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Pharmacogenetics of sulfotransferase
1Division of Drug Metabolism and Molecular Toxicology, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan. nagataki@mail.pharm.tohoku.ac.jp
Annual Review of Pharmacology and Toxicology
|June 3, 2000
Summary
Cytosolic sulfotransferases (SULTs) conjugate small molecules. Human SULTs, including those with genetic variations, are crucial for metabolizing hormones and xenobiotics.
Area of Science:
- Biochemistry
- Pharmacology
- Genetics
Background:
- Cytosolic sulfotransferases (SULTs) are enzymes facilitating sulfoconjugation.
- These enzymes process endogenous compounds (endobiotics) and foreign substances (xenobiotics).
- Mammalian SULTs comprise at least 44 forms across five distinct families.
Purpose of the Study:
- To characterize the human cytosolic sulfotransferase gene family.
- To investigate the substrate specificity and metabolic roles of human SULTs.
- To identify genetic variations within human SULT genes.
Main Methods:
- Bioinformatic analysis of amino acid sequences to determine SULT families.
- Gene identification and chromosomal localization studies in humans.
- Enzymatic characterization of recombinant SULT forms.
Main Results:
- Ten human sulfotransferase genes identified, located on at least five chromosomes.
- Recombinant SULTs exhibit substrate specificity linked to metabolism of hormones (estrogen, corticoid, thyroxine) and xenobiotics.
- Genetic polymorphisms identified in human SULTs ST1A2, ST1A3, and ST2A3.
Conclusions:
- Human cytosolic sulfotransferases play a significant role in the metabolism of hormones and xenobiotics.
- The diversity of SULTs suggests specialized functions in detoxification and endogenous compound regulation.
- Observed genetic polymorphisms may influence individual responses to drugs and environmental factors.