Sulfate Transfer to Thyroid Hormones and Their Analogs by Hepatic Aryl Sulfotransferases
Abstract
The transfer of sulfate to thyroid hormones and their analogs by a monkey hepatocarcinoma cell extract was compared to this reaction as catalyzed by two homogeneous aryl sulfotransferases from rat liver. The thyroid hormones 3,5,3'-triiodo-L-thyronine and L-T4 as well as analogs of these hormones, were used as substrates. While these compounds vary widely in their capacity as sulfate acceptors, the catalytic abilities of the three enzyme preparations generally reflect a broad pattern of overlapping specificity. The finding that T4 is a very poor substrate, that 3'-iodothyronine and 3,3'-diiodothyronine are very good substrates, and that T3 is intermediate in its acceptor activity probably explains the relative sulfation of these compounds in vivo and by living hepatocytes. (Endocrinology 108: 454, 1981)
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The phenolic hydroxyl within the T3 molecule can be sulfated (T3-S), a reaction that inactivates T3 but dramatically enhances its solubility in water and loss to the environment.
“The first molecule takes advantage of the fact that the phenolic hydroxyl within the T3 molecule can be sulfated (T3-S), a reaction that inactivates T3 but dramatically enhances its solubility in water and loss to the environment (57).”
From Emerging Therapies in Hypothyroidism (2024) · cites this paper as [57]
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Rapid and selective inner ring deiodination of thyroxine sulfate by rat-liver deiodinase
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Hydrolysis of iodothyronine conjugates by intestinal bacteria
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Desulfation of 3,5,3-triiodothyronine sulfate by microsomes from human and rat tissues
KUNG, M.-P., SPAULDING, S. W., & ROTH, J. A. (1988) · Endocrinology · doi:10.1210/endo-122-4-1195 · Cited by 42 · see citing works
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Bianco, A. C. (2024) · Annual Review of Medicine · doi:10.1146/annurev-med-060622-101007 · Cited by 36 · see citing works
- Authors
- SEKURA, R. D., SATO, K., CAHNMANN, H. J., ROBBINS, J., & JAKOBY, W. B.
- Affiliations
- National Institutes of Health (US)
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1981-02
- Volume
- 108
- Issue
- 2
- Pages
- 454-456
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2093483447
- Cited by
- 58
- References
- 0
- Citations by year
- 2025: 1 · 2023: 2 · 2019: 1 · 2017: 1 · 2016: 1 · 2014: 1 · 2012: 1
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- aryl sulfotransferase, thyroid hormones, 3,5,3'-triiodothyronine, thyroxine, 3,3'-diiodothyronine, enzyme substrate specificity, rat liver
- MeSH terms
- Animals, Haplorhini, Cell Line, Cytoplasm, Liver, Liver Neoplasms, Experimental, Phenols, Phosphoadenosine Phosphosulfate, Sulfurtransferases, Thyroid Hormones, Thyronines, Thyroxine, Triiodothyronine, Arylsulfotransferase, Rats, In Vitro Techniques
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