Sulfotransferase 2A1 forms estradiol-17-sulfate and celecoxib switches the dominant product from estradiol-3-sulfate to estradiol-17-sulfate

Wang, Li-Quan; James, Margaret O.

doi:10.1016/j.jsbmb.2005.05.002

Cited by 43Pharmacogenetics and Drug MetabolismEstrogen and related hormone effectsGlutathione Transferases and Polymorphisms

Sulfotransferase 2A1 forms estradiol-17-sulfate and celecoxib switches the dominant product from estradiol-3-sulfate to estradiol-17-sulfate

Wang, Li-Quan, James, Margaret O.·2005·The Journal of Steroid Biochemistry and Molecular Biology

DOI 10.1016/j.jsbmb.2005.05.002

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Abstract

Using recombinant sulfotransferases (SULTs) expressed in E. coli, beta-estradiol (E2) sulfonation was examined to determine which SULT enzyme is responsible for producing E2-17-sulfate (E2-17-S). SULTs 1A1*1, 1A1*2, 1A3, 1E1 and 2A1 all sulfated E2 to varying extents. No activity was observed with SULT1B1. Among the SULTs studied, SULT2A1 produced primarily E2-3-sulfate (E2-3-S), but also some E2-17-S and trace amounts of E2 disulfate. SULT2A1 had a K(m) value of 1.52 microM for formation of E2-3-S and 2.95 microM for formation of E2-17-S. SULT2A1 had the highest V(max) of 493 pmol/min/mg protein for formation of E2-3-S, which was 8.8- and 47-fold higher than the maximal rates of formation of E2-17-S and E2 disulfate, respectively. SULT2A1 formed E2-3-S more efficiently. However, when celecoxib (0-160 microM) was included in the incubation with either SULT2A1 or human liver cytosol, sulfonation switched from E2-3-S to E2-17-S in a concentration-dependent manner. The ratio of E2-17-S/E2-3-S went up to 15 with SULT2A1, and was saturated at 1 with human liver cytosol. In both cases, more E2-17-S was formed, with the unreacted E2 remained unchanged, suggesting celecoxib probably bound to a separate effector site to cause a conformational change in SULT2A1, which favored production of E2-17-S. The ability of celecoxib to alter the position of sulfonation of E2 may in part explain its success in the experimental prevention and treatment of breast cancer.

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Estrogens and catecholestrogens are efficiently sulfated at several positions.
“Estrogens and catecholestrogens are efficiently sulfated at several positions [[325], [326], [327]].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [327]
SULT1A1 and SULT1A3 also sulfate estrogens, but with a lower affinity.
“SULT1E1 is the major SULT for estrogen sulfation [328,329], while SULT1A1 and SULT1A3 also sulfate estrogens, but with a lower affinity [327].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [327]

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HETEROTROPIC MODULATION OF SULFOTRANSFERASE 2A1 ACTIVITY BY CELECOXIB: PRODUCT RATIO SWITCHING OF ETHYNYLESTRADIOL SULFATION
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Authors: Wang, L.-Q., & James, M. O.
Affiliations: University of Florida (US)
Corresponding author: James, Margaret O.
ORCID: James, Margaret O.
Venue: The Journal of Steroid Biochemistry and Molecular Biology
Publisher: Elsevier BV
Published: 2005-09
Volume: 96
Issue: 5
Pages: 367-374
ISSN: 0960-0760 (ISSN-L)
DOI: 10.1016/j.jsbmb.2005.05.002
OpenAlex: W2002627378
Cited by: 43
References: 62
Citations by year: 2024: 2 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 6 · 2016: 2 · 2015: 3 · 2013: 1 · 2012: 4
FWCI: 1.13
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Funders: Univerzita Karlova v Praze
University of Alabama at Birmingham
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords: SULT2A1, celecoxib, enzyme conformational change, human liver cytosol, breast cancer prevention, drug-metabolizing enzyme inhibition
MeSH terms: Celecoxib, Cytosol, Estradiol, Humans, Kinetics, Liver, Phenotype, Pyrazoles, Sulfonamides, Sulfotransferases, Cyclooxygenase Inhibitors

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Sulfotransferase 2A1 forms estradiol-17-sulfate and celecoxib switches the dominant product from estradiol-3-sulfate to estradiol-17-sulfate

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