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)

Plasmid pSK-TTR was digested by BamHI and the DNA fragment containing Transthyretin gene was cloned into the BamHI site of vector pHIL-SI. The recombinant plasmid pHIL-SI-TTR was digested by BglII; the larger fragment was transformed into yeast Pichia pastoris. SDS-PAGE analysis showed that the yeast transformant can express and secrete TTR as a fusion protein, TTRF. To purify TTRF,the DEAE-Sepherose F.F. chromatography and Sephacryl S-200 chromatography were used. The in vitro test showed that TTRF could inhibit the growth of human hepatoma cells.
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PMID:Expression of transthyretin gene in Pichia pastoris. 1103 45

NF-IL6 (Nuclear factor for IL-6 expression) is involved in inflammatory reaction, expression of acute-phase proteins and cytokines, apoptosis and suppression of tumor cells, and maintenance of macrophage immunological functions. To investigate the role of highly expressed exogenous NF-IL6 in macrophage tumor cytotoxicity, a recombinant expression plasmid, pCN, which harbored the coding region of NF-IL6, was transfected into murine primary cultured peritoneal resident macrophages by an improved DEAE-dextran method. Western blot showed the high expression of NF-IL6 in these macrophages. Then the tumor cytotoxicity of the NF-IL6-overexpressing macrophages from normal and nude mice was measured by an alkaline phosphatase assay, using the human hepatocarcinoma cell line SMMC 7721 as target cells. Results showed that the overexpression of NF-IL6 enhanced the tumor cytotoxicity in both types of macrophages, demonstrating that the expression level of the NF-IL6 gene was directly related to the tumoricidal activity in these cells.
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PMID:Enhancement of Macrophage Cytotoxicity by Overexpression of Exogenous NF-IL6 Gene. 1205 86

A peptide, with a molecular mass of 9.5kDa and demonstrating an N-terminal sequence similar to ubiquitin, was isolated from fruiting bodies of the mushroom Agrocybe cylindracea. The peptide was isolated with a purification protocol involving ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, FPLC-ion exchange chromatography on Mono S and FPLC-gel filtration on Superdex 75. The peptide was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and Mono S. It showed antiproliferative activity on leukemia cell line (M1) and hepatoma cell line (HepG2), and enhanced nitric oxide production in murine peritoneal macrophages with a potency comparable to that of lipopolysaccharide. A pH of 6.0 was required for optimal RNase activity. Its RNase activity was stable over the temperature range of 0-60 degrees C. It exerted ribonucleolytic activity preferentially on polyC, much lower activity on polyU, and negligible activity on polyA and polyG.
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PMID:Purification and characterization of a ubiquitin-like peptide with macrophage stimulating, antiproliferative and ribonuclease activities from the mushroom Agrocybe cylindracea. 1289 48

A protein designated alliumin, with a molecular mass of 13 kDa and an N-terminal sequence similar to a partial sequence of glucanase, and demonstrating antifungal activity against Mycosphaerella arachidicola, but not against Fusarium oxysporum, was isolated from multiple-cloved garlic (Allium sativum) bulbs. The protein, designated as alliumin, was purified using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Mono S, affinity chromatography on Affi-gel blue gel, and gel filtration on Superdex 75. Alliumin was unadsorbed on DEAE-cellulose, but was adsorbed on Affi-gel blue gel, CM-cellulose and Mono S. Its antifungal activity was retained after boiling for 1 h and also after treatment with trypsin or chymotrypsin (1:1, w/w) for 30 min at room temperature. Alliumin was inhibitory to the bacterium Pseudomonas fluorescens and exerted antiproliferative activity toward leukemia L1210 cells. However, it was devoid of ribonuclease activity, protease activity, mitogenic activity toward mouse splenocytes, and antiproliferative activity toward hepatoma Hep G2 cells.
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PMID:Isolation of alliumin, a novel protein with antimicrobial and antiproliferative activities from multiple-cloved garlic bulbs. 1562 28

An antifungal peptide with a molecular mass of 9 kDa was isolated from fresh fruiting bodies of the mushroom Agrocybe cylindracea. The isolation procedure comprised ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and FPLC-gel filtration on a Superdex 75 column. The antifungal peptide, designated as agrocybin, was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. Agrocybin exerted antifungal activity against several fungal species but lacked inhibitory activity against bacteria when tested up to 300 microM. The activity of HIV-1 reverse transcriptase was attenuated in the presence of agrocybin. It exhibited weaker mitogenic activity than Con A on isolated murine splenocytes, but was devoid of antiproliferative activity on Hep G2 (hepatoma) cells when tested at 110 microM.
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PMID:Agrocybin, an antifungal peptide from the edible mushroom Agrocybe cylindracea. 1562 30

A homotetrameric agglutinin with a molecular mass of 130 kDa was isolated from seeds of the haricot bean. The agglutinin was isolated using a procedure that involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel and gel filtration by fast protein liquid chromatography on Superdex 200. Haricot bean agglutinin was adsorbed on DEAE-cellulose and Affi-gel blue gel. The hemagglutinating activity of the agglutinin was stable up to 40 degrees C. It underwent a 40% decline when the temperature was raised to 50 degrees C and a complete loss when the temperature was further increased to 80 degrees C. The hemagglutinating activity exhibited a time-dependent loss in activity when the agglutinin was incubated at 100 degrees C for different durations. No activity was discernible when the agglutinin was left at 100 degrees C for 1 min. The activity also underwent a decline in the presence of 500 mM FeCl(3) and CaCl(2). Haricot bean agglutinin manifested a weaker mitogenic activity than concanavalin A toward mouse splenocytes. It exhibited antiproliferative activity toward the tumor cell lines M1 [leukemia], HepG2 [hepatoma] and L1210 [leukemia] cells.
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PMID:A homotetrameric agglutinin with antiproliferative and mitogenic activities from haricot beans. 1624 45

