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

Contribution of UDP-glucuronosyltransferases 1A9 and 2B7 to the glucuronidation of indomethacin in the human liver.

OBJECTIVE: We characterized the kinetics of indomethacin glucuronidation by recombinant UDP-glucuronosyltransferase (UGT) isozymes and human liver microsomes (HLM) and identified the human UGT isozymes involved. METHODS: Indomethacin glucuronidation was investigated using HLM and recombinant human UGT isozymes. Human UGTs involved in indomethacin glucuronidation were assessed in kinetic studies, chemical inhibition studies, and correlation studies. RESULTS: Among the UGT isozymes investigated, UGT1A1, 1A3, 1A9, and 2B7 showed glucuronidation activity for indomethacin, with UGT1A9 possessing the highest activity, followed by UGT2B7. Glucuronidation of indomethacin by recombinant UGT1A9 and 2B7 showed substrate inhibition kinetics with K (m) values of 35 and 32 microM, respectively. The glucuronidation of indomethacin was significantly correlated with morphine 3OH-glucuronidation (r = 0.69, p < 0.05) and 3'-azido-3'-deoxythymidine glucuronidation (r = 0.82, p < 0.05), a reaction mainly catalyzed by UGT2B7. Propofol inhibited indomethacin glucuronidation in HLM with an IC(50) value of 248 microM, which is between the IC(50) value in recombinant UGT1A9 (106 microM) and UGT2B7 (> 400 microM). CONCLUSIONS: These findings suggest that UGT2B7 plays a predominant role in indomethacin glucuronidation in the human liver and that UGT1A9 is partially involved.[1]


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