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UDP-glucuronosyltransferases in human intestinal mucosa

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1998
While UDP-glucuronosyltransferases (UGTs) are known to be expressed at high levels in human liver, relatively little is known about extrahepatic expression. In the present study, UGT2B family isoforms involved in the glucuronidation of steroid hormones and bile acids have been characterized in microsomes prepared from jejunum, ileum and colon from six ...
Jean-Pierre Raufman   +6 more
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Coffee and Gastrointestinal Glucuronosyltransferases

2015
Abstract The beneficial health effects of coffee have, among other mechanisms, been linked to the activation of phase II enzymes, including UDP-glucuronosyltransferases (UGTs). UGTs catalyze the detoxification of many xenobiotic compounds, including human carcinogens and reactive oxygen species.
Christian P. Strassburg, Sandra Kalthoff
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Cloning and Characterization of a Canine UDP-Glucuronosyltransferase

Archives of Biochemistry and Biophysics, 2001
UDP-glucuronosyltransferases (UGTs) are a major family of enzymes catalyzing the transfer of glucuronic acid to a range of endogenous compounds and xenobiotics facilitating their elimination in either urine or bile. Although the dog is commonly used in drug metabolism studies, relatively little is known about the expression and activity of UGTs in this
D.J. Smith   +3 more
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Inhibition of aflatoxins on UDP-glucuronosyltransferases (UGTs)

Toxicology in Vitro, 2023
Aflatoxins have been recognized as the most harmful mycotoxins leading to various toxic effects. The present study aims to determine the inhibition behavior of aflatoxins on the activity of the important phase II metabolizing enzymes, UDP-glucuronosyltransferases (UGTs), based on in vitro incubation system of recombinant human UGTs-catalyzed ...
Zuo, Du, Zhen-Zhong, Liu
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Isolation and purification of UDP-glucuronosyltransferases

Chemical Research in Toxicology, 1990
UDPGTs are members of a class of enzymes located in the endoplasmic reticulum and are encoded by a multigene family. These proteins are responsible for the glucuronidation of hundreds of xenobiotics of many chemical classes and many endogenous substances such as steroid hormones, bile acids, and bilirubin.
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UDP-glucuronosyltransferases: a family of detoxifying enzymes

Trends in Pharmacological Sciences, 1990
Glucuronidation is an important process in the metabolism of xenobiotic and endogenous substances leading to enhancement of excretion of these compounds from the body. A multigene family encodes a number of UDP-glucuronosyltransferase enzymes which catalyse this route of metabolism.
Brian Burchell, Thomas R. Tephly
openaire   +3 more sources

Development of Human Liver UDP-Glucuronosyltransferases

Developmental Pharmacology and Therapeutics, 1989
The development of multiple UDPGT activities towards eight substrates has been studied in fetal term and adult post-mortem (less than 5 h after death) liver samples. Most fetal and term liver activities were less than 14% of adult values, except that towards 5-hydroxytryptamine which was present in fetal and term liver at adult levels.
David Harding   +6 more
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Natural and synthetic inhibitors of UDP-glucuronosyltransferase

Pharmacology & Therapeutics, 2001
Glucuronidation is a major detoxification pathway in vertebrates. The reaction is catalyzed by a family of UDP-glucuronosyltransferases (UGTs) and involves conjugation of many endobiotic and xenobiotic substances with glucuronic acid, forming inactive water-soluble glucuronides.
Zlatina Naydenova   +3 more
openaire   +2 more sources

Polymorphism of UDP-Glucuronosyltransferase and Drug Metabolism

Current Drug Metabolism, 2005
UDP-glucuronosyltransferase is a group of catabolic enzymes involved in the detoxification and excretion of many xenobiotic and endogeneous substances in intrahepatic and extrahepatic tissues. The group consists of two subfamilies, UGT1 and UGT2. UGT1 consists of 5 exons and has a unique gene structure.
Yoshihiro Maruo   +4 more
openaire   +3 more sources

Polymorphisms of UDP-Glucuronosyltransferase and Pharmacokinetics of Irinotecan

Therapeutic Drug Monitoring, 2002
Irinotecan is a prodrug that is hydrolyzed by carboxylesterase in vivo to form an active metabolite SN-38. SN-38 is further conjugated and detoxified by UDP-glucuronosyltransferase (UGT) to yield its beta-glucuronide (SN-38G). Although irinotecan is widely used, the drug causes unpredictably severe, occasionally fatal, toxicity of leukopenia or ...
Hiroshi Ueoka   +5 more
openaire   +2 more sources

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