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)

The localization of cardiolipin biosynthesis in rat hepatoma 27 and Jensen sarcoma cells was investigated. In both tumors cardiolipin was found to be synthesized only in the mitochondria as is the case in normal rat liver. It is concluded that the occurrence of cardiolipin in the microsomes of the tumor cells may be connected with a transmembrane exchange of phospholipids in vivo.
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PMID:[Biosynthesis of cardiolipin in the rat hepatoma 27 and Jensen sarcoma]. 19 37

The N-[p-(fluorosulfonyl)benzyl] derivatives of L-asparagine and L-glutamine (1a,b) were synthesized as potential inhibitors of L-asparagine synthetase (ASase). Condensation of p-(fluorosulfonyl)benzylamine (2) with the suitably protected amino acid in the presence of dicyclohexylcarbodiimide, followed by deblocking, afforded 1a and 1b. Derivatives 1a and 1b at 10 mM inhibit ASase isolated from Novikoff hepatoma (rats) by 60 and 46%, respectively. Preliminary results on inhibition of Jensen sarcoma (L-asparaginase sensitive) and JA-1 sarcoma (L-asparaginase resistant) tissue cultures by 0.3 mM 1a (139,90%) and 1b (101, 103%), respectively, are discussed.
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PMID:Potential inhibitors of L-asparagine biosynthesis. 3. Aromatic sulfonyl fluoride analogs of L-asparagine and L-glutamine. 24 24

A full-length cDNA clone of the human pregnancy zone protein (PZP) was cloned from the hepatocellular carcinoma cell line Hep3B. Based on the exon sequences of the PZP gene (Devriendt et al. (1989) Gene 81, 325-334; Marynen et al., unpublished data), primer pairs were designed to amplify six overlapping fragments of the PZP cDNA. The obtained cDNA is 4609 bp long and contains an open reading frame coding for 1482 amino acids, including a signal peptide of 25 amino acid residues. Comparison with the published partial PZP amino acid sequence (Sottrup-Jensen et al. (1984) Proc. Natl. Acad. Sci. USA 81, 7353-7357) and the PZP genomic sequences confirmed the identity as a PZP cDNA. 71% of the corresponding amino acid residues in PZP and human alpha 2-macroglobulin (alpha 2M) are identical and all cysteine residues are conserved. A typical internal thiol ester site and a bait domain were identified. A Pro/Thr polymorphism was identified at amino acid position 1180, and an A/G nucleotide polymorphism at bp 4097.
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PMID:Primary structure of pregnancy zone protein. Molecular cloning of a full-length PZP cDNA clone by the polymerase chain reaction. 198 98

The effects of acute diabetes mellitus on the growth of Morris hepatoma 7288CTC and Jensen sarcoma were studied in fed, young (less than 200 g), and adult (greater than 250 g) rats. Animals were matched for tumor size and growth; the rates of tumor growth were the same in fed, young and adult nondiabetic rats. Diabetes was induced by the i.v. injection of streptozotocin (65 mg/kg total body weight) into tumor-bearing rats and changes in arterial blood nutrient concentrations were compared to changes in the rates of tumor growth and DNA synthesis. In young rats acute diabetes did not increase the blood concentrations of the fat store-derived nutrients and did not increase the rate of tumor growth. In adult rats, however, acute diabetes raised the arterial blood free fatty acid, glycerol, triglyceride, and ketone body concentrations to high levels and increased the rate of tumor growth about three times over that observed in untreated rats. Progress curves for the mobilization of host fat stores and for incorporation of [methyl-3H]thymidine into tumor DNA during the onset of diabetes showed that these activities were closely correlated in adult rats. Both processes began to increase 2 to 4 h after streptozotocin treatment, reached an initial peak at 12 to 16 h, decreased to a low point at 18 to 20 h, and then increased again to the new steady state after 23 to 24 h. The results indicate that the rate of tumor growth in rats in vivo is limited by the availability of a substance(s) present in the hyperlipemic blood of adult diabetic rats. The tight relationship between host lipolysis and tumor growth suggests that the substance(s) is derived from host fat stores.
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PMID:Stimulation of tumor growth in adult rats in vivo during acute streptozotocin-induced diabetes. 381 72

