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Helen Garside Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Charlotte Waters Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Andy Berry Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Lisa Rice Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Helen C Ardley Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Anne White Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Philip A Robinson Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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David Ray Endocrine Sciences Research Group and Centre for Molecular Medicine, Faculty of Medicine, University of Manchester, Stopford Building, Oxford Road, Manchester M13 9PT, UK
Molecular Medicine Unit, CSB, St. James’s University Hospital, University of Leeds, Leeds LS9 7TF, UK

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Introduction The glucocorticoid receptor (GR) is a member of the nuclear receptor superfamily. It is a key regulator of many homeostatic mechanisms and is also the target of therapeutic glucocorticoids used to treat inflammatory

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06799
Volume/Issue:
Volume 190: Issue 3
Free access
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
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Akira Takeshita Endocrine Center, Toranomon Hospital and Okinaka Memorial Institute for Medical Research, 2-2-2 Toranomon, Minato, Tokyo 105-8470, Japan
Department of Anatomy and Cell Biology, St Marianna University School of Medicine, Kawasaki, Kanagawa 216-8511, Japan
Department of Integrative Physiology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan

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Keiji Inagaki Endocrine Center, Toranomon Hospital and Okinaka Memorial Institute for Medical Research, 2-2-2 Toranomon, Minato, Tokyo 105-8470, Japan
Department of Anatomy and Cell Biology, St Marianna University School of Medicine, Kawasaki, Kanagawa 216-8511, Japan
Department of Integrative Physiology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan

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Junko Igarashi-Migitaka Endocrine Center, Toranomon Hospital and Okinaka Memorial Institute for Medical Research, 2-2-2 Toranomon, Minato, Tokyo 105-8470, Japan
Department of Anatomy and Cell Biology, St Marianna University School of Medicine, Kawasaki, Kanagawa 216-8511, Japan
Department of Integrative Physiology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan

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Yasunori Ozawa Endocrine Center, Toranomon Hospital and Okinaka Memorial Institute for Medical Research, 2-2-2 Toranomon, Minato, Tokyo 105-8470, Japan
Department of Anatomy and Cell Biology, St Marianna University School of Medicine, Kawasaki, Kanagawa 216-8511, Japan
Department of Integrative Physiology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan

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Noriyuki Koibuchi Endocrine Center, Toranomon Hospital and Okinaka Memorial Institute for Medical Research, 2-2-2 Toranomon, Minato, Tokyo 105-8470, Japan
Department of Anatomy and Cell Biology, St Marianna University School of Medicine, Kawasaki, Kanagawa 216-8511, Japan
Department of Integrative Physiology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan

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-dependent membrane efflux pump to exclude anticancer drugs from tumor cells. Thus, MDR1 decreases intracellular drug concentrations to confer a MDR (for reviews, see Loo & Clarke 1999 , Robert 1999 , Gottesman et al. 2002 ). The orphan nuclear receptor

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06664
Volume/Issue:
Volume 190: Issue 3
Free access
Y-H Suh
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S-Y Kim
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H-Y Lee
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B C Jang
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J H Bae
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J-N Sohn
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J-H Bae
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S-I Suh
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J-W Park
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K-U Lee
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D-K Song
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defect in at least one gene of the nuclear receptor superfamily ( Shih et al. 2001 ). Mutation in the short heterodimer partner (SHP) (NR0B2), which is an orphan nuclear receptor ( Seol et al. 1996 , Lee et al. 1998 , Nishizawa et al

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.05675
Volume/Issue:
Volume 183: Issue 1
Free access
Aline Cordeiro Biophysics Institute Carlos Chagas Filho, Federal University of Rio de Janeiro, Centro de Ciências da Saúde, Avenida Carlos Chagas Filho, 373, Bloco G, Cidade Universitária - Ilha do Fundão, Rio de Janeiro - RJ 21941-902, Brazil

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Luana Lopes Souza Biophysics Institute Carlos Chagas Filho, Federal University of Rio de Janeiro, Centro de Ciências da Saúde, Avenida Carlos Chagas Filho, 373, Bloco G, Cidade Universitária - Ilha do Fundão, Rio de Janeiro - RJ 21941-902, Brazil

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Marcelo Einicker-Lamas Biophysics Institute Carlos Chagas Filho, Federal University of Rio de Janeiro, Centro de Ciências da Saúde, Avenida Carlos Chagas Filho, 373, Bloco G, Cidade Universitária - Ilha do Fundão, Rio de Janeiro - RJ 21941-902, Brazil

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Carmen Cabanelas Pazos-Moura Biophysics Institute Carlos Chagas Filho, Federal University of Rio de Janeiro, Centro de Ciências da Saúde, Avenida Carlos Chagas Filho, 373, Bloco G, Cidade Universitária - Ilha do Fundão, Rio de Janeiro - RJ 21941-902, Brazil

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respectively. TR can form homodimers or interact with other nuclear receptors, such as retinoid X receptor (RXR), generating heterodimers ( Forman et al . 1992 , Bogazzi et al . 1994 ). Heterodimerisation leads to more efficient T 3 -dependent

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-12-0542
Volume/Issue:
Volume 216: Issue 3
Free access
Chunyan Zhao Department of Biosciences and Nutrition, Novum, Karolinska Institutet, S-141 57 Huddinge, Sweden

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Karin Dahlman-Wright Department of Biosciences and Nutrition, Novum, Karolinska Institutet, S-141 57 Huddinge, Sweden

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Liver X receptor The liver X receptors (LXRs), LXRα (NR1H3) and LXRβ (NR1H2), belong to the nuclear receptor superfamily of ligand-activated transcription factors ( Janowski et al . 1996 ). LXRα was initially isolated from a rat liver cDNA library

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0271
Volume/Issue:
Volume 204: Issue 3
Free access
Patrick Müller Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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Kenneth W Merrell Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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Justin D Crofts Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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Caroline Rönnlund Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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Chin-Yo Lin Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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Jan-Åke Gustafsson Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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Anders Ström Department of Biosciences and Nutrition, Department of Microbiology and Molecular Biology, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden

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showing the recruitment of nuclear receptor co-repressors and the corresponding decrease in histone deacetylation ( Fig. 5 ) as potentially important mechanisms requiring an intact nucleosomal structure not present in the reporter gene construct. Deletion

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-08-0094
Volume/Issue:
Volume 200: Issue 3
Free access
Hongbin Liu Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia

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Anthony E Dear Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia

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Lotte B Knudsen Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia

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Richard W Simpson Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia
Australian Centre for Blood Diseases, Eastern Clinical Research Unit, Novo Nordisk A/S, Department of Diabetes and Endocrinology, Monash University, 6th Floor Burnett Tower, 89 Commercial Road, Prahran 3181, Melbourne, Victoria, Australia

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native GLP-1 attenuates TNFα-induced PAI-1 expression in human vascular endothelial cells, an effect that may utilize the orphan nuclear receptor NUR77 ( Liu et al . 2008 ) and provide further evidence for GLP-1-mediated reduction in endothelial cell

Article Type:
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DOI:
https://doi.org/10.1677/JOE-08-0468
Volume/Issue:
Volume 201: Issue 1
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Peter J Fuller Prince Henry's Institute and the Monash University, Department of Medicine, PO Box 5152, Clayton, Victoria 3168, Australia

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Yizou Yao Prince Henry's Institute and the Monash University, Department of Medicine, PO Box 5152, Clayton, Victoria 3168, Australia

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Jun Yang Prince Henry's Institute and the Monash University, Department of Medicine, PO Box 5152, Clayton, Victoria 3168, Australia

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Morag J Young Prince Henry's Institute and the Monash University, Department of Medicine, PO Box 5152, Clayton, Victoria 3168, Australia

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Introduction The mineralocorticoid receptor (MR) is arguably unique amongst the nuclear receptors in that it has two physiological ligands, aldosterone and cortisol (corticosterone in rodents). There is increasing evidence that the consequences of

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-11-0372
Volume/Issue:
Volume 213: Issue 1
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R C M Simmen Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA

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J M P Pabona Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA

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M C Velarde Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA

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C Simmons Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA

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O Rahal Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA

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F A Simmen Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA

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; and d) post-translational modifications (e.g. phosphorylation) of nuclear receptors or their cofactors through control of expression and/or activity of specific kinases that modify these proteins. The latter possibility, while speculative, comes from

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0329
Volume/Issue:
Volume 204: Issue 3
Free access