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Identification of cytochrome P450 1A2 as enzyme involved in the microsomal metabolism of Huperzine A.
European Journal of Pharmacology 2003 Februrary 15
Huperzine A is a reversible and selective cholinesterase inhibitor approved for the treatment of Alzheimer's disease. To identify which cytochrome P450 (CYP) isoenzymes are involved in the metabolism of Huperzine A, an in vitro study was performed with rat liver microsomes and immunoinhibition and chemical inhibition methods. Huperzine A metabolism was analyzed with high-performance liquid chromatography (HPLC) and expressed as Huperzine A disappearance rate. Result showed that 76.2% of Huperzine A metabolism was inhibited by CYP1A2 antibody and 17.8% by CYP3A1/2 antibody. Inhibitory effects produced by CYP2C11 and 2E1 antibodies were minor. The CYP1A2 substrate phenacetin showed an inhibitory effect of 70.3%. In conclusion, Huperzine A metabolism in rat liver microsomes is mediated primarily by CYP1A2, with a probable secondary contribution of CYP3A1/2. CYP2C11 and 2E1 are likely not involved in Huperzine A metabolism.
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