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Cyril S Anyetei-Anum Department of Biology, College of William and Mary, Williamsburg, Virginia, USA

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Vincent R Roggero Department of Biology, College of William and Mary, Williamsburg, Virginia, USA

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Lizabeth A Allison Department of Biology, College of William and Mary, Williamsburg, Virginia, USA

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, Mullur et al . 2014 , Mondal et al . 2016 , Mendoza & Hollenberg 2017 , van der Spek et al . 2017 ). Much of thyroid hormone action is mediated by the thyroid hormone receptors (TRs), members of the nuclear receptor superfamily that act as ligand

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-17-0708
Volume/Issue:
Volume 237: Issue 1
Free access
Ángela Sánchez Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain

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Constanza Contreras-Jurado Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain
Centro de Investigación Biomédica en Red de Cáncer (CIBERONC), Madrid, Spain

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Diego Rodríguez Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain

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Javier Regadera Department of Anatomy, Histology and Neuroscience, Universidad Autónoma de Madrid, Madrid, Spain

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Susana Alemany Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain

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Ana Aranda Instituto de Investigaciones Biomédicas ‘Alberto Sols’, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain
Centro de Investigación Biomédica en Red de Cáncer (CIBERONC), Madrid, Spain

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triiodothyronine (T3) are initiated by binding to the nuclear thyroid hormone receptors (TRs), encoded by the TRα and TRβ genes, which result in several isoforms with different expression and functions ( Aranda & Pascual 2001 , Aranda et al . 2013 , Pascual

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-19-0339
Volume/Issue:
Volume 244: Issue 1
Restricted access
Ana Sofia Rocha IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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Ricardo Marques IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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Inês Bento IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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Ricardo Soares IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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João Magalhães IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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Inês Vieira de Castro IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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Paula Soares IPATIMUP, Institute of Molecular Pathology and Immunology of the University of Porto, Rua Roberto Frias s/n, 4200-065 Porto, Portugal
Department of Pathology, Hospital São João, Porto, Portugal
Department of Pathology, Medical Faculty, University of São Paulo, São Paulo, Brazil
Department of Pathology, Medical Faculty, University of Porto, Porto, Portugal

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( Castro et al. 2006 ). At variance with PTC, a mouse model for FTC was lacking until Kaneshige et al. (2000) described a mutant mouse with a mutation ( PV ) targeted to the thyroid hormone receptor β (THRB) locus. In a heterozygous condition

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-06-0009
Volume/Issue:
Volume 192: Issue 1
Free access
Suzana T Cunha Lima Diabetes Center, Instituto de Biologia, Centro Universitário da Bahia ‐ FIB, University of California, 513 Parnassus Avenue, 94143 San Francisco, California, USA
Diabetes Center, Instituto de Biologia, Centro Universitário da Bahia ‐ FIB, University of California, 513 Parnassus Avenue, 94143 San Francisco, California, USA

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Edson D Rodrigues Diabetes Center, Instituto de Biologia, Centro Universitário da Bahia ‐ FIB, University of California, 513 Parnassus Avenue, 94143 San Francisco, California, USA
Diabetes Center, Instituto de Biologia, Centro Universitário da Bahia ‐ FIB, University of California, 513 Parnassus Avenue, 94143 San Francisco, California, USA

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Introduction The nuclear receptor (NR) family of transcription factors includes receptors for thyroid hormone (TH), steroids, vitamins A and D, and other small hydrophobic molecules ( Laudet & Gronemeyer 2002 ). NRs play widespread roles in growth

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-11-0019
Volume/Issue:
Volume 210: Issue 1
Free access
Bénédicte Rabier INSERM U577-Biomatériaux et Réparation Tissulaire, Université Bordeaux 2 Victor Segalen, Zone Nord, Bâtiment 4A, 2ème étage, 33076 Bordeaux Cedex, France
Université Victor Segalen Bordeaux 2, Bordeaux, France
Molecular Endocrinology Group, Division of Medicine, Faculty of Medicine, MRC Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK
Laboratoire de Biologie et Ingénierie du Cartilage, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/UCBLyon 1, 7 passage du Vercors, 69367 Lyon Cedex 07, France

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Allan J Williams INSERM U577-Biomatériaux et Réparation Tissulaire, Université Bordeaux 2 Victor Segalen, Zone Nord, Bâtiment 4A, 2ème étage, 33076 Bordeaux Cedex, France
Université Victor Segalen Bordeaux 2, Bordeaux, France
Molecular Endocrinology Group, Division of Medicine, Faculty of Medicine, MRC Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK
Laboratoire de Biologie et Ingénierie du Cartilage, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/UCBLyon 1, 7 passage du Vercors, 69367 Lyon Cedex 07, France

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Frederic Mallein-Gerin INSERM U577-Biomatériaux et Réparation Tissulaire, Université Bordeaux 2 Victor Segalen, Zone Nord, Bâtiment 4A, 2ème étage, 33076 Bordeaux Cedex, France
Université Victor Segalen Bordeaux 2, Bordeaux, France
Molecular Endocrinology Group, Division of Medicine, Faculty of Medicine, MRC Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK
Laboratoire de Biologie et Ingénierie du Cartilage, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/UCBLyon 1, 7 passage du Vercors, 69367 Lyon Cedex 07, France

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Graham R Williams INSERM U577-Biomatériaux et Réparation Tissulaire, Université Bordeaux 2 Victor Segalen, Zone Nord, Bâtiment 4A, 2ème étage, 33076 Bordeaux Cedex, France
Université Victor Segalen Bordeaux 2, Bordeaux, France
Molecular Endocrinology Group, Division of Medicine, Faculty of Medicine, MRC Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK
Laboratoire de Biologie et Ingénierie du Cartilage, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/UCBLyon 1, 7 passage du Vercors, 69367 Lyon Cedex 07, France

