Acetone-dependent regulation of cytochrome P-450j (IIE1) and P-450b (IIB1) in rat liver.
1. Concomitant changes in the concentration of P450 IIB1 (P-450b) and the rate of O-depentylation of 7-pentoxyresorufin was observed in rat liver microsomes after a single intragastric dose of acetone. 2. In contrast the concentration of P450 IIE1 (P-450j) did not coincide with changes in the rate of P450 IIE1-dependent p-nitrophenol hydroxylation or metabolic activation of carbon tetrachloride. 3. Quantification of the proteins in lysosomes indicated that both P450 IIB1 and P450 IIE1 are degraded via an autophagosomal/autolysosomal pathway. 4. It is concluded that P450 IIE1 is catalytically inactivated in microsomes prior to the degradation of this protein.
Ronis
M J
MJ
Department of Physiological Chemistry, Karolinska Institute, Stockholm, Sweden.
Ingelman-Sundberg
M
M
D000096:Acetone / Q000494:pharmacology*; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis*; D004790:Enzyme Induction; D007527:Isoenzymes / Q000096:biosynthesis*; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects*; D006899:Mixed Function Oxygenases / Q000096:biosynthesis*; D051381:Rats; D011919:Rats, Inbred Strains
D007527:Isoenzymes; D000096:Acetone; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases