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Anne H van der Spek Department of Endocrinology and Metabolism, Academic Medical Center, Amsterdam, The Netherlands

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Eric Fliers Department of Endocrinology and Metabolism, Academic Medical Center, Amsterdam, The Netherlands

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Anita Boelen Department of Endocrinology and Metabolism, Academic Medical Center, Amsterdam, The Netherlands

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distribution have been observed between humans and rodents ( Bernal et al . 2015 ). After being transported into the cell, TH is metabolized by the iodothyronine deiodinases. This a family of enzymes that remove an iodine atom from the phenolic or tyrosyl

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-16-0462
Volume/Issue:
Volume 232: Issue 2
Free access
Aurea Orozco
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Carlos Valverde-R
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Aurora Olvera
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Carlota García-G Instituto de Neurobiología, Departamento de Investigación Biomédica, Universidad Nacional Autónoma de México (UNAM), Boulevard Juriquilla 3001, Juriquilla, Querétaro 76230, México

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iodothyronine deiodinases (Ds). Indeed, iodothyronine deiodination is the essential first step in the pre-receptor control mechanism of TH action ( Nobel et al . 2001 ). From an evolutionary perspective, Ds may be considered pivotal players in the emergence and

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-12-0258
Volume/Issue:
Volume 215: Issue 2
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Veerle M Darras Animal Physiology and Neurobiology Section, Department of Biology, Laboratory of Comparative Endocrinology, KU Leuven, Naamsestraat 61, PO Box 2464, B-3000 Leuven, Belgium

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Stijn L J Van Herck Animal Physiology and Neurobiology Section, Department of Biology, Laboratory of Comparative Endocrinology, KU Leuven, Naamsestraat 61, PO Box 2464, B-3000 Leuven, Belgium

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1, type 2 and type 3 iodothyronine deiodinase (D1, D2 and D3). Two of these enzyme types are selective: D2 only catalyses outer ring deiodination (ORD) while D3 only catalyses inner ring deiodination (IRD). The D1 enzyme is non-selective and

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-12-0204
Volume/Issue:
Volume 215: Issue 2
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Type 1 iodothyronine deiodinase in human physiology and disease

Deiodinases: the balance of thyroid hormone

Ana Luiza Maia Endocrine Division, Thyroid Section, Serviço de Endocrinologia, Hospital de Clínicas de Porto Alegre, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos, 2350, CEP 90035-003 Porto Alegre, RS, Brazil

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Iuri Martin Goemann Endocrine Division, Thyroid Section, Serviço de Endocrinologia, Hospital de Clínicas de Porto Alegre, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos, 2350, CEP 90035-003 Porto Alegre, RS, Brazil

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Erika L Souza Meyer Endocrine Division, Thyroid Section, Serviço de Endocrinologia, Hospital de Clínicas de Porto Alegre, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos, 2350, CEP 90035-003 Porto Alegre, RS, Brazil

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Simone Magagnin Wajner Endocrine Division, Thyroid Section, Serviço de Endocrinologia, Hospital de Clínicas de Porto Alegre, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos, 2350, CEP 90035-003 Porto Alegre, RS, Brazil

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3 ). In euthyroid individuals, the conversion of peripheral T 4 to T 3 accounts for 80% of all the T 3 produced. This critical step in thyroid hormone metabolism is catalyzed by two enzymes, the type 1 and type 2 iodothyronine deiodinases (D1 and

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-10-0481
Volume/Issue:
Volume 209: Issue 3
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Branka Šošić-Jurjević
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Branko Filipović
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Kostja Renko Department of Cytology, Institut für Experimentelle Endokrinologie, Institute for Biological Research ‘Siniša Stanković’, University of Belgrade, Despot Stefan Boulevard 142, 11000 Belgrade, Serbia

