Control of Thyroid Hormone Activation and Inactivation by the Iodothyronine Deiodinase Family of Selenoenzymes View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2011

AUTHORS

Ann Marie Zavacki , Alessandro Marsili , P. Reed Larsen

ABSTRACT

The iodothyronine deiodinases both activate and inactivate thyroid hormone, thus controlling thyroid hormone action. These enzymes are also selenoproteins, containing the rare amino acid selenocysteine in their active center. SBP-2 is an important component of the selenoprotein synthesis machinery, and its binding to selenocysteine insertion sequence (SECIS) elements is crucial for selenocysteine incorporation at the UGA codon vs. termination. Recently, several patients have been identified with impaired selenoprotein synthesis due to mutations in SBP-2. One hallmark of this syndrome, found in all patients to date, is abnormal serum thyroid hormone profiles, with low 3,3′,5-triiodothyronine (T3), elevated thyroxine (T4), and inappropriately normal or elevated TSH due to alterations in deiodinase activity. Thus, the constraints that influence selenoprotein synthesis are also relevant to thyroid hormone metabolism. New work in the deiodinase field is also advancing the paradigm that the type 2 deiodinase (D2), the thyroid hormone activating enzyme, and the type 3 deiodinase (D3) the thyroid-inactivating enzyme, play an important role in the modulation of T3 locally within a tissue, without changing circulating levels of T3. One recent example of this can be found in the role D2 plays in providing intracellular T3 necessary during muscle differentiation and regeneration. We have recently shown that in primary muscle precursor cells D2 increases prior to the upregulation of other T3-dependent genes that are necessary for muscle differentiation such as MyoD. Further, when D2 activity is knocked down in this system via an RNAi strategy, myoblast differentiation is dramatically impaired. We have also found that in a mouse model of muscle injury D2 activity increases transiently when muscle is regenerating, and declines when this process is complete. Remarkably, in mice without D2 (D2 knockout) there is a significant delay in muscle repair after injury. While wild type animals have completed the regeneration process by 15 days after injury, D2 knockout mice had a much greater number of newly formed centrally nucleated immature myofibers, indicating an impairment in the muscle differentiation process. Thus, the impaired expression of selenoproteins such as the deiodinases can result in alterations in both circulating and intracellular levels of thyroid hormone leading to significant pathophysiologic consequences. More... »

PAGES

369-381

Book

TITLE

Selenium

ISBN

978-1-4614-1024-9
978-1-4614-1025-6

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4614-1025-6_29

DOI

http://dx.doi.org/10.1007/978-1-4614-1025-6_29

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038190360


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