Modulation of UDP-glucuronosyltransferase activity by endogenous compounds

Yuji Ishii, Arief Nurrochmad, Hideyuki Yamada

Research output: Contribution to journalReview articlepeer-review

30 Citations (Scopus)


Glucuronidation is one of the major pathways of metabolism of endo- and xenobiotics. UDP-Glucuronosyltransferase (UGT)-catalyzed glucuronidation accounts for up to 35z of phase II reactions. The expression and function of UGT is modulated by gene regulation, post-translational modifications and protein-protein association. Many studies have focused on drug-drug interactions involving UGT, and there are a number of reports describing the inhibition of UGT by xenobiotics. However, studies about the role of endogenous compounds as an inhibitor or activator of UGT are limited, and it is important to understand any change in the function and regulation of UGT by endogenous compounds. Recent studies in our laboratory have shown that fatty acyl-CoAs are endogenous activators of UGT, although fatty acyl-CoAs had been considered as inhibitors of UGT. Further, we have also suggested that adenine and related compounds are endogenous allosteric inhibitors of UGT. In this review, we summarize the endogenous modulators of UGT and discuss their relevance to UGT function.

Original languageEnglish
Pages (from-to)134-148
Number of pages15
JournalDrug metabolism and pharmacokinetics
Issue number2
Publication statusPublished - 2010

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmaceutical Science
  • Pharmacology (medical)


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