These experiments were designed to determine the characteristics of lactic acid utilization and production in vivo in Jensen sarcoma and Morris hepatoma 7288CTC. Arteriovenous differences for lactic and pyruvic acids, glucose, and the ketone bodies were measured across "tissue-isolated" tumors growing in fed and fasted rats. Lactic acid was utilized (n = 18), produced (n = 24), or neither utilized nor produced (n = 1) by the tumors. Net tumor lactate production or utilization did not depend on the mean rate of glucose utilization which was the same in the lactate-utilizing and -producing tumors. For the lactic acid-utilizing tumors, the mean arterial whole blood lactate concentration entering the tumor was 3.47 +/- 0.39 mM, and the concentration in the tumor venous blood was 2.31 +/- 0.25 mM. For the lactic acid-producing tumors, the mean arterial lactic acid concentration was 1.29 +/- 0.10 mM, and the tumor venous blood concentration was 2.19 +/- 0.19 mM. Thus, both lactate-producing and lactate-utilizing tumors showed identical rates of glucose utilization and identical lactic acid concentrations in the venous blood leaving the tumors. Metabolite levels were also measured in tumors that were freeze clamped in situ immediately following collection of the arterial and tumor venous blood samples. The lactic acid content in the tumor mass (corrected for total tumor water) and the concentration in the tumor venous blood plasma were nearly identical, suggesting that the lactate concentrations in the tumor cells and tumor venous blood are at equilibrium. Transport of lactic acid between arterial plasma and tumor or between tumor and venous plasma was always down a concentration gradient; net lactate uptake and release in these tumors followed the law of mass action. High lactate concentrations were not observed in the Jensen sarcomas or in the venous blood leaving these tumors, and we were unable to confirm earlier studies indicating that Jensen sarcomas are consistently high net lactate producers in vivo.
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PMID:In vivo lactate production and utilization by Jensen sarcoma and Morris hepatoma 7288CTC. 394 Jun 35

Rabbit antiserum against alkali-insoluble nuclear residual protein of transplantable rat hepatoma 27 reacted with residual proteins during immunodiffusion in agarose gel, provided immunoprecipitation of isolated nuclei and indirect immunofluorescence with Zajdela's rat ascites hepatoma and mouse ascites hepatoma 22a, while the reaction with non-liver tumors--rat Jensen, Yoshida and M 1 sarcomas and mouse Ehrlich ascites carcinoma was negative. Mild indirect immunofluorescence with kidney and spleen sections was eliminated if antiserum was preincubated with acetone powders of these tissues.
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PMID:[Immunologic similarity of antigens of residual nuclear proteins from various hepatomas]. 618 89

The interaction of postmicrosomal supernatants from the Jensen sarcoma, sarcoma 45, nephroma RA, normal, regeherating and fetal rat livers with antisera to the sphingomyelin exchange protein isolated from hepatoma 27 was studied by double immunodiffusion. It was shown that this protein is present in comparable amounts in all the tumours tested and in fetal rat liver, whereas in normal and regenerating liver its content is negligible. Based on the correlation between the content of sphingomyelin exchange protein in cell cytosols and the amount of sphingomyelin in the corresponding mitochondria it is suggested that this protein is responsible for the presence of sphingomyelin in mitochondria.
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PMID:[Immunological detection of sphingomyelin exchange protein in tumors and in embryonic rat liver]. 627 81

A marked difference in polypeptide pattern and electron micrographs of the nuclear residual protein fraction between normal tissues /liver, kidney, spleen/ and tumors /hepatoma 27, Jensen and Yoshida sarcomas/ is revealed. While in normal tissues the polypeptides with molecular weight lower than 26 KD constituted about one half of the total residual protein, in tumors the polypeptides with molecular weight exceeding 100 KD were markedly prevailing. In electron micrographs the uniform filaments with a diameter of 4-5 nm, and periodical structure represented the bulk of the preparation from normal liver, while in the case of hepatoma 27 an amorphous granulated material was predominating.
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PMID:[Protein composition and electron microscopy of the residual protein fractions of cell nuclei of certain normal organs and tumors of rats]. 745 74