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Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase
Abstract
A distinct human estrogen sulfotransferase (hEST-1) cDNA has been isolated from a human liver lambda Zap cDNA library using a PCR procedure. The enzymatically active protein has been expressed in two bacterial expression systems and the kinetic and immunologic properties of the enzyme have been characterized. The full-length cDNA for hEST-1 is 994 base pairs in length and encodes a 294 amino acid protein with a calculated molecular mass of 35,123 Da. Purified hEST-1 migrated with an apparent molecular mass of 35,000 Da during SDS-polyacrylamide gel electrophoresis. Immunoblot analysis of hEST-1 expressed in E. coli with a rabbit anti-hEST-1 antibody yields a band of approximately 35,000 Da. The anti-hEST-1 antibody also detects a single band in human liver and jejunum cytosol which migrates with the same molecular mass as expressed hEST-1. There was also no cross-reactivity of hEST-1 with rabbit anti-hP-PST or rabbit anti-hDHEA-ST antibodies upon immunoblot analysis. hEST-1 was expressed in bacteria and purified to homogeneity. Expressed hEST-1 activity has a significantly greater affinity for estrogen sulfation than that found for the other human STs which conjugate estrogens. hEST-1 maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated. The results presented in this paper describe the expression and characterization of a human EST distinct from other human STs which sulfate estrogens. The high affinity of hEST-1 for estrogens indicates that this ST may be important in both the metabolism of estrogens and in the regulation of their activities.
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“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 [329]
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“[328,329], while SULT1A1 and SULT1A3 also sulfate estrogens, but with a lower affinity [327].”
Metadata
- Authors
- Falany, C. N., Krasnykh, V., & Falany, J. L.
- Affiliations
- University of Alabama at Birmingham (US)
- Corresponding author
- Falany, Charles N.
- Venue
- The Journal of Steroid Biochemistry and Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1995-06
- Volume
- 52
- Issue
- 6
- Pages
- 529-539
- ISSN
- 0960-0760 (ISSN-L)
- OpenAlex
- W2130145312
- Cited by
- 220
- References
- 28
- Citations by year
- 2025: 2 · 2024: 4 · 2023: 3 · 2022: 5 · 2021: 3 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 2 · 2015: 6 · 2014: 5 · 2013: 9 · 2012: 7
- FWCI
- 8.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-38953)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Keywords
- cDNA cloning, prokaryotic expression, enzyme kinetics, estrogen sulfation, beta-estradiol, estrone, dehydroepiandrosterone, pregnenolone, ethinyl estradiol, 1-naphthol, steroid metabolism, immunoblot detection
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Escherichia coli, Estrogens, Humans, Kinetics, Liver, Molecular Sequence Data, Molecular Weight, Rabbits, Species Specificity, Substrate Specificity, Sulfotransferases, Gene Expression, Polymerase Chain Reaction, Sequence Homology, Amino Acid, DNA, Complementary
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