Diurnal variation in cholesterol 7α-hydroxylase activity is determined by the -203A>C polymorphism of the CYP7A1 gene

Croat Med J. 2016 Apr 23;57(2):111-7. doi: 10.3325/cmj.2016.57.111.

Abstract

Aim: To determine whether the promoter polymorphism -203A>C of cholesterol-7α-hydroxylase encoding gene (CYP7A1) affects diurnal variation in CYP7A1 enzyme activity.

Methods: The study included 16 healthy male volunteers - 8 homozygous for -203A and 8 homozygous for the -203C allele of CYP7A1. Three 15-hour examinations (from 7am to 10pm) were carried out for each of the participants: after one-day treatment with cholestyramine; after one-day treatment with chenodeoxycholic acid (CDCA); and a control examination without any treatment. The plasma concentration of 7α-hydroxy-4-cholesten-3-one (C4), a marker of CYP7A1 activity, was determined in all the experiments at 90-min intervals.

Results: CYP7A1 activity was up-regulated after treatment with cholestyramine and suppressed after treatment with CDCA. There were no differences between -203A and -203C allele carriers in the response of enzyme activity to both drugs. In the control experiment, -203A allele carriers displayed diurnal variation in enzyme activity, whereas CYP7A1 activity did not change in -203C allele carriers. These results were confirmed by modeling the dynamics of C4 using polynomial regression.

Conclusion: The promoter polymorphism of the CYP7A1 gene has a pronounced impact on diurnal variation in CYP7A1 activity.

MeSH terms

  • Adult
  • Area Under Curve
  • Bile Acids and Salts / biosynthesis*
  • Cholestenones / blood
  • Cholesterol / blood
  • Cholesterol 7-alpha-Hydroxylase / genetics
  • Cholesterol 7-alpha-Hydroxylase / metabolism*
  • Circadian Rhythm / physiology
  • Enzyme Activation
  • Humans
  • Male
  • Polymorphism, Genetic*
  • Promoter Regions, Genetic
  • Up-Regulation

Substances

  • Bile Acids and Salts
  • Cholestenones
  • 7 alpha-hydroxy-4-cholesten-3-one
  • Cholesterol
  • CYP7A1 protein, human
  • Cholesterol 7-alpha-Hydroxylase