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

Tizanidine is mainly metabolized by cytochrome p450 1A2 in vitro.

AIMS: To identify the cytochrome p450 ( CYP) enzyme(s) that catalyze the metabolism of tizanidine in vitro. METHODS: The effect of CYP isoform inhibitors on the elimination of tizanidine was studied using pooled human liver microsomes. The metabolism of the drug by a range of human recombinant CYP isoforms was then investigated. RESULTS: Incubation of tizanidine (80 nm) with human liver microsomes resulted in time- and NADPH-dependent substrate consumption with a half-life of 50 min, initial reaction velocity of 1.1 pmol x min-1 x mg-1 protein and intrinsic clearance of 17 ml x min-1 x kg-1. The predicted in vivo hepatic clearance (CLh) of tizanidine using the well-stirred and parallel-tube model was close (68% and 82%, respectively) to its estimated in vivo CLh. Fluvoxamine and furafylline strongly inhibited tizanidine metabolism. Inhibitors specific to isoforms other than CYP1A2 had no substantial effect. Recombinant CYP1A2 metabolized tizanidine to a substantial degree (35% in 45 min), but other recombinant CYPs had little metabolic capacity for the drug. CONCLUSIONS: CYP1A2 is primarily responsible for the metabolism of tizanidine. CYP1A2 inhibitors may inhibit its metabolism also in vivo.[1]


  1. Tizanidine is mainly metabolized by cytochrome p450 1A2 in vitro. Granfors, M.T., Backman, J.T., Laitila, J., Neuvonen, P.J. British journal of clinical pharmacology. (2004) [Pubmed]
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