ArticleEuropean journal of drug metabolism and pharmacokinetics2021
Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17β-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.
Article in European journal of drug metabolism and pharmacokinetics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Functional and Mechanistic Studies of theBiology · 2026Article
- Impact of genetic polymorphisms on the sulfation of dehydroepiandrosterone and 17-β estradiol by human cytosolic sulfotransferase SULT2B1a.Pharmacogenetics and genomics · 2026Article
- Impact of Complex Genetic and Drug-Drug Interactions on Tamoxifen Metabolism and Efficacy.Journal of personalized medicine · 2025Review
- Steroid sulfatase and sulfotransferases in the estrogen and androgen action of gynecological cancers: current status and perspectives.Essays in biochemistry · 2024Review
- Estrogen sulfotransferase and sulfatase in steroid homeostasis, metabolic disease, and cancer.Steroids · 2024Review
- SULT genetic polymorphisms: physiological, pharmacological and clinical implications.Expert opinion on drug metabolism & toxicology · 2021Review
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
BACKGROUND AND
objectivesPrevious studies have revealed that sulfation, as mediated by the estrogen-sulfating cytosolic sulfotransferase (SULT) SULT1E1, is involved in the metabolism of 17β-estradiol (E2), 4-hydroxytamoxifen (4OH-tamoxifen), and diethylstilbestrol in humans. It is an interesting question whether the genetic polymorphisms of SULT1E1, the gene that encodes the SULT1E1 enzyme, may impact on the metabolism of E2 and these two drug compounds through sulfation.
methodsIn this study, five missense coding single nucleotide polymorphisms of the SULT1E1 gene were selected to investigate the sulfating activity of the coded SULT1E1 allozymes toward E2, 4OH-tamoxifen, and diethylstilbestrol. Corresponding cDNAs were generated by site-directed mutagenesis, and recombinant SULT1E1 allozymes were bacterially expressed, affinity-purified, and characterized using enzymatic assays.
resultsPurified SULT1E1 allozymes were shown to display differential sulfating activities toward E2, 4OH-tamoxifen, and diethylstilbestrol. Kinetic analysis revealed further distinct K
conclusionsTaken together, these findings highlighted the significant differences in E2-, as well as the drug-sulfating activities of SULT1E1 allozymes, which may have implications in the differential metabolism of E2, 4OH-tamoxifen, and diethylstilbestrol in individuals with different SULT1E1 genotypes.
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