{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUGT2B15 is a phase‐II conjugating enzyme that plays a central role in the glucuronidation and inactivation of several xenobiotics and endogenous compounds. In drug metabolism studies, UGT2B15 has been shown to stereoselectively glucuronidate substrates such as S‐oxazepam—where recombinant enzyme studies revealed that common polymorphisms (eg, D85Y) lead to markedly lower catalytic activity—and contribute to the disposition of active‐drug metabolites. Furthermore, in tamoxifen‐treated breast cancer patients, high activity UGT2B15 genotypes were associated with increased formation of glucuronide conjugates of active tamoxifen metabolites, a feature that correlated with increased risk of recurrence and poorer survival. Similar genotype–phenotype associations have been observed in in vivo pharmacokinetic studies employing oxazepam as a probe substrate for UGT2B15 activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn steroid hormone metabolism—especially within androgen‐responsive tissues—UGT2B15 is critical for the inactivation of potent androgens such as dihydrotestosterone. Its expression in prostate tissue, frequently observed in luminal cells, complements that of its isoform UGT2B17 to control local androgen bioavailability. Studies have found that genetic variants of UGT2B15, including the D85Y substitution, may alter enzyme kinetics and have been linked to increased risk for prostate cancer, while estrogen‐regulated up‐modulation of UGT2B15 in breast cancer cells may help temper excessive estrogen and androgen signaling. Collectively, these findings underscore UGT2B15’s physiologic importance in maintaining hormone homeostasis in both normal and malignant tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its substrate‐specific catalytic functions, UGT2B15 expression and activity are subject to complex regulation and genetic variation that influence both development and disease risk. High‐density mapping studies have catalogued numerous UGT2B15 variants, and functionally important polymorphisms (eg, the D85Y variant) have been linked to diminished Vmax values, thereby affecting the metabolism of not only drugs (including benzodiazepines and acetaminophen) but also steroid hormones and endocrine disruptors such as bisphenol A. Moreover, UGT2B15 basal expression is modulated by transcription factors (eg, FOXA1) and by post‐transcriptional mechanisms involving microRNAs that bind to its 3′ untranslated region, while its developmental onset in fetal and neonatal tissues further shapes age‐dependent clearance capabilities. Additional studies also suggest that external regulators such as calcitriol can down‐regulate UGT2B15 expression, and that genetic variation in UGT2B15, alone or in concert with related isoforms, may influence the risk of hormone‐dependent neoplasms and alter pharmacokinetic profiles of endocrine therapies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Michael H Court, Su X Duan, Chantal Guillemette, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Stereoselective conjugation of oxazepam by human UDP-glucuronosyltransferases (UGTs): S-oxazepam is glucuronidated by UGT2B15, while R-oxazepam is glucuronidated by UGT2B7 and UGT1A9."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Drug Metab Dispos (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1124/dmd.30.11.1257"}], "href": "https://doi.org/10.1124/dmd.30.11.1257"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12386133"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12386133"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Michael H Court, Qin Hao, Soundararajan Krishnaswamy, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Stereoselective glucuronidation of 5-(4'-hydroxyphenyl)-5-phenylhydantoin by human UDP-glucuronosyltransferase (UGT) 1A1, UGT1A9, and UGT2B15: effects of UGT-UGT interactions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Drug Metab Dispos (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1124/dmd.107.015909"}], "href": "https://doi.org/10.1124/dmd.107.015909"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17576806"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17576806"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Xi He, Leah M Hesse, Suwagmani Hazarika, et al. 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