UDP-Glucuronosyltransferase 1A1 Is the Principal Enzyme Responsible for Etoposide Glucuronidation in Human Liver and Intestinal Microsomes: Structural Characterization of Phenolic and Alcoholic Glucuronides of Etoposide and Estimation of Enzyme Kinetics

2006 ◽  
Vol 35 (3) ◽  
pp. 371-380 ◽  
Author(s):  
Zhiming Wen ◽  
Melanie N. Tallman ◽  
Shazia Y. Ali ◽  
Philip C. Smith
Keyword(s):  
Enzyme Kinetics ◽  
Structural Characterization ◽  
Human Liver ◽  
Intestinal Microsomes ◽  
Udp Glucuronosyltransferase

scholarly journals Identification of Catalposide Metabolites in Human Liver and Intestinal Preparations and Characterization of the Relevant Sulfotransferase, UDP-glucuronosyltransferase, and Carboxylesterase Enzymes

Pharmaceutics ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 355 ◽  
Author(s):  
Deok-Kyu Hwang ◽  
Ju-Hyun Kim ◽  
Yongho Shin ◽  
Won-Gu Choi ◽  
Sunjoo Kim ◽  
...  
Keyword(s):  
Human Liver ◽  
Individual Variability ◽  
Hydroxybenzoic Acid ◽  
Catalpa Ovata ◽  
Anti Oxidant ◽  
Extrahepatic Tissues ◽  
Udp Glucuronosyltransferase ◽  
Hydrolysis Of

Catalposide, an active component of Veronica species such as Catalpa ovata and Pseudolysimachion lingifolium, exhibits anti-inflammatory, antinociceptic, anti-oxidant, hepatoprotective, and cytostatic activities. We characterized the in vitro metabolic pathways of catalposide to predict its pharmacokinetics. Catalposide was metabolized to catalposide sulfate (M1), 4-hydroxybenzoic acid (M2), 4-hydroxybenzoic acid glucuronide (M3), and catalposide glucuronide (M4) by human hepatocytes, liver S9 fractions, and intestinal microsomes. M1 formation from catalposide was catalyzed by sulfotransferases (SULTs) 1C4, SULT1A1*1, SULT1A1*2, and SULT1E1. Catalposide glucuronidation to M4 was catalyzed by gastrointestine-specific UDP-glucuronosyltransferases (UGTs) 1A8 and UGT1A10; M4 was not detected after incubation of catalposide with human liver preparations. Hydrolysis of catalposide to M2 was catalyzed by carboxylesterases (CESs) 1 and 2, and M2 was further metabolized to M3 by UGT1A6 and UGT1A9 enzymes. Catalposide was also metabolized in extrahepatic tissues; genetic polymorphisms of the carboxylesterase (CES), UDP-glucuronosyltransferase (UGT), and sulfotransferase (SULT) enzymes responsible for catalposide metabolism may cause inter-individual variability in terms of catalposide pharmacokinetics.

Structural characterization of human liver heparan sulfate

2005 ◽  
Vol 1721 (1-3) ◽  
pp. 1-8 ◽  
Author(s):  
Preeyanat Vongchan ◽  
Mohamad Warda ◽  
Hidenao Toyoda ◽  
Toshihiko Toida ◽  
Rory M. Marks ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Structural Characterization ◽  
Human Liver

Identification of UDP-glucuronosyltransferase isoforms responsible for leonurine glucuronidation in human liver and intestinal microsomes

Xenobiotica ◽  
2014 ◽  
Vol 44 (9) ◽  
pp. 775-784 ◽  
Author(s):  
Bo Tan ◽  
Weimin Cai ◽  
Jinlian Zhang ◽  
Ning Zhou ◽  
Guo Ma ◽  
...  
Keyword(s):  
Human Liver ◽  
Intestinal Microsomes ◽  
Udp Glucuronosyltransferase
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