The DOI matches its Crossref record; 507 of the 531 references it cites were found in a registry or an index.
Biochemistry, Cellular and Molecular Biology, and Physiological Roles of the Iodothyronine Selenodeiodinases
Abstract
The goal of this review is to place the exciting advances that have occurred in our understanding of the molecular biology of the types 1, 2, and 3 (D1, D2, and D3, respectively) iodothyronine deiodinases into a biochemical and physiological context. We review new data regarding the mechanism of selenoprotein synthesis, the molecular and cellular biological properties of the individual deiodinases, including gene structure, mRNA and protein characteristics, tissue distribution, subcellular localization and topology, enzymatic properties, structure-activity relationships, and regulation of synthesis, inactivation, and degradation. These provide the background for a discussion of their role in thyroid physiology in humans and other vertebrates, including evidence that D2 plays a significant role in human plasma T(3) production. We discuss the pathological role of D3 overexpression causing "consumptive hypothyroidism" as well as our current understanding of the pathophysiology of iodothyronine deiodination during illness and amiodarone therapy. Finally, we review the new insights from analysis of mice with targeted disruption of the Dio2 gene and overexpression of D2 in the myocardium.
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In the citing paper
“Due to alterations in rates of local deiodination in tissues, thyroid hormone signaling can change irrespective of serum hormonal concentrations (3, 5).”
From Can Reverse T3 Assay Be Employed to Guide T4 vs. T4/T3 Therapy in Hypothyroidism? (2019) · cites this paper as [3]
In the citing paper
“Of note, the D1 gene is upregulated by T3, and thus in hyperthyroidism the proportion of circulating T3 arising from the D1 pathway is significantly increased (11).”
From Guidelines for the Treatment of Hypothyroidism: Prepared by the American Thyroid Association Task Force on Thyroid Hormone Replacement (2014) · cites this paper as [11]
In the citing paper
“A third deiodinase, type 3 deiodinase (D3) participates in the clearance of both serum T4 and T3 (11).”
From Guidelines for the Treatment of Hypothyroidism: Prepared by the American Thyroid Association Task Force on Thyroid Hormone Replacement (2014) · cites this paper as [11]
In the citing paper
“The in-sufficient peripheral T3 production cannot be appropriately corrected by increasing L-T4 dose, because the inhibitory effect of elevated T4 on D2 [28,30,69] will end up increasing the imbalance of serum free T4 to free T3 ratio [67] .”
From 2012 ETA Guidelines: The Use of L-T4 + L-T3 in the Treatment of Hypothyroidism (2012) · cites this paper as [69]
In the citing paper
“with the thyroid producing only ∼5 mcg T3”
From Liothyronine and Desiccated Thyroid Extract in the Treatment of Hypothyroidism (2020) · cites this paper as [32]
In the citing paper
“an additional ∼25 mcg T3 is produced daily outside of the thyroid parenchyma via T4 deiodination (32).”
From Liothyronine and Desiccated Thyroid Extract in the Treatment of Hypothyroidism (2020) · cites this paper as [32]
In the citing paper
“The daily T3 production in a 70-kg healthy adult is ∼30 mcg”
From Liothyronine and Desiccated Thyroid Extract in the Treatment of Hypothyroidism (2020) · cites this paper as [32]
In the citing paper
“FT3 measurement has somewhat limited utility, however, in the diagnosis of hypothyroidism, since FT3 values often fall in the normal range as a result of hyperstimulation of the remaining functioning thyroid tissue by elevated TSH and to up-regulation of deiodinase D2”
From Diagnosis and management of treatment-refractory hypothyroidism: an expert consensus report (2017) · cites this paper as [25]
In the citing paper
“Similarly, deiodinases in central and peripheral tissues are also regulated differently, enhancing T3 conversion and providing a differentiated mechanism for oversensitively responding to changes in FT4 in the feedback loop (55–63).”
From Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment (2015) · cites this paper as [57]
In the citing paper
“T3 supply is locally controlled by several mechanisms, such as active thyroid hormone uptake, tissue-specific expression and activity of two distinct types of deiodinases converting T3 from T4, and thyroid hormone inactivation by deiodination or degradation by sulfatation, deamination, or glucoronidation (57–66).”
From Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment (2015) · cites this paper as [57]
In the citing paper
“The regulation varies by tissue as the brain predominantly expresses type 2 deiodinase, whereas type 1 deiodinase is abundant in other tissues of the body, and by thyroid state, as T3 excess upregulates type 1 deiodinase but downregulates type 2 deiodinase, which is upregulated in hypothyroidism (57–64).”
From Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment (2015) · cites this paper as [57]
In the citing paper
“The regulation varies by tissue as the brain predominantly expresses type 2 deiodinase, whereas type 1 deiodinase is abundant in other tissues of the body, and by thyroid state, as T3 excess upregulates type 1 deiodinase but downregulates type 2 deiodinase, which is upregulated in hypothyroidism (57–64).”
From Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment (2015) · cites this paper as [57]
In the citing paper
“The regulation varies by tissue as the brain predominantly expresses type 2 deiodinase, whereas type 1 deiodinase is abundant in other tissues of the body, and by thyroid state, as T3 excess upregulates type 1 deiodinase but downregulates type 2 deiodinase, which is upregulated in hypothyroidism (57–64).”
From Homeostatic control of the thyroid-pituitary axis: perspectives for diagnosis and treatment (2015) · cites this paper as [57]
In the citing paper
“the conversion of T 4 to T 3 in the brain is catalyzed by D2 (94)”
From Central regulation of hypothalamic-pituitary-thyroid axis under physiological and pathophysiological conditions (2014) · cites this paper as [94]
In the citing paper
“In the cortex, for example, hypothyroidism up-regulates D2 activity to produce more T 3 , whereas hyperthyroidism down-regulates D2 activity (94)”
From Central regulation of hypothalamic-pituitary-thyroid axis under physiological and pathophysiological conditions (2014) · cites this paper as [94]
In the citing paper
“Primarily, deiodination of T4’s outer ring by type 2 deiodinase (DIO2) gives liothyronine (L-tri-iodothyronine or T3, the main biologically active metabolite), and deiodination of the inner ring by type 1 or type 3 deiodinases (DIO1 or DIO3) gives the biologically inactive reverse T3 (rT3) [ 21 ].”
From Factors influencing the levothyroxine dose in the hormone replacement therapy of primary hypothyroidism in adults (2022) · cites this paper as [21]
Citations
Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438
Ingbar, S. H. (1965) · Archives of Internal Medicine · doi:10.1001/archinte.1965.03870060154035 · Cited by 1,745
Dickkopf-1 is a member of a new family of secreted proteins and functions in head induction
Glinka, A., Wu, W., Delius, H., Monaghan, A. P., Blumenstock, C., & Niehrs, C. (1998) · Nature · doi:10.1038/34848 · Cited by 1,608
Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
Enerbäck, S., Jacobsson, A., Simpson, E. M., Guerra, C., Yamashita, H., Harper, M.-E., & Kozak, L. P. (1997) · Nature · doi:10.1038/387090a0 · Cited by 1,379
Squire, L. R. (1986) · Science · doi:10.1126/science.3086978 · Cited by 1,278
Type I iodothyronine deiodinase is a selenocysteine-containing enzyme
Berry, M. J., Banu, L., & Larsen, P. R. (1991) · Nature · doi:10.1038/349438a0 · Cited by 883
Vulsma, T., Gons, M. H., & de Vijlder, J. J. M. (1989) · New England Journal of Medicine · doi:10.1056/nejm198907063210103 · Cited by 795
The Mechanism of Action of Thyroid Hormones
Zhang, J., & Lazar, M. A. (2000) · Annual Review of Physiology · doi:10.1146/annurev.physiol.62.1.439 · Cited by 725
Maternal and Fetal Thyroid Function
Epstein, F. H., Burrow, G. N., Fisher, D. A., & Larsen, P. R. (1994) · New England Journal of Medicine · doi:10.1056/nejm199410203311608 · Cited by 720
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24 of the 531 references couldn’t be matched to a known paper.
