Functional characterization of five novel CYP2C8 variants, G171S, R186X, R186G, K247R, and K383N, found in a Japanese population.

doi:10.1124/dmd.105.003830

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Functional characterization of five novel CYP2C8 variants, G171S, R186X, R186G, K247R, and K383N, found in a Japanese population.

Drug metabolism and disposition: the biological fate of chemicals - 1 May 2005

Hichiya Hiroyuki, Tanaka-Kagawa Toshiko, Soyama Akiko, Jinno Hideto, Koyano Satoru, Katori Noriko, Matsushima Erika, Uchiyama Shigehisa, Tokunaga Hiroshi, Kimura Hideo, Minami Narihiro, Katoh Masaaki, Sugai Kenji, Goto Yu-ichi, Tamura Tomohide, Yamamoto Noboru, Ohe Yuichiro, Kunitoh Hideo, Nokihara Hiroshi, Yoshida Teruhiko, Minami Hironobu, Saijo Nagahiro, Ando Masanori, Ozawa Shogo, Saito Yoshiro, Sawada Jun-ichi

Abstract excerpt

Cytochrome P450 2C8 is one of the primary enzymes responsible for the metabolism of a wide range of drugs such as paclitaxel, cerivastatin, and amiodarone. We have sequenced the CYP2C8 gene from 201 Japanese subjects and found five novel nonsynonymous single nucleotide polymorphisms (SNPs): 511G>A (G171S), 556C>T (R186X; X represents the translational stop codon), 556C>G (R186G), 740A>G (K247R), and 1149G>T...

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PMID: 15716363
DOI: 10.1124/dmd.105.003830

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