References
- Buckley DB, Klaassen CD. (2007). Tissue- and gender-specific mRNA expression of UDP-glucuronosyltransferases (UGTs) in mice. Drug Metab Dispos 35:121–7
- Buckley DB, Klaassen CD. (2009). Mechanism of gender-divergent UDP-glucuronosyltransferase mRNA expression in mouse liver and kidney. Drug Metab Dispos 37:834–40
- Court MH. (2005). Isoform-selective probe substrates for in vitro studies of human UDP-glucuronosyltransferases. Meth Enzymol 400:104–16
- Court MH, Duan SX, von Moltke LL, et al. (2001). Interindividual variability in acetaminophen glucuronidation by human liver microsomes: identification of relevant acetaminophen UDP-glucuronosyltransferase isoforms. J Pharmacol Exp Ther 299:998–1006
- de Leon J. (2003). Glucuronidation enzymes, genes and psychiatry. Int J Neuropsychopharmacol 6:57–72
- Ebner T, Burchell B. (1993). Substrate specificities of two stably expressed human liver UDP-glucuronosyltransferases of the UGT1 gene family. Drug Metab Dispos 21:50–5
- Fisher MB, Vandenbranden M, Findlay K, et al. (2000). Tissue distribution and interindividual variation in human UDP-glucuronosyltransferase activity: relationship between UGT1A1 promoter genotype and variability in a liver bank. Pharmacogenetics 10:727–39
- Hafdi Z, Couette S, Comoy E, et al. (1996). Locally formed 5-hydroxytryptamine stimulates phosphate transport in cultured opossum kidney cells and in rat kidney. Biochem J 320:615–21
- Harding D, Fournel-Gigleux S, Jackson MR, Burchell B. (1988). Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells. Proc Natl Acad Sci USA 85:8381–5
- Houston JB, Kenworthy KE. (2000). In vitro–in vivo scaling of CYP kinetic data not consistent with the classical Michaelis–Menten model. Drug Metab Dispos 28:246–54
- Itäaho K, Court MH, Uutela P, et al. (2009). Dopamine is a low-affinity and high-specificity substrate for the human UDP-glucuronosyltransferase 1A10. Drug Metab Dispos 37:768–75
- Ito Y, Yokota H, Wang R, et al. (2005). Species differences in the metabolism of di(2-ethylhexyl) phthalate (DEHP) in several organs of mice, rats, and marmosets. Arch Toxicol 79:147–54
- Kallionpää RA, Järvinen E, Finel M. (2015). Glucuronidation of estrone and 16α-hydroxyestrone by human UGT enzymes: the key roles of UGT1A10 and UGT2B7. J Steroid Biochem Mol Biol 154:104–11
- King CD, Rios GR, Assouline JA, Tephly TR. (1999). Expression of UDP-glucuronosyltransferases (UGTs) 2B7 and 1A6 in the human brain and identification of 5-hydroxytryptamine as a substrate. Arch Biochem Biophys 365:156–62
- Krishnaswamy S, Duan SX, Von Moltke LL, et al. (2003a). Validation of serotonin (5-hydroxtryptamine) as an in vitro substrate probe for human UDP-glucuronosyltransferase (UGT) 1A6. Drug Metab Dispos 31:133–9
- Krishnaswamy S, Duan SX, Von Moltke LL, et al. (2003b). Serotonin (5-hydroxytryptamine) glucuronidation in vitro: assay development, human liver microsome activities and species differences. Xenobiotica 33:169–80
- Kurkela M, Patana AS, Mackenzie PI, et al. (2007). Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics 17:115–26
- Leakey JE. (1978). An improved assay technique for uridine diphosphate glucuronosyltransferase activity towards 5-hydroxytryptamine and some properties of the enzyme. Biochem J 175:1119–24
- Mohamed ME, Frye RF. (2011). Inhibitory effects of commonly used herbal extracts on UDP-glucuronosyltransferase 1A4, 1A6, and 1A9 enzyme activities. Drug Metab Dispos 39:1522–8
- Nakamura A, Nakajima M, Yamanaka H, et al. (2008). Expression of UGT1A and UGT2B mRNA in human normal tissues and various cell lines. Drug Metab Dispos 36:1461–4
- Nakajima M, Yamanaka H, Fujiwara R, et al. (2007). Stereoselective glucuronidation of 5-(4′-hydroxyphenyl)-5-phenylhydantoin by human UDP-glucuronosyltransferase (UGT) 1A1, UGT1A9, and UGT2B15: effects of UGT-UGT interactions. Drug Metab Dispos 35:1679–86
- Radominska-Pandya A, Czernik PJ, Little JM, et al. (1999). Structural and functional studies of UDP-glucuronosyltransferases. Drug Metab Rev 31:817–99
- Roth KA, Gordon JI. (1990). Spatial differentiation of the intestinal epithelium: analysis of enteroendocrine cells containing immunoreactive serotonin, secretin, and substance P in normal and transgenic mice. Proc Natl Acad Sci USA 87:6408–12
- Shelby MK, Cherrington NJ, Vansell NR, Klaassen CD. (2003). Tissue mRNA expression of the rat UDP-glucuronosyltransferase gene family. Drug Metab Dispos 31:326–33
- Shiratani H, Katoh M, Nakajima M, Yokoi T. (2008). Species differences in UDP-glucuronosyltransferase activities in mice and rats. Drug Metab Dispos 36:1745–52
- Stier CT Jr, Itskovitz HD. (1985). Formation of serotonin by rat kidneys in vivo. Proc Soc Exp Biol Med 180:550–7
- Tukey RH, Strassburg CP. (2000). Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu Rev Pharmacol Toxicol 40:581–616
- Turgeon D, Carrier JS, Lévesque E, et al. (2001). Relative enzymatic activity, protein stability, and tissue distribution of human steroid-metabolizing UGT2B subfamily members. Endocrinology 142:778–87
- Uchaipichat V, Mackenzie PI, Guo XH, et al. (2004). Human udp-glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid. Drug Metab Dispos 32:413–23
- Uchihashi S, Nishikawa M, Sakaki T, Ikushiro S. (2013). Comparison of serotonin glucuronidation activity of UDP-glucuronosyltransferase 1a6a (Ugt1a6a) and Ugt1a6b: evidence for the preferential expression of Ugt1a6a in the mouse brain. Drug Metab Pharmacokinet 28:260–4
- Watanabe Y, Nakajima M, Yokoi T. (2002). Troglitazone glucuronidation in human liver and intestine microsomes: high catalytic activity of UGT1A8 and UGT1A10. Drug Metab Dispos 30:1462–9
- Weissbach H, Lovenberg W, Redfield BG, Udenfriend S. (1960). In vivo metabolism of serotonin and tryptamine: effect of monoamine oxidase inhibition. J Pharmacol Exp Ther 131:26–30
- Zheng X, Kang A, Dai C, et al. (2012). Quantitative analysis of neurochemical panel in rat brain and plasma by liquid chromatography–tandem mass spectrometry. Anal Chem 84:10044–51