucleotide effector, ATPase IV hydrolyzes either ATP or dATP to the nucleoside diphosphate plus Pi. Other ribo- or deoxyribonucleoside triphosphates are not substrates. ATPase IV utilizes double-stranded DNA and single-stranded DNA as effector; however, it does not utilize poly(dT). The Km for dsDNA or ssDNA is 2.2 microM (nucleotide). A variety of ATP analogues were found to be competitive inhibitors of ATPase IV.
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PMID:Purification and enzymological characterization of DNA-dependent ATPase IV from the Novikoff hepatoma. 296 5

We have obtained a cloned cell line (Li-7A) from primary cultures of a human hepatoma xenograft (Li-7). Li-7A was able to grow in the absence of serum. Growth was stimulated 0-3 fold by addition of newborn calf serum, but was inhibited in DME/F12 media containing nine growth factors. The ectoMg2+-ATPase was 1.5-2 fold higher than the ectoCa2+-ATPase activity in cells grown in media with or without serum. In cells grown in media supplemented with the nine factors, the ectoCa2+-ATPase activity exceeded the ectoMg2+-ATPase, and there was also a 5-10 fold increase in its specific activity. Inhibition of growth was due to epidermal growth factor alone. The increased expression of the ectoCa2+-ATPase was absolutely dependent on EGF, but also required hydrocortisone and cholera toxin. The characteristics of Li-7A cells make it a suitable system for studying both the mechanism of action of EGF and plasma membrane ATPases.
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PMID:Epidermal growth factor inhibits growth while increasing the expression of an ecto-Ca2+-ATPase of a human hepatoma cell line. 298 83

Ouabain uptake was studied on isolated rat hepatocytes. Hepatocellular uptake of the glycoside is saturable (Km = 348 mumol/l, Vmax = 1.4 nmol/mg cell protein per min), energy dependent and accumulative. Concentrative ouabain uptake is not present on permeable hepatocytes, Ehrlich ascites tumor cells and AS-30D ascites hepatoma cells. There is no correlation between ouabain binding to rat liver (Na+ + K+)ATPase and ouabain uptake into isolated rat hepatocytes. While ouabain uptake is competitively inhibited by cevadine, binding to (Na+ + K+)-ATPase is not affected by the alkaloid. Although the affinities of digitoxin and ouabain to (Na+ + K+)-ATPase are similar, digitoxin is 10000-times more potent in inhibiting [3H]ouabain uptake as compared to ouabain. That binding to (Na+ + K+)-ATPase appears to be no precondition for ouabain uptake was also found in experiments with plasmamembranes derived from Ehrlich ascites tumor cells and AS-30D hepatoma cells. While tumor cell (Na+ + K+)-ATPase is ouabain sensitive, the intact cells are transport deficient. Hepatic ouabain uptake might be related to bile acid transport. Several inhibitors of the bile acid uptake system also inhibit ouabain uptake.
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PMID:Transport functions of the liver. Lack of correlation between hepatocellular ouabain uptake and binding to (Na+ + K+)-ATPase. 298 94

A study was made of the ouabain effect (10(-3] on cell proliferation and the dependence of ATP hydrolysis on Na/K-concentration in homogenates of mouse hepatoma (XXIIa) and of L-cells, both sensitive and resistant to etidium bromide. Na+, K+-ATPase activity was found in homogenates of cells from sparse cultures in the presence of ouabain, the activity being stimulated by the Na/K-ratio pecular for the maximum enzymatic activity in cells from the dense cultures. The effect of ouabain on the cell proliferation is similar to the effect of transition of sparse cultures to dense ones.
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PMID:[Effect of ouabain on the Na+, K+-ATPase function and multiplication of transformed cells in culture]. 300 84

Mitochondrial ATPase and adenylate kinase activity of hepatoma cells were inhibited by hematoporphyrin derivative (HPD) followed by photoirradiation. Inhibition of ATPase activity was a dose- and time-related event. Malonaldehyde (MDA) content of mitochondrial membranes was markedly increased by HPD plus light. The content of mouse liver microsomal cytochrome P-450 was greatly increased after intraperitoneal injection of HPD for 4 days (5 mg/kg/day). The liver weight, and levels of liver microsomal G-6-phosphatase, MDA and triglyceride (TG) showed no difference in treated vs. control animals. The data presented here demonstrate that mitochondria may be a sensitive site of action of HPD photosensitization, and inactivation of ATPase and adenylate kinase may be an important contributing factor to tumor cell damage and death.
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PMID:Photosensitization of mitochondrial adenosine-triphosphatase and adenylate kinase by hematoporphyrin derivative in vitro. 300 50