A trypsin inhibitor, with an N-terminal sequence highly homologous to those of 8-kDa Bowman-Birk trypsin inhibitors, was isolated from the seeds of Hokkaido large black soybeans. The trypsin inhibitor was unadsorbed on SP-Sepharose but adsorbed on DEAE-cellulose and Mono Q. It inhibited proliferation in breast cancer (MCF-7) cells and hepatoma (Hep G2) cells with an IC50 of 35 and 140 microM, respectively. The trypsin inhibitory activity of the inhibitor was completely preserved after exposure to temperatures up to 100 degrees C for 30 min and to the pH range 2-13 for the same duration. The trypsin inhibitor inhibited HIV-1 reverse transcriptase with an IC50 of 38 microM, but was devoid of antifungal activity toward Fusarium oxysporum and Mycosphaerella arachidicola.
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PMID:A Bowman-Birk trypsin inhibitor with antiproliferative activity from Hokkaido large black soybeans. 1788 27

Recent studies have demonstrated that aldo-keto reductase family 1 B10 (AKR1B10), a novel protein overexpressed in human hepatocellular carcinoma and non-small cell lung carcinoma, may facilitate cancer cell growth by detoxifying intracellular reactive carbonyls. This study presents a novel function of AKR1B10 in tumorigenic mammary epithelial cells (RAO-3), regulating fatty acid synthesis. In RAO-3 cells, Sephacryl-S 300 gel filtration and DEAE-Sepharose ion exchange chromatography demonstrated that AKR1B10 exists in two distinct forms, monomers (approximately 40 kDa) bound to DEAE-Sepharose column and protein complexes (approximately 300 kDa) remaining in flow-through. Co-immunoprecipitation with AKR1B10 antibody and protein mass spectrometry analysis identified that AKR1B10 associates with acetyl-CoA carboxylase-alpha (ACCA), a rate-limiting enzyme of de novo fatty acid synthesis. This association between AKR1B10 and ACCA proteins was further confirmed by co-immunoprecipitation with ACCA antibody and pulldown assays with recombinant AKR1B10 protein. Intracellular fluorescent studies showed that AKR1B10 and ACCA proteins co-localize in the cytoplasm of RAO-3 cells. More interestingly, small interfering RNA-mediated AKR1B10 knock down increased ACCA degradation through ubiquitination-proteasome pathway and resulted in >50% decrease of fatty acid synthesis in RAO-3 cells. These data suggest that AKR1B10 is a novel regulator of the biosynthesis of fatty acid, an essential component of the cell membrane, in breast cancer cells.
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PMID:Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells. 1805 16

Ribosome inactivating proteins (RIPs) are enzymes that inactivate ribosomes by eliminating one or more adenosine residues from rRNA, a 9,567-Da RIP with a novel N-terminal sequence was isolated from fresh fruiting bodies of the mushroom Hypsizigus marmoreus. The protein was unadsorbed on DEAE-cellulose, adsorbed on Affi-gel blue gel, and appeared as a single peak upon gel filtration on Superdex 75. The protein, designated as marmorin, inhibited proliferation of hepatoma Hep G2 cells and breast cancer MCF-7 cells, HIV-1 reverse transcriptase activity, and translation in the rabbit reticulocyte lysate system with an IC50 of 0.15 microM, 5 microM, 30 microM, and 0.7 nM, respectively. Compared to RIPs from hairy gourd, bitter gourd, ridge gourd, garden pea, and the mushroom Flammulina velutipes, marmorin was more potent in its antiproliferative activity toward hepatoma (HepG2) and breast cancer (MCF-7) cells, similar in inhibitory potency toward HIV-1 reverse transcriptase (with the exception that it was more potent than ridge gourd RIP and bitter gourd RIP), and less potent in translation-inhibitory potency. Marmorin was devoid of antifungal, protease, RNase, mitogenic, anti-mitogenic, nitric oxide-inducing, hemagglutinating, and trypsin inhibitory activities.
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PMID:Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom Hypsizigus marmoreus. 1875 97

A protein exhibiting an N-terminal amino acid sequence with some similarity to imidazoleglycerol phosphate synthase was purified from fresh Capparis spinosa melon seeds. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, cation exchange chromatography on SP-Sepharose, and finally gel filtration by fast protein liquid chromatography on Superdex 75. The protein was adsorbed using 20 mM Tris-HCl buffer (pH 7.4) and desorbed using 1 M NaCl in the starting buffer from the DEAE-cellulose column and SP-Sepharose column. The protein demonstrated a molecular mass of 38 kDa in gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that it was monomeric. The protein inhibited proliferation of hepatoma HepG2 cells, colon cancer HT29 cells and breast cancer MCF-7 cells with an IC(50) of about 1, 40 and 60 microM, respectively. It inhibited HIV-1 reverse transcriptase with IC(50) of 0.23 microM. It inhibited mycelial growth in the fungus, Valsa mali. It did not exhibit hemagglutinating, ribonuclease, mitogenic or protease inhibitory activities.
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PMID:A protein with antiproliferative, antifungal and HIV-1 reverse transcriptase inhibitory activities from caper (Capparis spinosa) seeds. 1901 43


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