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)

Mallory bodies (MBs) were isolated from the livers of 8 alcoholic patients and a malignant hepatoma occurring in a non-alcoholic patient. MBs were isolated in large quantity and high purity. The isolates were devoid of liver cell organelles except in the case of malignant hepatoma where dense and membranous material resembling nuclear substances and endoplasmic reticulum were found. The "nuclear" material had continuity with MBs. Electron microscopic examination suggested the presence of a dense body and very fine filaments within in situ and isolated MBs in addition to the tubular structure of so-called MB fibers. Amino acid analysis indicated that the major component of MBs is a protein which does not contain unusual amino acids or any particular amino acid in a large quantity to characterize this protein. The isolated fractions were solubilized in 6 M guaindine hydrochloride by sonication or in 1% sodium dodecyl sulfate (SDS) with 2 mercaptoethanol and 8 M urea. The solubilized MB protein produced 3 peaks by Sephadex G 100 chromatography and at least five intense protein bands by SDS polyacrylamide gel electrophoresis. Serum sample and the fractions from control livers contained several protein bands which were similar to the major components of isolated MB protein. These morphological and biochemical findings suggest that MBs are not homogeneous protein, but they are probably complexes of various proteins and that some components of MBs are present in normal hepatocytes.
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PMID:A study on Mallory bodies. Isolation, ultrastructure and preliminary biochemical characterization of Mallory bodies from livers of alcoholic cirrhosis and malignant hepatoma. 18 65

The rates of urea synthesis in rat liver and in a series of rat liver neoplasms with widely different growth rates and degree of differentiation were investigated using tissue slices incubated in a Krebs-Ringer bicarbonate buffer. Urea synthesis did not occur in fast-growing, poorly differentiated Novikoff and Morris 3924A hepatomas, but it did occur in slow-growing, well- and highly differentiated hepatomas; however, there was no correlation with growth rate or degree of differentiation. Urea synthesis was comparable with normal liver, at about 32 mumoles/hr/g tissue, in the slow-growing Morris hepatomas 21, 28A, 47C, and 44; but it was very low in two other slow-growing, highly differentiated hepatomas, 9618A and 20. The well-differentiated Morris hepatoma 5123C had intermediate levels of urea synthesis. This pattern of urea synthesis closely paralleled the previously reported activity of carbamyl phosphate synthetase in these tumors. The rate of urea synthesis was normal in livers of Buffalo rats bearing fast- or slow-growing hepatomas in low urea synthesis rates, but it was markedly lowered in the livers of rats bearing large, slow-growing tumors with high urea synthesis rates. Urea synthesis in liver declined as the tumors increased in size. The total rate of urea synthesis in liver and tumor, as well as the concentrations of urea in the serum and urine of tumor-bearing animals, remained remarkably constant throughout the period of tumor growth, suggesting the existence of a homeostatic mechanism that controls the urea cycle activity in accordance with the synthetic activity of the tumor. In parabiotic animals, carbamyl phosphate synthetase activity and urea synthesis were lowered in the host livers of partners bearing tumors with high carbamyl phosphate synthetase- and urea-synthetic activity, but there was no significant effect on urea cycle activity in the normal partners. This result discounts the likelihood of a circulating humoral factor that controls hepatic urea cycle activity.
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PMID:Urea synthesis in Novikoff and Morris hepatomas. 18 16

A novel alkaline phosphatase differing from the so-called liver-specific isoenzyme was found in four out of twenty-four normal adult livers. Although the mobility of this enzyme was the same as that of so-called liver-specific alkaline phosphatase on the polyacrylamide gel electrophoretogram, its mobility was not altered following neuraminidase treatment, while that of the liver-specific enzyme was affected by the same treatment. Both enzymes also differed in other enzymatic and immunologic properties. The enzyme, however, resembled the so-called intestinal alkaline phosphatase in many enzymatic and immunologic properties. Thus, the inhibition patterns by amino acids, EDTA and inorganic phosphate, the pH optima, KM values for phenyl phosphate and reactivity with anti-intestinal alkaline phosphatase antibody were quite similar for both enzymes. Differences in the properties of this enzyme and intestinal alkaline phosphatase were in sensitivity to denaturation by treatment with heat and urea and to inhibition by Levamisole. The possible origin of the enzyme in normal liver and its relationship to the Kasahara isoenzyme and fetal intestine-type in hepatoma is discussed.
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PMID:A novel alkaline phosphatase, a minor component of normal liver phosphatases. 20 20

