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Pharmacogenetics of Phase II Enzymes: N-acetyltransferase, Thiopurine S-methyltransferase, UDP-glucuronosyltransferase

Pharmacogenetics of Phase II Enzymes: N-acetyltransferase, Thiopurine S-methyltransferase, UDP-glucuronosyltransferase

Phase II biotransformation reactions are essential for detoxifying and eliminating xenobiotics, including many pharmaceutical compounds. These reactions typically involve conjugation, the covalent attachment of polar endogenous groups such as glucuronic acid, sulfate, methyl, or acetyl moieties to functional groups introduced during Phase I metabolism. The resulting conjugates are more water-soluble, enabling efficient renal or biliary excretion.The major classes of Phase II enzymes include...

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Multiplexed Targeted Quantitative Proteomics Predicts Hepatic Glucuronidation Potential.

Guillaume Margaillan¹, Michèle Rouleau¹, Kathrin Klein¹

¹Pharmacogenomics Laboratory, Centre Hospitalier Universitaire (CHU) de Québec and Faculty of Pharmacy, Université Laval, Québec, Canada (G.M., M.R., P.C., L.V., C.G.); Dr. Margarete Fischer-Bosch Institute of Clinical Pharmacology, Stuttgart, and University of Tübingen, Tübingen, Germany (K.K., U.M.Z.); Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, North Carolina (J.K.F., P.C.S.); Canada Research Chair in Pharmacogenomics (C.G.).

Drug Metabolism and Disposition: the Biological Fate of Chemicals

|June 17, 2015

Summary

This summary is machine-generated.

This study quantified 14 hepatic UDP-glucuronosyltransferases (UGTs) using targeted proteomics. UGT2B7 was most abundant, with significant interindividual variability observed in UGT expression and activity.

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Area of Science:

Pharmacology
Biochemistry
Proteomics

Background:

Phase II metabolism is crucial for drug and endogenous molecule bioactivity.
UDP-glucuronosyltransferases (UGTs) are key enzymes in hepatic glucuronidation.
Understanding hepatic UGT expression is vital for drug development and personalized medicine.

Purpose of the Study:

To determine the expression profiles of 14 hepatic UDP-glucuronosyltransferases (UGTs) in human liver samples.
To quantify the absolute concentrations and assess the activity of hepatic UGTs.
To investigate the interrelationships and variability in UGT expression.

Main Methods:

Targeted proteomics was employed to quantify 14 hepatic UGTs in 48 liver samples.
Nano-ultra-performance liquid chromatography with tandem mass spectrometry (nano-UPLC-MS/MS) was utilized for sensitive analysis.
Glucuronidation activity was measured using specific probe substrates.

Main Results:

UGT2B7 was identified as the most abundant hepatic UGT, with UGT1A1, UGT1A4, UGT2B4, and UGT2B15 also highly expressed.
The five most abundant UGTs accounted for 81% of the total measured hepatic UGTs.
Significant interindividual variability in UGT concentrations and activities was observed, with strong correlations noted between UGT1A4 and other UGTs, and between UGT2B4/UGT2B7.

Conclusions:

Multiplexed targeted quantitative proteomics accurately assesses hepatic UGT concentrations and glucuronidation potential.
The study provides comprehensive absolute hepatic concentrations for 14 UGTs.
Co-regulated expression patterns among the most abundant hepatic UGTs were identified, expanding understanding of hepatic UGT profiles.