Biosynthesis and Function of Thyroid Hormones

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biological Factors".

Deadline for manuscript submissions: 10 January 2025 | Viewed by 664

Special Issue Editors


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Guest Editor
Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Institut für Experimentelle Endokrinologie, Berlin, Germany
Interests: thyroid hormone synthesis, metabolism and action; essential trace elements iodine, selenium and iron; endocrine disruptors and the thyroid hormone system; analytical methods for endocrine-relevant ligands

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Guest Editor
1. Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, Department of Endocrinology and Metabolism, Berlin, Germany
2. DZHK (German Center for Cardiovascular Research), Partner Site Berlin, Berlin, Germany
Interests: local thyroid hormone action on metabolism; thyroid hormones in carbohydrate and lipid metabolism; thyroid hormones in NAFLD and NASH; thyroid hormone transmembrane transport; thyroid hormone metabolism by deiodinases; brain energy metabolism; hypothalamic regulation of metabolism; thyroid gland function

Special Issue Information

Dear Colleagues,

Thyroid hormones (THs) and their metabolites are signaling molecules with a unique structure containing the essential trace element iodine. Due to the biochemical properties of these small tyrosine amino-acid-derived hormones, TH biosynthesis is an extraordinary, evolutionarily conserved process requiring structural and functional features that only the thyroid gland and its angiofollicular units can provide. THs govern major functions in embryonic development, cellular differentiation, and the energy metabolism of all vertebrate organisms and their evolutionary precursors. The effects of endogenous THs are predominantly exerted by the active hormone T3 which binds to intracellular, mainly nuclear, T3 receptors (TRs) that act as transcription factors. While the importance of iodide for the thyroid gland and several physiological effects of THs have already been known for over 100 years, current research on TH biosynthesis and function continues to provide major novel insights into molecular details and structures underlying the processes of generating THs and executing their multiple, clinically relevant functions.

With this Special Issue, we would like to invite and encourage colleagues to provide topical overviews and share novel data on TH biosynthesis—in principle largely known but exceptional in molecular and functional details. The development and adaptable functions of follicular units to endogenous and environmental demands still hold several unexplored research challenges. We would also like to provide the opportunity for long-standing TH researchers as well as colleagues in neighboring research areas to share their knowledge on the function and actions of THs within whole organisms, organs, and cells and to identify and raise open research questions. While there is a good level of knowledge about classic TH target organs, other multicellular organ systems are only on the verge of recognition as relevant TH targets. Therefore, new insights into TH function will certainly generate further opportunities for the utilization and modulation of systemic and local TH availability and activity in physiology and pathophysiology.

Original research and review articles are welcome in this Special Issue.

We look forward to your contributions, which will provide current information on TH biosynthesis and action and broaden the topic.

Prof. Dr. Josef Koehrle
Dr. Eva K. Wirth
Guest Editors

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Keywords

  • thyroid gland
  • thyroid follicle
  • TH release
  • iodide
  • deiodinase
  • TH transmembrane transport
  • TH receptors
  • intracellular TH binding proteins
  • thyroglobulin
  • sodium–iodide symporter
  • thyroperoxidase
  • dual oxidase
  • thyroid-relevant trace elements

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Published Papers (1 paper)

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Research

19 pages, 3370 KiB  
Article
Structural Insights into the Iodothyronine Deiodinase 2 Catalytic Core and Deiodinase Catalysis and Dimerization
by Holly Towell, Doreen Braun, Alexander Brol, Andrea di Fonzo, Eddy Rijntjes, Josef Köhrle, Ulrich Schweizer and Clemens Steegborn
Biomolecules 2024, 14(11), 1373; https://doi.org/10.3390/biom14111373 - 28 Oct 2024
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Abstract
Iodothyronine deiodinases (Dio) are selenocysteine-containing membrane enzymes that activate and inactivate the thyroid hormones (TH) through reductive iodide eliminations. The three deiodinase isoforms are homodimers sharing highly conserved amino acid sequences, but they differ in their regioselectivities for the deiodination reaction and regulatory [...] Read more.
Iodothyronine deiodinases (Dio) are selenocysteine-containing membrane enzymes that activate and inactivate the thyroid hormones (TH) through reductive iodide eliminations. The three deiodinase isoforms are homodimers sharing highly conserved amino acid sequences, but they differ in their regioselectivities for the deiodination reaction and regulatory features. We have now solved a crystal structure of the mouse deiodinase 2 (Dio2) catalytic domain. It reveals a high overall similarity to the deiodinase 3 structure, supporting the proposed common mechanism, but also Dio2-specific features, likely mediating its unique properties. Activity studies with an artificially enforced Dio dimer further confirm that dimerization is required for activity and requires both the catalytic core and the enzyme’s N-terminus. Cross-linking studies reveal the catalytic core’s dimerization interface, providing insights into the architecture of the complete, active Dio homodimer. Full article
(This article belongs to the Special Issue Biosynthesis and Function of Thyroid Hormones)
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