A membrane-bound arylamidase from well-differentiated hepatocellular carcinoma having the same electrophoretic mobility as placental membrane-bound arylamidase was found. The enzyme was found to be a sialoprotein and was activated by Co2+. Hepatoma membrane-bound arylamidase had a similar molecular weight (240 000) and kinetic properties to normal liver membrane-bound arylamidase, but differed from the liver enzyme with respect to electrophoretic mobility, heat stability and urea inactivation.
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PMID:Membrane-bound arylamidase from human hepatoma cells having the same electrophoretic mobility as placental membrane-bound arylamidase. 20 22

Protein 64/7.2 (molecular weight/isoelectric point) is present in the cytosol of several hepatomas including the Novikoff hepatoma and Morris hepatomas 9618A, 7794A, and 3924A, but it is not present in liver or 18-hr regenerating liver. Quantitatively, its concentration was highest in Novikoff hepatoma (150 microgram/g tissue) and Morris hepatoma 3924A (550 microgram/g tissue), which are rapid-growing tumors, less in Morris hepatoma 7794A (72 microgram/g tissue), which is of intermediate growth rate, and least in the slow-growing Morris hepatoma 9618A (25 microgram/g tissue). Protein 64/7.2 was isolated from Novikoff hepatoma ascites cells in high purity as shown by its migration as a single band on one-dimensional acid-urea-polyacrylamide gels and a single spot on two-dimensional isoelectric focusing sodium dodecyl sulfate-polyacrylamide gels. Its amino acid composition has an acidic to basic amino acid ratio of 1.6. Its amino-terminal amino acid is lysine, and its carboxyl-terminal amino acid is glycine. Interestingly, the amino acid composition is strikingly similar to that of the phosphorylated Novikoff hepatoma chromatin Protein Cg', partially characterized in our laboratory.
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PMID:Isolation and characterization of a cytosol protein (64/7.2) present in large amounts in rapidly growing hepatomas. 20 17

Ferritin was purified from normal, fetal, and malignant liver tissue. Ferritin purified from hepatoma tissue migrated slightly faster than normal human liver ferritin in polyacrylamide gel electrophoresis. Hepatoma and fetal liver ferritin contained an acidic components in gel and liquid isoelectric focusing not found in normal liver ferritin. We have called it a carcinofetal isoferritin. The subunit compositions of ferritins purified from human liver cell carcinoma and normal liver were then compared. Both ferritin consisted of a subunit species with an identical molecular weight of approximately 18,500. A single subunit of similar molecular weight was also demonstrable after dissociation of 8 M urea and by gel filtration in urea. Two subunits were demonstrable in normal liver ferritin by means of acrylamide electrophoresis in 8 M urea in acid pH. The same two subunits were also demonstrable in ferritin isolated from human liver cell carcinoma. However, a third subunit, intermediate in charge between the two normal liver subunits, was demonstrable in different amounts in ferritins from two hepatomas. Ferritins from normal and malignant livers were immunologically indistinguishable. The tumor-specific acidic isoferritin was isolated and antisera were prepared. The isolated acidic isoferritin was found to be immunologically identical to normal liver isoferritins. It is concluded that the multiple isoferritins of the human liver ferritin consist of two subunits, which are identical in molecular weight but which differ in net charge. Ferritin, isolated from two human liver carcinoma tissues, was composed of the same two subunits and a third unique subunit. Different amounts of these subunits may account for the several normal isoferritins and a unique tumor-specific acid isoferritin found in hepatoma.
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PMID:Characterization and subunit analysis of ferritin isolated from normal and malignant human liver. 23 22

