Functional characterization of CYP2C19 variants in nebivolol 4‐hydroxlation in vitro

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EarlyView Article

  • Published: Dec 11, 2017
  • Author: Xiao‐Yang Zhou, Xiao‐Xia Hu, Meng‐Fang Li, Hao Wang, Li‐Qun Zhang, Guo‐Xin Hu, Jian‐Ping Cai
  • Journal: Drug Testing and Analysis


Cytochrome P450 2C19 (CYP2C19) allelic variants are thought to play an important part in inter‐individual variability in drug metabolism. We evaluated the in vitro hydroxylation of nebivolol by 31 CYP2C19 alleles identified in a Chinese Han population recently. Wild‐type CYP2C19*1B and 30 isoforms were highly expressed in insect cells, and the enzymatic activities of CYP2C19 variants towards nebivolol hydroxylation were characterized. Among the 30 CYP2C19 alleles, most of the recombinant CYP2C19 variants exhibited no or significantly low activity compared with CYP2C19*1B. Three variants, CYP2C19*29 (K28I), L16F, and CYP2C19*23 (G91R), showed increased intrinsic clearance of >140% CYP2C19*1B. Combined with a previous study on the effects of CYP2D6 variants on nebivolol metabolism, our comprehensive analyses on the enzymatic activities of CYP2C19 variants towards nebivolol in the present study may contribute to determination of the optimal doses of nebivolol for the treatment of hypertension and understanding of “individualized” medication.

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