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Vol. 26, Issue 1, 73-77, January 1998
Department of Pharmacology, The University of Iowa
UGT2B7 has been cloned and expressed previously in COS cells and
HK293 cells. Two forms have been identified: one with a tyrosine and
one with a histidine at position 268. UGT2B7 has been shown to catalyze
NSAIDs, catechol estrogens, and morphine-3- and -6-glucuronidation. cDNAs for UGT2B7Y268 and H268 were cloned and stably expressed in HK
293 cells. Studies were designed to test each form for reactivity toward a number of opioid compounds, xenobiotics such as menthol, oxazepam, and propranolol, and androgens such as androsterone and
testosterone using membrane preparations derived from HK 293 cells.
Both UGT2B7Y and UGT2B7H are highly reactive with many opioids,
menthol, androsterone, and (R)- and
(S)-propranolol, and similar kinetic values were observed.
UGT2B7Y and UGT2B7H react poorly with oxazepam and no difference in
(R)- or (S)-glucuronidation rate ratios was
found. Thus, UGT2B7Y and H cannot account for the variability in the
plasma or urine concentrations of these glucuronides in human
populations. Our data suggest that UGT2B7 is a major isoform
responsible for the glucuronidation of androsterone. Neither UGT2B7Y
nor H catalyzes the glucuronidation of testosterone although each
catalyzes the glucuronidation of epitestosterone. UGT2B7 seems to be a
major human isoform responsible for the glucuronidation of opioids of
the morphinan and oripavine class and is capable of catalyzing the
glucuronidation of both the 3- and 6-hydroxyl moieties on these
molecules. Thus, UGT2B7 plays a major role in the conversion of
morphine to morphine-6-glucuronide, the potent analgesic metabolite of
morphine.
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