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)

We determined the activities of soluble and particulate guanylate cyclase [GTP pyrophosphatelyase (cyclizing); ?EC 4.6.1.2] IN REGENERATING RAT LIVER, FETAL AND NEONATAL RAT LIVER, AND HEPATOMA. TIn these tissues we found increased particulate and decreased soluble enzyme activities compared to normal adult rat liver. The particulate activity increased 12 hr after partial hepatectomy, reached maximal activity at 48 hr, and then declined. The soluble enzyme activity decreased within 8 hr and continued to decline. The activity of homogenates did not change. Guanylate cyclase activity was increased in plasma membrane and microsome fractions from regenerating liver. The increase in particulate activity was prevented with cycloheximide. Decreased soluble and increased particulate enzyme activities were found in fetal liver. After birth the soluble activity increased and the particulate activity decreased. Seven to 14 days after birth the activities of soluble and particulate fractions were similar to those of adult rat liver. In hepatoma 3924A, the activity of particulate guanylate cyclase was 9-fold greater and that of the soluble enzyme was 50% that of normal liver. These studies suggest that guanylate cyclase activity and its subcellular distribution may be related to liver growth through some unknown mechanism.
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PMID:Increased particulate and decreased soluble guanylate cyclase activity in regenerating liver, fetal liver, and hepatoma. 23 4

HYBRIDS FROM A CROSS OF RAT HEPATOMA CELLS WITH DIPLOID EPITHELIAL CELLS FROM RAT LIVER HAVE BEEN STUDIED WITH RESPECT TO KARYOTYPE AND EXPRESSION OF TWO FUNCTIONS LIMITED TO THE HEPATOMA PARENT: high level of the enzyme tyrosine aminotransferase (EC 2.6.1.5; L-tyrosine:2-oxoglutarate aminotransferase) and its inducibility with steroid hormones. The hybrids that contain the complete chromosomal complements from both parents show low enzyme activity and no inducibility. One hybrid clone, and all of its derivatives, which have lost 30-40% of the chromosomes initially present, show enzyme inducibility. Induction of tyrosine aminotransferase in the hepatoma and hybrid cells responds similarly to inhibition by cycloheximide and actinomycin D, and to steroid concentration. The enzymes from induced and noninduced hepatoma cells and from induced hybrid cells are similar in heat sensitivity and intracellular distribution; those from noninduced hybrid and diploid rat epithelial cells are different.
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PMID:Expression of differentiated functions in hepatoma cell hybrids: reappearance of tyrosine aminotransferase inducibility after the loss of chromosomes. 439 33

The sequence of the 5'-flanking region of the rat Mrp3 gene was determined up to 2723 bp upstream of the translation start site. Regulatory regions crucial for Mrp3 promoter activity were characterized between -157 and -106 bp in hepatoma cells. Within this sequence we identified putative binding sites for C/EBP and Sp1. EMSA and supershift assays demonstrated specific binding of Sp1, Sp3, C/EBPalpha, beta, and delta. In Drosophila SL2 cells, both Sp1 and Sp3 transactivated the Mrp3 minimal promoter (pWT-157). Structural and functional analysis demonstrated that binding sites for C/EBPs, Sp1 and Sp3 were essential for transcription of the rat Mrp3 gene in Mrp3-expressing cells (including: H4IIE, H4IIE C3, BRL 3A, Clone 9, and RAT 2). Cotransfection assays demonstrated that C/EBP transcription factors modulated the basal and tissue specific activity of the Mrp3 gene promoter by recognition of the C/EBP (-157/-140) element and through functional cooperation with factors interacting with the Sp1 (3) and Sp1 (4) (-140/-106) cis-acting elements. In this study, we found C/EBPs and Sp1/Sp3 cooperatively regulated the promoter activity of rat Mrp3 gene through proximal (-157/-106) region. It suggested another fine-tune regulation mechanism may involve in Mrp3 gene expression.
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PMID:Transcriptional regulation of the rat Mrp3 gene promoter by the specificity protein (Sp) family members and CCAAT/enhancer binding proteins. 1613 17