Regular ArticleCharacterization of Two UDP Glucuronosyltransferases That Are Predominantly Expressed in Human Colon☆
References (24)
- et al.
J. Biol. Chem.
(1997) Advanced Drug Delivery Reviews
(1997)- et al.
Pharmacol. Ther.
(1990) - et al.
Biochem. Pharmacol.
(1988) - et al.
J. Biol. Chem.
(1998) - et al.
J. Biol. Chem.
(1996) - et al.
Biochem. Biophys. Res. Commun.
(1997) - et al.
Biochem. Biophys. Res. Commun.
(1996) - et al.
J. Biol. Chem.
(1989) - et al.
J. Biol. Chem.
(1984)
Anal. Biochem.
Cited by (102)
Evaluation of inhibitors of intestinal UDP-glucuronosyltransferases 1A8 and 1A10 using raloxifene as a substrate in Caco-2 cells: Studies with four flavonoids of Scutellaria baicalensis
2021, Toxicology in VitroCitation Excerpt :UGT1A10 is expressed throughout the tract and, additionally, in the bile ducts (Gregory et al., 2004). These expression patterns suggests that UGT1A8 and UGT1A10 may play an important role in the metabolism of dietary xenobiotics (Mojarrabi and Mackenzie, 1998; Wang et al., 2016). It has been reported that overexpression of the UGT1A enzymes would lead to development of chemotherapeutic drug resistance (Pathania et al., 2018).
UDP-Glycosyltransferases
2018, Comprehensive Toxicology: Third EditionPrevalence of UDP-glucuronosyltransferase polymorphisms (UGT1A6∗2, 1A7∗12, 1A8∗3, 1A9∗3, 2B7∗2, and 2B15∗2) in a Saudi population
2017, Saudi Pharmaceutical JournalCitation Excerpt :The UGT1A8 is a very rare form of polymorphism and is expressed entirely in the extra-hepatic tissues of the gastrointestinal tract (Tukey and Strassburg, 2000, 2001). It has been found that UGT1A8 plays a role in the metabolism of dietary and environmental carcinogens (Mojarrabi and Mackenzie, 1998; Nowell et al., 1999; Cheng et al., 1998, 1999). UGT1A8∗3 has been classified as a low-activity protein on various substrates, including a reduction in MPAG (MPA glucuronide metabolite) formation (Huang et al., 2002).
Cellular asymmetric catalysis by UDP-glucuronosyltransferase 1A8 shows functional localization to the basolateral plasma membrane
2015, Journal of Biological ChemistryThe UDP-glucuronosyltransferases: Their role in drug metabolism and detoxification
2013, International Journal of Biochemistry and Cell BiologyCitation Excerpt :Conversely, the general pattern of UGT expression in the small intestine and colon more closely resemble the liver, with a large number of enzymes exhibiting significant expression (Table 2), and a greater abundance of UGT2B compared with UGT1A. However, expression of UGT2B4 (the most abundant UGT liver) is limited throughout the GIT, while UGT1A7, 1A8 and 1A10, which are essentially absent from human liver are all expressed in the small intestine and colon (Mojarrabi and Mackenzie, 1998; Ohno et al., 2009; Court et al., 2012). It is important to note that these data are generated by quantification of mRNA expression, which is an indirect measure of protein abundance.
Identification of the human UDP-glucuronosyltransferase isoforms involved in the glucuronidation of the phytochemical ferulic acid
2011, Drug Metabolism and Pharmacokinetics
- ☆
Abbreviations used are: UGT, Uridine diphosphoglucuronosyltransferase; PCR, polymerase chain reaction; RT, reverse transcription; G3PDH, glyceraldehyde-3-phosphate dehydrogenase; TLC, thin layer chromatography
- 1
Corresponding author. Fax: 61 8 8204 5114. E-mail:[email protected].