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O Chassande INSERM U577-Biomatériaux et Réparation Tissulaire, Université Bordeaux 2 Victor Segalen, Zone Nord, Bâtiment 4A, 2ème étage, 33076 Bordeaux Cedex, France
Université Victor Segalen Bordeaux 2, Bordeaux, France
Molecular Endocrinology Group, Division of Medicine, Faculty of Medicine, MRC Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK
Laboratoire de Biologie et Ingénierie du Cartilage, Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/UCBLyon 1, 7 passage du Vercors, 69367 Lyon Cedex 07, France

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plate remain unclear. In vivo , thyroid hormones regulate expression of parathyroid hormone related peptide (PTHrP) and PTHrP receptors, which control the pace of chondrocyte proliferation during endochondral ossification ( Stevens et al. 2000 ). In

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06838
Volume/Issue:
Volume 191: Issue 1
Free access
J Kwakkel
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O Chassande Department of Endocrinology and Metabolism, Academic Medical Center University of Amsterdam, INSERM U 577, Université Victor Segalen Bordeaux 2, F5-165, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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H C van Beeren
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W M Wiersinga
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A Boelen
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. Table 1 Basal laboratory values of thyroid hormone receptor (TRβ −/− ) and wild-type (WT) mice. Mean values± s.e.m. are given Wild-type TRβ −/− ♀ ♂ ♀ ♂ Serum T 3 (nmol/l) 1.55±0.34 1.34±0.14 2.53±0.24* 2.68±0.21 † Serum T 4 (nmol/l) 67±6 57±4 133

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0601
Volume/Issue:
Volume 197: Issue 1
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Marcelo A Christoffolete
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Márton Doleschall Human and Natural Sciences Center, Laboratory of Endocrine Neurobiology, Division of Endocrinology, Division of Endocrinology, Federal University of ABC, Santo Andre-SP 09210-370, Brazil

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Péter Egri Human and Natural Sciences Center, Laboratory of Endocrine Neurobiology, Division of Endocrinology, Division of Endocrinology, Federal University of ABC, Santo Andre-SP 09210-370, Brazil

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Zsolt Liposits Human and Natural Sciences Center, Laboratory of Endocrine Neurobiology, Division of Endocrinology, Division of Endocrinology, Federal University of ABC, Santo Andre-SP 09210-370, Brazil

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Ann Marie Zavacki Human and Natural Sciences Center, Laboratory of Endocrine Neurobiology, Division of Endocrinology, Division of Endocrinology, Federal University of ABC, Santo Andre-SP 09210-370, Brazil

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Antonio C Bianco Human and Natural Sciences Center, Laboratory of Endocrine Neurobiology, Division of Endocrinology, Division of Endocrinology, Federal University of ABC, Santo Andre-SP 09210-370, Brazil

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Balázs Gereben Human and Natural Sciences Center, Laboratory of Endocrine Neurobiology, Division of Endocrinology, Division of Endocrinology, Federal University of ABC, Santo Andre-SP 09210-370, Brazil

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Introduction Thyroid hormone receptor (TR) and liver X-receptors (LXRs) are the key regulators of lipid metabolism. Both these receptors prefer to bind to a direct repeat of the consensus DNA-binding site separated by a 4 bp spacing (DR-4), and thus

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0448
Volume/Issue:
Volume 205: Issue 2
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C R Liu Key Laboratory of Hormones and Development, Department of Pathology, Ministry of Health China, Endocrinology Institute of Tianjin Medical University, Tianjin Medical Institute, Tianjin 300070, China

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L Y Li
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F Shi
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X Y Zang
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Y M Liu Key Laboratory of Hormones and Development, Department of Pathology, Ministry of Health China, Endocrinology Institute of Tianjin Medical University, Tianjin Medical Institute, Tianjin 300070, China

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Y Sun
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B H Kan
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-affinity thyroid hormone receptor (TR) located in the nucleus. TR plays an important role in mediating the cardiac physiologic actions of T 3 ( Sussman 2001 , Dillmann 2002 ). Normal thyroid hormone level is essential for maintaining normal heart structure and

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0253
Volume/Issue:
Volume 195: Issue 3
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J Kwakkel Department of Endocrinology and Metabolism, Academic Medical Center F5-165, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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W M Wiersinga Department of Endocrinology and Metabolism, Academic Medical Center F5-165, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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A Boelen Department of Endocrinology and Metabolism, Academic Medical Center F5-165, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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decreased activity of liver D1 therefore contributes to low serum T 3 levels. TRβ1, one of the thyroid hormone receptors through which T 3 exerts its actions in the liver, is also downregulated in an animal model of NTI. This suggests that impaired T 3

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-06-0177
Volume/Issue:
Volume 194: Issue 2
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Sylvia V H Grommen
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Lutgarde Arckens Research Group of Comparative Endocrinology, Research Group of Neuroplasticity and Neuroproteomics, Animal Physiology and Neurobiology Section, Department of Biology, K U Leuven, Naamsestraat 61, B-3000 Leuven, Belgium

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Tim Theuwissen Research Group of Comparative Endocrinology, Research Group of Neuroplasticity and Neuroproteomics, Animal Physiology and Neurobiology Section, Department of Biology, K U Leuven, Naamsestraat 61, B-3000 Leuven, Belgium

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Veerle M Darras
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Bert De Groef
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TRβ2 FAM-AGTCCACTGATTATTGC-NFQ-MGB bp 85–100 β-actin FAM-CCCCAGACATCAGGGT-NFQ-MGB bp 179–194 The EMBL accession number is indicated in parentheses beside each gene. TRβ2, thyroid hormone receptor β2; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; FAM

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-07-0443
Volume/Issue:
Volume 196: Issue 3
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