Functional characterization of 10 CYP4A11 allelic variants to evaluate the effect of genotype on arachidonic acid ω-hydroxylation

Drug Metab Pharmacokinet. 2015 Feb;30(1):119-22. doi: 10.1016/j.dmpk.2014.09.001. Epub 2014 Sep 28.

Abstract

Genetic variations in cytochrome P450 4A11 (CYP4A11) contributes to inter-individual variability in the metabolism of fatty acids such as arachidonic acid. CYP4A11 metabolizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE), which is important for the regulation of blood pressure. Polymorphisms in CYP4A11 are associated with susceptibility to hypertension. In this study, we evaluated the in vitro ω-hydroxylation of arachidonic acid by 10 CYP4A11 allelic variants, which cause amino acid substitutions in the encoded proteins. CYP4A11 variants were heterologously expressed in COS-7 cells and the kinetic parameters of arachidonic acid ω-hydroxylation were estimated. Among 10 CYP4A11 variants, 5 (CYP4A11-v1, CYP4A11-v2, CYP4A11-v3, CYP4A11-v4, and CYP4A11-v7) showed no or markedly lower activity compared to wild-type CYP4A11. This functional analysis of CYP4A11 variants could provide useful information for the effective prevention and treatment of hypertension.

Keywords: 20-HETE; Arachidonic acid; CYP4A11; Cytochrome P450; Genetic polymorphisms; Hypertension.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alleles*
  • Animals
  • Arachidonic Acid / metabolism*
  • COS Cells
  • Chlorocebus aethiops
  • Cytochrome P-450 CYP4A
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism*
  • Genotype
  • Humans
  • Hydroxylation
  • Mutagenesis, Site-Directed
  • Polymorphism, Single Nucleotide*
  • Transfection

Substances

  • Arachidonic Acid
  • Cytochrome P-450 Enzyme System
  • CYP4A11 protein, human
  • Cytochrome P-450 CYP4A