The nature of nuclear proteins that are soluble in 8 M urea-50 mM phosphate, pH 7.6, was compared in rat liver and Morris hepatomas, Isoelectric focusing, using carrier ampholytes for a pH gradient of 3.5 to 10, indicated that with increasing growth rate of the hepatomas there was a progressive tendency for a decrease in nonhistone nuclear proteins with isoelectric points in the range 7.5 to 8.9 and an increase in the range 5.1 to 6.7. Studies on the influence of time on the pH gradient revealed that a nonuniform drift provided a better resolution of the pH range 7.5 to 8.9 at 7 hr than at 24 hr, while the latter time for electrofocusing gave an improved resolution of the pH range 5.1 to 6.7 Polyarcylamide gel electrophoresis in a urea-acetic acid system showed that 8 M urea-50 mM phosphate; pH 7.6 extracted a small part of the histones from nuclei of both liver and hepatomas. There was less extraction of histones from the hepatoma nuclei, especially in two rapidly growing hepatomas with the most notable difference being seen in the lysine-rich H1 histone. The results suggested that in addition to qualitative or quantitative changes in nonhistone nuclear proteins in liver cancer there are alterations in the binding of histones to chromatin.
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PMID:Nuclear protein changes in rat hepatomas correlating with growth rate. 23 25

Normal rat hepatocytes have been fused with highly differentiated rat hepatoma cells. Some of the hybrids express a physiologically significant level of activity of the urea cycle enzyme ornithine carbamoyltransferase (OCT), a liver-specific function not found in the hepatoma cells. These hybrids have 10% of the adult rat liver OCT specific activity, incorporate 3H-ornithine into protein arginine, and can be selectively grown in arginine-free medium supplemented with ornithine. Somatic cell hybridization of normal differentiated cells with highly differentiated neoplastic cells of the same tissue type may be useful as a general method for obtaining permanent cell lines with new tissue-specific phenotypes.
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PMID:Immortalization of normal liver functions in cell culture: rat hepatocyte-hepatoma cell hybrids expressing ornithine carbamoyltransferase activity. 48 65

Pyridine N-oxides having 1-(2-chloroethyl)-1-nitrosoureidoalkyl or 1-methyl-1-nitrosoureidoalkyl groups were evaluated for their antitumor activity against AH13 hepatoma and L1210 leukemia. Among them, 1-(2-chloroethyl)-1-nitroso-3-(2-pyridylmethyl)urea N-oxide (1), its tosylate (2), 1-(2-chloroethyl)-1-nitroso-3-(2-pyridylethyl)urea N-oxide (4), and 1-(2-chloroethyl)-1-nitroso-3-(3-pyridylmethyl)urea N-oxide (6) were highly active against both tumors in ip-ip system. These compounds were also active in ip-iv and ip-po systems of L1210. On the other hand, pyridine N-oxides having 1-methyl-1-nitrosoureidoalkyl group were all inactive against AH13 and weakly active against L1210. Effect on blood cells in Donryu rats bearing EDEN-5 erythroblastic leukemia cells was tested with these 1-(2-chloroethyl)-1-nitrosoureidoalkylureas. These compounds caused leucopenia and compound (4) was only slightly effective against EDEN-5.
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PMID:Antitumor effect of pyridine N-oxides having 1-(2-chloroethyl)-1-nitrosoureidoalkyl and 1-methyl-1-nitrosoureidoalkyl groups. 53 84

A nucleolar chromatin antigen (NoAg-1) found in Novikoff hepatoma but not in normal liver has been purified to homogeneity as shown by two-dimensional gel electrophoresis. Initial purification of NoAg-1 was partially achieved by isolation of nucleolar chromatin and fractionation of its proteins by successive extraction with solutions of increasing salt concentration. Further purification of this antigen was achieved by affinity and hydroxylapatite chromatography. Although approximately 50% of the NoAg-1 antigen was in the 0.6 M NaCl extract of Novikoff nucleoli, it was less pure than in the 2 M NaCl:5 M urea extract which contained 25% of the NoAg-1 at a purity of 40%. The highly purified NoAg-1 had an approximate molecular weight of 60,000 and pl of 5.1; the yield of NoAg-1 was 0.22% of the total nucleolar proteins.
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PMID:Purification and partial characterization of nucleolar antigen-1 of the Novikoff hepatoma. 76 Nov 99


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