Thyroid hormone biosynthesis and release
Abstract
Thyroid hormones (TH) 3,5,3',5'- tetraiodothyronine or thyroxine (T4) and 3,5,3'- triiodothyronine (T3) contain iodine atoms as part of their structure, and their synthesis occur in the unique structures called thyroid follicles. Iodide reaches thyroid cells through the bloodstream that supplies the basolateral plasma membrane of thyrocytes, where it is avidly taken up through the sodium/iodide symporter (NIS). Thyrocytes are also specialized in the secretion of the high molecular weight protein thyroglobulin (TG) in the follicular lumen. The iodination of the tyrosyl residues of TG preceeds TH biosynthesis, which depends on the interaction of iodide, TG, hydrogen peroxide (H 2 O 2 ) and thyroid peroxidase (TPO) at the apical plasma membrane of thyrocytes. Thyroid hormone biosynthesis is under the tonic control of thyrotropin (TSH), while the iodide recycling ability is very important for normal thyroid function. We discuss herein the biochemical aspects of TH biosynthesis and release, highlighting the novel molecules involved in the process.
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Hormone synthesis from thyroglobulin occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines and is completed by TG proteolysis.
“Hormone synthesis from thyroglobulin (TG) occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines and is completed by TG proteolysis3.”
From The structure of human thyroglobulin (2020) · cites this paper as [3]
TPO utilizes H2O2 generated by DUOX/DUOXA to catalyze the oxidation of I- and subsequent iodination of tyrosine residues of soluble TG molecules nearby.
“TPO utilizes H2O2 generated by DUOX/DUOXA to catalyze the oxidation of I- and subsequent iodination of the tyrosine residues of soluble TG molecules nearby (60).”
From Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion (2022) · cites this paper as [60]
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The structure of human thyroglobulin
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Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion
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- Authors
- Carvalho, D. P., & Dupuy, C.
- Affiliations
- Universidade Federal do Rio de Janeiro (BR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Carvalho, Denise P.
- Venue
- Molecular and Cellular Endocrinology
- Publisher
- Elsevier BV
- Published
- 2017-12
- Volume
- 458
- Pages
- 6-15
- ISSN
- 0303-7207 (ISSN-L)
- OpenAlex
- W2585303886
- Cited by
- 346
- References
- 3
- Citations by year
- 2026: 35 · 2025: 35 · 2024: 53 · 2023: 37 · 2022: 53 · 2021: 54 · 2020: 27 · 2019: 31 · 2018: 14 · 2017: 6 · 2014: 1
- FWCI
- 16.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular and Cellular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (472630/2012-1)
- Ligue Contre le Cancer
- Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (26/010.001.252/2015)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Cancer Diagnosis and Treatment
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Chemical Analysis and Environmental Impact
- Keywords
- thyroid hormone synthesis, thyroxine, triiodothyronine, thyroglobulin, sodium iodide symporter, thyroid peroxidase, iodide uptake, thyroid-stimulating hormone, thyroid follicles, thyroid follicular cells, hormone secretion
- MeSH terms
- Thyroid Epithelial Cells, Sodium-Iodide Symporters, Animals, Autoantigens, Cell Membrane, Humans, Iodide Peroxidase, Thyroid Hormones, Thyroxine, Triiodothyronine, Molecular Structure, Chloride Channels, Symporters, Iron-Binding Proteins
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