The activities of several ATPases of the ascitic hepatoma cells in mice were compared. The activities of the total ATPase and mitochondrial Mg++-ATPase in normal liver cells were 50% and 140% higher than those in the hepatoma cells (P less than 0.001). However, the Na+, K+-ATPase activity in hepatoma cells was 170% higher than that in normal liver cells (P less than 0.01). The proportion of the activities of mitochondrial Mg++-ATPase, as well as Na+, K+-ATPase to their respective total ATPase in hepatoma cells was in disorder. The relation between the changes of the activity of different ATPases, their proportion and the abnormal metabolism as well as some characteristics of tumor cells are discussed.
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PMID:[Study on ATPase of tumor cells--I. A comparison of several ATPase activities]. 301 32

A polyclonal antibody to the catalytic subunit of rat kidney Na,K-ATPase has been raised in rabbits and used to analyze the turnover of the subunit in the rat hepatoma cell line HTC. It had been shown previously (Baumann, H., and Doyle, D. (1978) J. Biol. Chem. 253, 4408-4418) that the membrane proteins of these cells displayed multicomponent turnover kinetics, the minority of the surface proteins turning over with a half-time of about 20 h and the remainder with a half-time of about 100 h. That the antibody precipitated both the alpha (catalytic) and beta (glycosylated) subunits of the Na,K-ATPase from Triton extracts of HTC cells could be demonstrated following metabolic labeling of the cells with either [3H]leucine or a mixture of [3H] mannose and [3H]fucose, but following labeling with [35S]methionine radioactivity was found only in the alpha subunit of the precipitates. Incorporation of [35S]methionine into the alpha subunit could be detected 2 min after addition of the isotope to the cell suspension. Then and at all times thereafter the label was recoverable only from the particulate fraction of a 150,000 X g 60-min centrifugation; no labeled alpha subunit was ever detected in the supernatant fraction. By quantitative densitometry of radioautographs of sodium dodecyl sulfate-polyacrylamide gels of labeled antibody precipitates, it could be shown in pulse-chase experiments that the specific activity of the alpha subunit remained unchanged for 3-4 h (transit time) after the pulse was initiated and that the activity subsequently decayed exponentially with a half-time of 18 h. In a population growing with a generation time (tG) of 33 h, this decay corresponds to a turnover rate constant of 0.49/tG. The catalytic subunit is among those membrane proteins with a rapid turnover rate.
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PMID:Turnover of the catalytic subunit of Na,K-ATPase in HTC cells. 301 30

Molar ratio of cholesterol/phospholipids was decreased in Zajdela hepatoma cell membranes as compared with rat normal hepatocytes. Microviscosity of lipid bilayer was increased in membranes of normal and malignant cells, while the activity of Na+, K+-ATPase and 5'-nucleotidase was decreased during introduction of cholesterol into the cell membranes. As compared with control groups the duration of life was increased in the group of animals implanted with Zajdela hepatoma cells modified by cholesterol. The data obtained suggest that an increase in microviscosity of membranes in tumoral cells, enriched with cholesterol, might inhibit their mitotic divisions.
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PMID:[Incorporation and release of cholesterol from plasma membranes of hepatocytes and Zajdela hepatoma cells]. 302 83

cDNA complementary to mRNA coding for the beta subunit of dog renal (Na+ + K+)-ATPase has been cloned into lambda gt11 and the nucleotide sequence of the DNA has been determined. The amino acid sequence of the beta subunit polypeptide has also been deduced from the DNA. The mature form of the dog kidney beta subunit contains 302 amino acids with three potential asparagine-linked attachment sites for carbohydrate. The initiation methionine is removed during processing of the polypeptide to its mature form. Although the beta subunit is an integral membrane protein there is no signal sequence for the polypeptide, and hydropathy analysis predicts that the beta subunit polypeptide spans the cell membrane only once. Secondary structure predictions and a model for the structure of the beta subunit are proposed. DNA sequencing of the 5' non-coding region of the mRNA revealed a 200 bp inverted repeat from the coding region. Blot hybridization of a fragment of the beta subunit cDNA identified a single mRNA species of 2.7 kb in dog kidney and several rat tissues. RNA from rat liver was deficient in mRNA that hybridized to the dog kidney beta subunit cDNA, although mRNA that hybridized to an alpha subunit cDNA was detected. RNA from a human hepatoma cell line, HepG2, however, contained comparable levels of mRNA for both the alpha and the beta subunits.
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PMID:Molecular cloning and sequence analysis of the (Na+ + K+)-ATPase beta subunit from dog kidney. 303 Apr 34

A hepatocellular carcinoma cell line, LMH, has been established from a hepatocellular carcinoma induced in a male leghorn chicken by diethylnitrosamine. The cell line is characterized by well-differentiated morphological and biochemical features including the expression of glucose-6-phosphatase and canalicular ATPase activities and triploid karyotype with six marker chromosomes. The cells have been continuously propagated in culture for 5 yr and are now at about the 120th passage. Morphological change occurred in culture associated with gradual increase in growth rate at about the 40th passage. However, the biochemical and chromosomal features remained constant. This is the first established domestic fowl epithelial cell line and will allow comparative investigation of a number of parameters relevant to chicken hepatocarcinogenesis.
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PMID:Establishment and characterization of a chicken hepatocellular carcinoma cell line, LMH. 360 75


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