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Letters to the Editor |
Sezione di Chimica Clinica, Dipartimento di Scienze, Morfologico-Biomediche, Università degli Studi di Verona, Verona, Italy
aAddress correspondence to this author at: Istituto di Chimica e Microscopia Clinica, Dipartimento di Scienze Morfologico-Biomediche, Università degli Studi di Verona, Ospedale Policlinico G.B. Rossi, Piazzale Scuro, 10, 37134 Verona, Italy. Fax 0039-045-8201889; e-mail ulippi@tin.it.
| The first 20% of the full text of this article appears below. |
To the Editor:
Warfarin, a commonly prescribed anticoagulant drug used to prevent thrombosis, has a narrow therapeutic range, and small dose variations may result in hemorrhagic or thrombotic complications. The 2 key enzymes in the metabolism of warfarin are cytochrome P450 (CYP) 2C9 (CYP2C9 gene) and the C1 subunit of the vitamin K 2,3 epoxide reductase complex (VKORC1 gene). CYP2C9 accounts for up to 85% of the metabolism of the pharmacologically more potent S-warfarin enantiomer, and VKORC1, the 2nd key enzyme in warfarin metabolism, is responsible for recycling reduced vitamin K. In their recent article, Zhu et al. (1) concluded that
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