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Vikte Lionikaite Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Karin L Gustafsson Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Anna Westerlund Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Sara H Windahl Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Antti Koskela Department of Anatomy and Cell Biology, Medical Research Center, University of Oulu, Oulu, Finland

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Juha Tuukkanen Department of Anatomy and Cell Biology, Medical Research Center, University of Oulu, Oulu, Finland

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Helena Johansson Institute for Health and Aging, Catholic University of Australia, Melbourne, Australia

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Claes Ohlsson Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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H Herschel Conaway Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA

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Petra Henning Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Ulf H Lerner Centre for Bone and Arthritis Research, Department of Internal Medicine and Clinical Nutrition, Institute for Medicine, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden

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Introduction Vitamin A is an essential nutrient consumed in the diet in the form of retinyl esters or beta carotene. Retinyl esters are transported by chylomicrons to the liver where they are converted to retinol and bound to retinol

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Gulizar Issa Ameen Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK

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Silvia Mora Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK

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). Retinol-binding protein 4 (RBP4) is both an adipokine and liver-derived protein that transports retinol (vitamin A) in the blood ( Tamori et al . 2006 ). It has been implicated in the metabolic syndrome and adipose tissue inflammation ( Kovacs et al

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Gencer Sancar German Center for Diabetes Research, Neuherberg, Germany
Department of Internal Medicine IV, Division of Diabetology, Endocrinology and Nephrology, Eberhard-Karls University of Tübingen, Tübingen, Germany
Institute for Diabetes Research and Metabolic Diseases, Helmholtz Center Munich, Eberhard-Karls University of Tübingen, Tübingen, Germany

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Andreas L Birkenfeld German Center for Diabetes Research, Neuherberg, Germany
Department of Internal Medicine IV, Division of Diabetology, Endocrinology and Nephrology, Eberhard-Karls University of Tübingen, Tübingen, Germany
Institute for Diabetes Research and Metabolic Diseases, Helmholtz Center Munich, Eberhard-Karls University of Tübingen, Tübingen, Germany

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. 2006 Retinol-binding protein 4 and insulin resistance in lean, obese, and diabetic subjects . New England Journal of Medicine 354 2552 – 2563 . ( https://doi.org/10.1056/NEJMoa054862 ) Groop LC Kankuri M Schalin-Jäntti C Ekstrand A Nikula

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S Khan Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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D E W Livingstone Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK
Centre for Discovery Brain Science, University of Edinburgh, Hugh Robson Building, Edinburgh, UK

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A Zielinska College of Medical and Dental Sciences, University of Birmingham, Birmingham, UK

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C L Doig Department of Biosciences, School of Science & Technology, Nottingham Trent University, Nottingham, UK

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D F Cobice Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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C L Esteves Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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J T Y Man Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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N Z M Homer Mass Spectrometry Core Laboratory, Edinburgh Clinical Research Facility, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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J R Seckl Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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C L MacKay SIRCAMS, School of Chemistry, University of Edinburgh, Joseph Black Building, King's Buildings, Edinburgh, UK

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S P Webster Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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G G Lavery Department of Biosciences, School of Science & Technology, Nottingham Trent University, Nottingham, UK

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K E Chapman Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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B R Walker Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK
Clinical & Translational Research Institute, Newcastle University, International Centre for Life, Central Parkway, Newcastle upon Tyne, UK

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R Andrew Centre for Cardiovascular Science, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK
Mass Spectrometry Core Laboratory, Edinburgh Clinical Research Facility, Queen’s Medical Research Institute, University of Edinburgh, Edinburgh, UK

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& Walker BR 2012 Deletion of the androgen receptor in adipose tissue in male mice elevates retinol binding protein 4 and reveals independent effects on visceral fat mass and on glucose homeostasis . Diabetes 61 1072 – 1081 . ( https://doi.org/10.2337/db

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Gisela Helfer School of Chemistry and Biosciences, University of Bradford, Bradford, UK

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Qing-Feng Wu State Key Laboratory of Molecular Development Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China

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is downstream of retinoic acid signalling. Retinol enters the tanycytes where it is synthesised to retinoic acid (RA). RA enters the nucleus and binding to its receptors RAR and RXR leads to transcription of Rarres2 , which is translated into c

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Shona Wood Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK

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Andrew Loudon Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK

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ES Ross AW Wilson D Plé H Mercer JG Ebling FJ Schuhler S Dupré SM 2006 Photoperiodic regulation of cellular retinol binding protein, CRBP1 [corrected] and nestin in tanycytes of the third ventricle ependymal layer of the Siberian

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Renata Risi Department of Experimental Medicine, Sapienza University of Rome, Sapienza University of Rome, Rome, Italy
University of Cambridge Metabolic Research Laboratories, Wellcome Trust-MRC Institute of Metabolic Science, Cambridge, UK

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Antonio Vidal-Puig University of Cambridge Metabolic Research Laboratories, Wellcome Trust-MRC Institute of Metabolic Science, Cambridge, UK
Cambridge University Nanjing Centre of Technology and Innovation, Nanjing, P. R. China
Centro de Investigacion Principe Felipe, Valencia, Spain

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Guillaume Bidault University of Cambridge Metabolic Research Laboratories, Wellcome Trust-MRC Institute of Metabolic Science, Cambridge, UK

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and a lipid core composed of TAGs, cholesterol ester and retinol ester ( Welte & Gould 2017 ) that are detected in adult islet β cells ( Vernier et al. 2012 , Trevino et al. 2015 , Dai et al. 2016 ). LD formation starts as TAG accumulation

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