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Research Article

Pharmacogenetics of Uridine Diphosphoglucuronosyltransferase (UGT) 1A Family Members and its Role in Patient Response to Irinotecan

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Pages 393-409 | Published online: 09 Oct 2008
 

Abstract

Glucuronidation, catalyzed by the glucuronosyltransferase (UGT) superfamily, is a major biotransformation pathway for several drugs, including irinotecan. Irinotecan is commonly used in colorectal cancer chemotherapy. Irinotecan undergoes metabolism in humans and is converted to its active metabolite SN-38, a topoisomerase I inhibitor. SN-38 is inactivated via glucuronidation catalyzed by various hepatic and extrahepatic UGT1A isozymes. Although the role of the UGT1A1 *28 genetic variant has received much attention in altered toxicity upon irinotecan treatment, other UGT1A enzymes also play an important role. This review summarizes pharmacokinetic, toxicologic, and pharmacogenetic studies carried out to date in irinotecan and SN-38 disposition.

Notes

*Presented at the 13th North American International Society for the Study of Xenobiotics Meeting/20th Japanese Society for the Study of Xenobiotics Meeting, Maui, Hawaii, October 23–27, 2005.

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