UDP-Glucuronosyltransferase 1a Enzymes Are Present and Active in the Mouse Blastocyst
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چکیده
منابع مشابه
UDP-glucuronosyltransferase 1a enzymes are present and active in the mouse blastocyst.
The UDP-glucuronosyltransferase (UGT) enzymes are critical for regulating nutrients, hormones, and endobiotics, as well as for detoxifying xenobiotics. Human and murine fetuses are known to express glucuronidation enzymes, but there are currently no data prior to implantation. Here we addressed this gap in knowledge and tested whether Ugt enzymes are already present in preimplantation-stage emb...
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Bile acids (BA) are essential modulators of lipid, glucose, and cholesterol homeostasis, but they exert cytotoxic effects in the cholestatic liver. Glucuronidation, catalyzed by the UDP-glucuronosyltransferase (UGT) enzymes is a pharmacologically relevant BA detoxification process. The present study characterized the BA-conjugating activity of the little-studied human UGTs of subfamily 2A: UGT2...
متن کاملQuantification of Hepatic UDP glucuronosyltransferase 1A splice variant expression and correlation of UDP glucuronosyltransferase 1A1 variant expression with glucuronidation activity.
The UDP glucuronosyltransferase (UGT) 1A gene cluster encodes nine UGT1A family members via splicing of individual first exons to common exons 2 through 5. Each of these nine UGT1As can also undergo alternative splicing at their 3' ends by using an alternate exon 5, resulting in 27 different UGT1A mRNA species with each UGT1A gene encoding three different combinations of 5A and 5B UGT1A exons. ...
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The Gunn rat has been a valuable model for investigating the effect of UDP-glucuronosyltransferase 1A (UGT1A) deficiencies on drug metabolism and toxicity, but it is limited in some aspects. For example, the native Gunn rat model cannot distinguish between hepatic and extrahepatic UGT1A deficiencies in toxicological mechanisms. To extend the model's utility, we investigated the use of replicati...
متن کاملEffects of ketoconazole on glucuronidation by UDP-glucuronosyltransferase enzymes.
PURPOSE Ketoconazole has been shown to inhibit the glucuronidation of the UGT2B7 substrates zidovudine and lorazepam. Its effect on UGT1A substrates is unclear. A recent study found that coadministration of irinotecan and ketoconazole led to a significant increase in the formation of SN-38 (7-ethyl-10-hydroxycamptothecine), an UGT1A substrate. This study investigates whether ketoconazole contri...
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ژورنال
عنوان ژورنال: Drug Metabolism and Disposition
سال: 2014
ISSN: 0090-9556,1521-009X
DOI: 10.1124/dmd.114.059766