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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Inhibition of human hepatic cytochrome P450s and steroidogenic CYP17 by nonylphenol.

Effect of nonylphenol on aminopyrine N-demethylase activity, a typical drug-metabolizing enzyme activity, by ten kinds of human hepatic cytochrome P450s (CYP) and on progesterone 17alpha-hydroxylase activity by steroidogenic CYP17 was investigated. When determined at 2 mM substrate concentration, nonylphenol (1 mM) most efficiently inhibited aminopyrine N-demethylation by CYP2C9 and CYP2C19, by 61% and 59%, respectively, followed by CYP2D6, CYP1A2, CYP2C18 and CYP2C8 (46-51%), whereas inhibition of the activities by other CYPs was less than 27%. Additionally, nonylphenol competitively inhibited diclofenac 4'-hydroxylation by CYP2C9 and S-mephenytoin 4'-hydroxylation by CYP2C19 with Ki values of 5.3 and 37 microM, respectively. Furthermore, nonylphenol exhibited a competitive inhibition of progesterone 17alpha-hydroxylase activity by CYP17 with Ki value of 62 microM. These results suggest that nonylphenol inhibits human hepatic CYPs, especially CYP2C9 and CYP2C19, and steroidogenic CYP17 activities.[1]

References

  1. Inhibition of human hepatic cytochrome P450s and steroidogenic CYP17 by nonylphenol. Niwa, T., Maekawa, Y., Fujimoto, M., Kishimoto, K., Yabusaki, Y., Ishibashi, F., Katagiri, M. Biol. Pharm. Bull. (2002) [Pubmed]
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