Research works printed but not linked: 5
- Berry, 1994, Selenocysteine and the structure, function, and regulation of iodothyronine deiodination: update 1994., Endocr Rev, 3, 265
- Dunn, 1999, Global IDD status., IDD Newsletter, 15, 17
- Ricquier, 1982, Ultrastructural and biochemical characterization of human brown adipose tissue in pheochromocytoma., J Clin Endocrinol Metab, 54, 803
- Young, 1982, Effect of thyroid state on norepinephrine (NE) turnover in rat brown adipose tissue (BAT): potential importance of the pituitary., Clin Res, 32, 407
- Burrow, 1994, Maternal and fetal thyroid function., N Engl J Med, 331, 1072, 10.1056/NEJM199410203311608 · DOI · Paper page
Cited by
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Items 701–800 of 1,006
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Pantos, C. I., Mourouzis, I. S., & Cokkinos, D. V. (2012) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y2012-031 · Cited by 34
Raja, K., & Mugesh, G. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502762 · Cited by 34
Endogenous ways to stimulate brown adipose tissue in humans
Broeders, E. P. M., Bouvy, N. D., & Lichtenbelt, W. D. V. M. (2014) · Annals of Medicine · doi:10.3109/07853890.2013.874663 · Cited by 37
Maia, A. L., Dupuis, J., Manning, A. K., Liu, C., Meigs, J. B., Cupples, L. A., Larsen, P. R., & Fox, C. S. (2007) · Thyroid · doi:10.1089/thy.2006.0298 · Cited by 34
Sánchez, E., Singru, P. S., Fekete, C., & Lechan, R. M. (2008) · Endocrinology · doi:10.1210/en.2007-1697 · Cited by 34
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Fekete, C., Freitas, B. C. G., Zeöld, A., Wittmann, G., Kádár, A., Liposits, Z., Christoffolete, M. A., Singru, P., Lechan, R. M., Bianco, A. C., et al. (2007) · Endocrinology · doi:10.1210/en.2007-0448 · Cited by 33
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State of the art paper Thyroid diseases in patients with acromegaly
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Valverde-R, C., Orozco, A., Becerra, A., Jeziorski, M. C., Villalobos, P., & Solís-S, J. C. (2004) · International Review of Cytology · doi:10.1016/s0074-7696(04)34004-0 · Cited by 28
Chen, Y., Sible, J. C., & McNabb, F. M. A. (2008) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2008.08.014 · Cited by 33
Placental restriction alters circulating thyroid hormone in the young lamb postnatally
Blasio, M. J. D., Gatford, K. L., Robinson, J. S., & Owens, J. A. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00103.2006 · Cited by 33
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Bechtold, D. A., & Loudon, A. S. I. (2007) · Endocrinology · doi:10.1210/en.2007-0596 · Cited by 33
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Alkemade, A. (2009) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2009.01932.x · Cited by 32
Gashu, D., Stoecker, B. J., Adish, A. A., Haki, G. D., Bougma, K., Aboud, F. E., & Marquis, G. S. (2016) · European Journal of Clinical Nutrition · doi:10.1038/ejcn.2016.27 · Cited by 32
Oliveira, L. S. D., & Ritter, M. J. (2024) · Hepatology Communications · doi:10.1097/hc9.0000000000000596 · Cited by 33
Chadio, S. E., Pappas, A. C., Papanastasatos, A., Pantelia, D., Dardamani, A., Fegeros, K., & Zervas, G. P. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.09.010 · Cited by 31
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de Moura, E. G., & de Moura, C. C. P. (2004) · Arquivos Brasileiros de Endocrinologia & Metabologia · doi:10.1590/s0004-27302004000100006 · Cited by 32
Bayse, C. A. (2018) · New Journal of Chemistry · doi:10.1039/c8nj00557e · Cited by 31
Varlamova, E. G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.04.005 · Cited by 32
Bradley, D. P., Liu, J., Blaszczak, A. M., Wright, V. P., Jalilvand, A., NEEDLEMAN, B. J., Noria, S. F., Renton, D., & Hsueh, W. A. (2018) · Journal of Diabetes Research · doi:10.1155/2018/2464652 · Cited by 31
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McNabb, F. M. A., & Darras, V. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-407160-5.00024-5 · Cited by 31
Tiekink, E. R. T. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213586 · Cited by 31
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Ghenimi, N., Alfos, S., Redonnet, A., Higueret, P., Pallet, V., & Enderlin, V. (2010) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2010.02002.x · Cited by 31
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Metadata
- Authors
- Bianco, A. C., Salvatore, D., Gereben, B., Berry, M. J., & Larsen, P. R.
- Affiliations
- Brigham and Women's Hospital (US)
- Federico II University Hospital (IT)
- Institute of Experimental Medicine, Hungarian Academy of Sciences (B.G.), Budapest, H-1083 Hungary
- Corresponding author
- Larsen, P. Reed
- Venue
- Endocrine Reviews
- Publisher
- The Endocrine Society
- Published
- 2002-02-01
- Volume
- 23
- Issue
- 1
- Pages
- 38-89
- ISSN
- 0163-769X (ISSN-L)
- 1945-7189
- OpenAlex
- W2104878795
- Cited by
- 1,853
- References
- 531
- Citations by year
- 2026: 32 · 2025: 59 · 2024: 44 · 2023: 58 · 2022: 88 · 2021: 83 · 2020: 85 · 2019: 81 · 2018: 69 · 2017: 84 · 2016: 82 · 2015: 90 · 2014: 71 · 2013: 69 · 2012: 85
- FWCI
- 12.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Endocrine Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Brigham and Women's Hospital
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK044128, DK36256, DK 58538, DK-44128, R01DK036256, T32DK007529, DK-07529)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Chemical Analysis and Environmental Impact
- Keywords
- iodothyronine deiodinase, selenoprotein biosynthesis, type 2 deiodinase, type 3 deiodinase, type I deiodinase, thyroid hormone metabolism, structure-activity relationship
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Humans, Iodide Peroxidase, Molecular Sequence Data, Polymorphism, Genetic, Proteins, Protein Biosynthesis, Sequence Homology, Amino Acid, Selenoproteins
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