Identification of UGT2B9*2 and UGT2B33 isolated from female rhesus monkey liver

Two UDP-glucuronosyltransferases (UGT2B9*2 and UGT2B33) have been isolated from female rhesus monkey liver. Microsomal preparations of the cell lines expressing the UGTs catalyzed the glucuronidation of the general substrate 7-hydroxy-4-(trifluoromethyl)coumarin in addition to selected estrogens (β-estradiol and estriol) and opioids (morphine, naloxone, and naltrexone). UGT2B9*2 displayed highest efficiency for β-estradiol-17-glucuronide production and did not catalyze the glucuronidation of naltrexone. UGT2B33 displayed highest efficiency for estriol and did not catalyze the glucuronidation of β-estradiol. UGT2B9*2 was found also to catalyze the glucuronidation of 4-hydroxyestrone, 16-epiestriol, and hyodeoxycholic acid, while UGT2B33 was capable of conjugating 4-hydroxyestrone, androsterone, diclofenac, and hyodeoxycholic acid. Three glucocorticoids (cortisone, cortisol, and corticosterone) were not substrates for glucuronidation by liver or kidney microsomes or any expressed UGTs. Our current data suggest the use of β-estradiol-3-glucuronidation, β-estradiol-17-glucuronidation, and estriol-17-glucuronidation to assay UGT1A01, UGT2B9*2, and UGT2B33 activity in rhesus liver microsomes, respectively.