Lanosterol 14α-Demethylase (Cytochrome P-45014DM) : Modulation of Its Enzyme Activity by Cholesterol Feeding

• Published in: Biological & pharmaceutical bulletin Vol. 18; no. 7; pp. 1009 - 1011
• Main Authors: SONODA, Yoshiko, AMANO, Chiyuki, ENDO, Masayuki, SATO, Yoshihiro, SEKIGAWA, Yoshio, FUKUHARA, Morio
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 01.07.1995; Maruzen
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; cholesterol; Cholesterol, Dietary - pharmacology; Cytochrome P-450 Enzyme Inhibitors; cytochrome P-45014DM; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Immunoblotting; In Vitro Techniques; lanosterol 14α-demethylase; Liver - drug effects; Liver - enzymology; Male; modulation; NADPH-Ferrihemoprotein Reductase - metabolism; Oxidoreductases; Oxidoreductases - antagonists & inhibitors; Phosphoric Monoester Hydrolases - pharmacology; phosphorylation; Rats; Rats, Wistar; Sterol 14-Demethylase; Phosphorylation; Rat; Isozyme; Cytochrome P450; Rodentia; Lipids; Cholesterol; Mechanism; Vertebrata; Regulation(control); Mammalia; Enzymatic activity; Diet; Animal; Modulation
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.18.1009

Regulation of the activity of lanosterol 14α-demethylase (cytochrome P-45014DM) by dietary cholesterol was studied in rats. In male rats fed a 3% cholesterol diet for 1 and 4 weeks, the activity of 24, 25-dihydrolanosterol 14α-demethylase was decreased in the liver. The cytochrome P-45014DM protein content detected by immunoblotting was also decreased by cholesterol feeding. These results demonstrate that dietary cholesterol acts as a repressive factor for lanosterol 14α-demethylase. Further, the activity was enhanced by preincubation with phosphatase of the enzyme solution from both the control and cholesterol fed rats at the same rate. This result suggests that regulation of the activity involves phosphorylation of this enzyme.