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)

Transfection of sense cDNA of N-acetylglucosaminyltransferase V (GnTV) into H7721 human hepatocellular carcinoma cells resulted in the decreased expression of surface sialyl Lewis X (SLe(x)), a sialylated fucose-containing antigen. The enzymatic mechanisms were speculated to be the concomitantly decreased expression of alpha1,3-fucosyltransferase (FucT)-III, -VI, -VII and the branching enzyme of O-glycans, core 2-beta1,6-N-acetylglucosaminyltransferase (C2GnT)-I, -II. These two glycosyltransferase families were suggested to be the key enzymes in the synthesis of SLe(x). The expression of alpha2,3-sialyltransferase (ST3)-IV, but not ST3-I, -II and -III was elevated by sense GnTV. However, it did not cause the increase of SLe(x) synthesis. Transfection of antisense GnTV into H7721 cells showed entirely opposite effects on the expression of above-mentioned SLe(x) and glycosyltransferases as the sense GnTV.
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PMID:Effect of N-acetylglucosaminyltransferase V on the expressions of other glycosyltransferases. 1504 7

To establish the zebrafish as a model to investigate drug metabolism through sulfation, we had previous cloned, expressed, and purified fourteen distinct zebrafish cytosolic sulfotransferases (SULTs). In the present study, we carried a systematic analysis of the sulfating activities of these fourteen zebrafish SULTs toward a panel of drug compounds. Results showed that four of the fourteen zebrafish SULTs showed no detectable activities toward any of the tested drugs. Among the other ten zebrafish SULTs, three SULT1 enzymes (SULT1 ST1, SULT1 ST2, and SULT1 ST3) displayed considerably stronger activities than the others toward the majority of the drug compounds tested. Specifically, SULT1 ST1, SULT1 ST2, and SULT1 ST3 showed the highest specific activities, at 26.9, 29.3, and 31.5 nmol/min/mg, toward aesculetin, 4-methylembelliferone, and dobutamine, respectively. To further investigate the sulfation of tested drugs by the responsible zebrafish SULT enzymes, the kinetics of the sulfation reactions were analyzed. Kinetic constants determined indicated that the sulfation of these drugs by the SULT enzymes tested is likely to be physiologically relevant. A metabolic labeling experiment using cultured zebrafish liver cells and HepG2 human hepatoma cells was performed. Results showed that zebrafish liver cells displayed a similar pattern of sulfation of the drugs tested as that of HepG2 cells, implying that human and zebrafish liver cells may share considerable similarities with regard to their constituent drug-sulfating SULT enzymes.
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PMID:Sulfation of drug compounds by the zebrafish cytosolic sulfotransferases (SULTs). 2044 11