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)

Nucleotide sugars derived from 5-fluorouridine were studied in cultured AS-30D hepatoma cells as well as in kinetic enzyme assays in vitro in comparison with the physiologic uridine diphospho sugars. Hepatoma cells converted 5-fluoro [14C]uridine to 5-fluorouridine diphospho (FUDP) glucose, FUDP-galactose, FUDP-N-acetylglucosamine, FUDP-N-acetylgalactosamine, and trace amounts of FUDP-glucuronate, as analyzed by different systems of high-performance liquid chromatography. 5-Fluoro[14C]uridine and [14C]uridine, at concentrations of 5 microM in the culture medium, were phosphorylated by the cells during 60 min to similar amounts of FUTP and UTP, respectively, while the synthesis of [14]FUDP-sugars was reduced to 14% as compared to that of [14C]UDP-sugars. FUDP-sugars, synthesized by chemical and enzymatic procedures, were assayed in vitro as substrates for enzymes of UDP-sugar metabolism. Km and V values in a range comparable to that of the respective UDP-sugars were determined for FUDP-sugars in the reactions catalyzed by UDP-glucose pyrophosphorylase, galactose-1-phosphate uridylyltransferase, UDP-glucose 4-epimerase, UDP-N-acetylglucosamine 2-epimerase, glycogen synthase, and UDP-glucose dehydrogenase. Our experiments in hepatoma cells and with enzymes in vitro have revealed additional reactions of FUDP-sugar metabolism demonstrating a metabolite pattern analogous to that of UDP-sugars. The amounts of FUDP-sugars formed relative to UDP-sugars in intact cells were smaller than suggested on the basis of their kinetic comparison in vitro.
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PMID:Substrate properties of 5-fluorouridine diphospho sugars detected in hepatoma cells. 646 51

UDP-N-acetylglucosamine 2'-epimerase was partially purified from Yoshida sarcoma, a strain of rat ascites hepatoma, by (NH4)2SO4 precipitation followed by TEAE-cellulose chromatography. The purified enzyme was inhibited by CMP-N-acetylneuraminic acid to similar extent to partially purified rat liver 2'-epimerase. Although the two enzymes were also similar in Km for UDP-N-acetylglucosamine, they were differentiated by chromatography on TEAE-cellulose, DEAE-Sephadex and hydroxyapatite, tumor enzyme being less tightly bound to these columns than liver enzyme. Similar chromatographic difference was also noted between 2'-epimerases of mouse liver and mouse Ehrlich asites carcinoma.
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PMID:UDP-N-acetylglucosamine 2'-epimerase of rat hepatoma and its comparison with the enzyme of rat liver. 741 4