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Vladimir Ajdžanović
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Milica Manojlović-Stojanoski
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Verica Milošević
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Josef Köhrle Department of Cytology, Institut für Experimentelle Endokrinologie, Institute for Biological Research ‘Siniša Stanković’, University of Belgrade, Despot Stefan Boulevard 142, 11000 Belgrade, Serbia

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Introduction Homeostasis of thyroid hormone (TH) status is regulated by systemic control of TH release from the thyroid and by local enzymatic activation and inactivation of TH in extrathyroidal tissues that is catalyzed by iodothyronine deiodinase

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-12-0336
Volume/Issue:
Volume 215: Issue 2
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Emmely M de Vries Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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Eric Fliers Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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Anita Boelen Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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decrease precede the decrease in circulating TH levels ( Fekete et al . 2005 ). A striking observation that has been linked to the illness induced TRH decrease is a marked increase in type 2 deiodinase (D2/ Dio2 ) mRNA expression both in tanycytes

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-15-0133
Volume/Issue:
Volume 225: Issue 3
Free access
Audrey Lamirand INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France

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Martine Ramaugé INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France

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Michel Pierre INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France

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Françoise Courtin INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France
INSERM UMR 788, INSERM UMR 854, University Paris-Sud 11, Stéroïdes, neuroprotection et neurogénération, 94275 Le Kremlin-Bicêtre cedex, France

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Introduction Type 2 iodothyronine deiodinase (D2) catalyzes the 5′-deiodination of thyroxine (T 4 ) into the active form of thyroid hormones, 3,5,3′-triiodothyronine (T 3 ; Bianco et al . 2002 , Gereben et al . 2008 ). Notably, in the brain most

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-10-0218
Volume/Issue:
Volume 208: Issue 2
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J Kwakkel
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H C van Beeren
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M T Ackermans Department of Endocrinology and Metabolism, Laboratory of Endocrinology, Department of Clinical Chemistry, Academic Medical Center, University of Amsterdam, F5-165, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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M C Platvoet-ter Schiphorst
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E Fliers
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W M Wiersinga
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A Boelen
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remains unchanged or even decreases. Furthermore, the expression of deiodinating enzymes changes in various tissues ( Wiersinga 2005 ). Deiodinase type 2 (D2; listed as Dio2 in MGI Database) is one of the three known deiodinases. It converts the

Article Type:
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DOI:
https://doi.org/10.1677/JOE-09-0118
Volume/Issue:
Volume 203: Issue 2
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Bo Zhu Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Ashutosh Shrivastava Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Cristina Luongo Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Ting Chen Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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John W Harney Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Alessandro Marsili Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Thuy-Van Tran Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Anulika Bhadouria Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Radhika Mopala Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Amanda I Steen Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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P Reed Larsen Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Ann Marie Zavacki Division of Endocrinology, Diabetes and Hypertension, Thyroid Section, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA

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Introduction The iodothyronine deiodinases are selenoenzymes that modulate tri-iodothyronine (T 3 ) concentrations by catalyzing both its production and degradation ( Bianco et al . 2002 , Gereben et al . 2008 ). Thyroxine (T 4 ) is activated via

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-11-0459
Volume/Issue:
Volume 214: Issue 1
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Local control of thyroid hormone action: role of type 2 deiodinase

Deiodinases: the balance of thyroid hormone

Graham R Williams Molecular Endocrinology Group, Department of Medicine and Medical Research Council Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Commonwealth Building 7th Floor, Du Cane Road, London W12 0NN, UK

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J H Duncan Bassett Molecular Endocrinology Group, Department of Medicine and Medical Research Council Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Commonwealth Building 7th Floor, Du Cane Road, London W12 0NN, UK

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3 is catalyzed by the type 2 iodothyronine deiodinase enzyme (DIO2), while the type 3 enzyme (DIO3) prevents activation of T 4 and inactivates T 3 . This pre-receptor control of ligand availability to TRs in target cells is a crucial mechanism that

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-10-0448
Volume/Issue:
Volume 209: Issue 3
Free access