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Department of Pharmacology, University of Iowa
A human UDP-glucuronosyltransferase (UGT) catalyzing the
glucuronidation of morphine has been identified. A full length cDNA was
isolated from a human liver cDNA library and found to be identical to
the UGT2B7 form having a tyrosine at position 268. This cDNA was
transfected into HK 293 cells, and stable expression was achieved. Cell
homogenates and membrane preparations from HK 293 cells expressing UGT2B7 catalyzed the glucuronidation of morphine and other clinically significant opioid agonists, antagonists, and partial agonists. UGT2B7
catalyzed morphine glucuronidation at the 3- and 6-hydroxy positions
and also mediated the formation of codeine-6-glucuronide from codeine.
This represents the first demonstration of a UGT capable of catalyzing
the glucuronidation of both the 3- and 6-positions of opioids. Since
humans excrete morphine-3-glucuronide and morphine-6-glucuronide after
morphine administration, it is likely that UGT2B7 is a major isoform in
humans responsible for the metabolism of this important drug and its
surrogates.
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