6533b854fe1ef96bd12af60a
RESEARCH PRODUCT
Xenobiotic-metabolizing enzyme activities in hybrid cell lines established by fusion of primary rat liver parenchymal cells with hepatoma cells
D. UteschE. PetzingerMichael ArandFranz OeschHelmut Thomassubject
Male1303 BiochemistryHealth Toxicology and Mutagenesis10050 Institute of Pharmacology and Toxicology610 Medicine & healthHybrid CellsToxicologyBiochemistryCell LineMixed Function OxygenasesXenobioticsCell FusionRats Sprague-Dawleychemistry.chemical_compoundLiver Neoplasms Experimental2307 Health Toxicology and MutagenesisTumor Cells CulturedAnimalsEnzyme inducerEpoxide hydrolasePharmacologychemistry.chemical_classificationbiologydigestive oral and skin physiologyCytochrome P4503005 ToxicologyGeneral MedicineGlutathioneRatsEnzyme3004 PharmacologychemistryBiochemistryLiverCell cultureEnzyme inhibitorbiology.proteinMicrosome570 Life sciences; biologydescription
1. The activities of xenobiotic-metabolizing enzymes were determined in hybrid cell lines (hepatocytoma, HPCT) which have been established by fusion of liver parenchymal cells from adult rat (PC) with cells from a Reuber hepatoma cell line (FAO). 2. Cytochrome P450 was not measurable spectrophotometrically in FAO and HPCT. P450-dependent conversion of testosterone was below the detection limit in FAO and only marginally present in HPCT. 3. Microsomal and cytosolic epoxide hydrolase, glutathione S-transferase and phenol sulphotranserase were low or even below detection limit in FAO. These enzyme activities were significantly higher in HPCT and correspond to about 1-10% the activities measured in PC. 4. 1-Naphthol UPD-glucuronosyl transferase activity was about 20% in FAO and about 100% in HPCT compared to PC. 5. Metabolic conversion of benzo[a]pyrene was low in FAO, high in PC, and intermediate in HPCT. The presented data, however, do not allow the conclusion whether this intermediate rate is catalyzed by similar P450 isoenzymes as in PC. 6. Due to the easily measurable phase II-metabolizing enzyme activities HPCT may, however, be useful for in vitro enzyme induction or repression studies.
year | journal | country | edition | language |
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1992-12-01 |