Comparison of the induction of a 4S beta-naphthoflavone-binding protein, cytochrome P450 1A1 and NAD(P)H:quinone oxidoreductase in beta-naphthoflavone-treated rats.
A profound induction of a 4S beta-naphthoflavone (BNF)-binding protein, cytochrome P450 1A1 (CYP1A1) and NAD(P)H:quinone oxidoreductase (NQO1) activities was determined in the livers of Sprague-Dawley rats following intraperitoneal administration of BNF. Time-course of this induction differed for CYP1A1 and NQO1 activities, suggesting independent regulation of the phase I and II enzymes of xenobiotic metabolism. Time-course of the induction of CYP1A1 and BNF-binding activities was similar, suggesting that regulation of a 4S BNF- binding protein is associated with that of the CYP1A1 enzyme activity. The BNF specific binding to a 4S protein was inhibited by exogenous (BNF) and endogenous (indirubin and indigo) ligands for the aryl hydrocarbon receptor.
Institute of Human Genetics, Polish Academy of Sciences, ul. Strzeszyńska 32, 60-479 Poznań, Poland. brauzdam@man.poznan.pl
Damian
D
Brauze
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D019363:Cytochrome P-450 CYP1A1 / Q000096:biosynthesis*; D003600:Cytosol / Q000187:drug effects / Q000201:enzymology; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D005260:Female; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000096:biosynthesis*; D011485:Protein Binding; D051381:Rats; D017207:Rats, Sprague-Dawley; D013047:Specific Pathogen-Free Organisms; D013997:Time Factors; D019324:beta-Naphthoflavone / Q000494:pharmacology*
D002352:Carrier Proteins; D004791:Enzyme Inhibitors; D019324:beta-Naphthoflavone; D019363:Cytochrome P-450 CYP1A1; D016660:NAD(P)H Dehydrogenase (Quinone)