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Nicolai Preisler Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Pascal Laforêt Centre de Référence de Pathologie Neuromusculaire Paris-Est, Institut de Myologie, GH Pitié-Salpêtrière, Assistance Publique-Hôpitaux de Paris, Paris, France

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Karen Lindhardt Madsen Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Edith Husu Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Christoffer Rasmus Vissing Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Gitte Hedermann Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Henrik Galbo Department of Inflammation Research, Rigshospitalet, Copenhagen, Denmark

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Christopher Lindberg Department of Neurology, Sahlgrenska University Hospital, Gothenburg, Sweden

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John Vissing Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark

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Introduction Pompe disease (Glycogenosis type II; OMIM #232300) is caused by lysosomal acid alpha-glucosidase deficiency (EC# 3.2.1.20), which leads to a metabolic block in intra-lysosomal glycogen breakdown ( 1 ). In the late-onset forms of

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-17-0042
Volume/Issue:
Volume 6: Issue 6
Open access
Selina Mäkinen Minerva Foundation Institute for Medical Research, Helsinki, Finland
Department of Medicine, University of Helsinki, Helsinki University Central Hospital, Helsinki, Finland

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Neeta Datta Minerva Foundation Institute for Medical Research, Helsinki, Finland
Department of Medicine, University of Helsinki, Helsinki University Central Hospital, Helsinki, Finland

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Yen H Nguyen Minerva Foundation Institute for Medical Research, Helsinki, Finland
Department of Medicine, University of Helsinki, Helsinki University Central Hospital, Helsinki, Finland

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Petro Kyrylenko Minerva Foundation Institute for Medical Research, Helsinki, Finland
Department of Medicine, University of Helsinki, Helsinki University Central Hospital, Helsinki, Finland

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Markku Laakso Institute of Clinical Medicine, Internal Medicine, University of Eastern Finland, Kuopio, Finland

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Heikki A Koistinen Minerva Foundation Institute for Medical Research, Helsinki, Finland
Department of Medicine, University of Helsinki, Helsinki University Central Hospital, Helsinki, Finland

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-free DMEM (Gibco cat. 11966). Antibiotics used in proliferation and differentiation medias were Amphotericin B from Gibco and penicillin–streptomycin solution from Sigma. FBS and l -glutamine, glycogen carrier from rat liver and cytochalasin B were from

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-20-0444
Volume/Issue:
Volume 9: Issue 11
Open access
Zhiwei Zhang Department of Obstetrics and Gynecology, Liaocheng People’s Hospital, Liaocheng, Shandong, China

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Hui Zhao Department of Obstetrics and Gynecology, Liaocheng People’s Hospital, Liaocheng, Shandong, China

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Aixia Wang Department of Obstetrics and Gynecology, Liaocheng People’s Hospital, Liaocheng, Shandong, China

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weight, plasma insulin levels and hepatic glycogen contents, were compared in GDM mice with or without oleuropein treatment. Oxidative stress was examined by measuring liver oxidative stress markers. Inflammatory levels were evaluated by assessing

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-20-0466
Volume/Issue:
Volume 10: Issue 1
Open access
Chao Xu Key Laboratory of Aquatic Nutrition and Feed Science of Jiangsu Province, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China

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Xiang-Fei Li Key Laboratory of Aquatic Nutrition and Feed Science of Jiangsu Province, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China

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Hong-Yan Tian Department of Ocean Technology, College of Marine and Biology Engineering, Yancheng Institute of Technology, Yancheng, Province Jiangsu, China

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Hua-Juan Shi Key Laboratory of Aquatic Nutrition and Feed Science of Jiangsu Province, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China

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Ding-Dong Zhang Key Laboratory of Aquatic Nutrition and Feed Science of Jiangsu Province, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China

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Kenneth Prudence Abasubong Key Laboratory of Aquatic Nutrition and Feed Science of Jiangsu Province, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China

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Wen-Bin Liu Key Laboratory of Aquatic Nutrition and Feed Science of Jiangsu Province, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China

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pathways, such as the enhancement of glycogenesis by increasing the phosphorylation of glycogen synthase kinase-3β (Gsk3β) ( 15 ), the inhibition of fatty acid synthesis by reducing the activity of acetyl-CoA carboxylase and the depression of the

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-18-0517
Volume/Issue:
Volume 8: Issue 3
Open access
Helle Keinicke Insulin and Device Trial Operations, Novo Nordisk A/S, Søborg, Denmark

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Gao Sun Pharmacology and Histopathology, Novo Nordisk A/S, China

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Caroline M Junker Mentzel Department of Experimental Animal Models, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg C, Denmark

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Merete Fredholm Department of Veterinary Clinical and Animal Science, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg C, Denmark

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Linu Mary John Global Obesity and Liver Disease Research, Novo Nordisk A/S, Måløv, Denmark

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Birgitte Andersen Global Obesity and Liver Disease Research, Novo Nordisk A/S, Måløv, Denmark

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Kirsten Raun Global Obesity and Liver Disease Research, Novo Nordisk A/S, Måløv, Denmark

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Marina Kjaergaard Global Obesity and Liver Disease Research, Novo Nordisk A/S, Måløv, Denmark

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measured by luminescent oxygen channeling (LOCI) assays (Perkin Elmer alphaLISA, kit AL521F). Frozen liver samples of 20–42 mg were used for the determination of lipid and glycogen as previously described ( 26 ). Note that, in this study, samples were

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-20-0152
Volume/Issue:
Volume 9: Issue 8
Open access
Estíbaliz Castillero
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Ana Isabel Martín
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Maria Paz Nieto-Bona Department of Physiology, Department of Histology, Faculty of Medicine, Complutense University of Madrid, 28040 Madrid, Spain

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Carmen Fernández-Galaz
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María López-Menduiña
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María Ángeles Villanúa
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Asunción López-Calderón
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adiponectin, leptin, resistin, insulin, and glucose assays were performed. Liver was removed, dissected, frozen, and stored at −80 °C until glycogen analysis. Left gastrocnemius and periepididymal WATs were dissected and weighed. Left soleus from nine rats of

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-12-0003
Volume/Issue:
Volume 1: Issue 1
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Svjatoslavs Kistkins Pauls Stradiņš Clinical University Hospital, Riga, Latvia

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Othmar Moser Division of Exercise Physiology and Metabolism, Institute of Sport Science, University of Bayreuth, Bayreuth, Germany

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Vitālijs Ankudovičs Pauls Stradiņš Clinical University Hospital, Riga, Latvia

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Dmitrijs Blizņuks Institute of Smart Computing Technologies, Riga Technical University, Riga, Latvia

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Timurs Mihailovs Institute of Smart Computing Technologies, Riga Technical University, Riga, Latvia

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Sergejs Lobanovs Pauls Stradiņš Clinical University Hospital, Riga, Latvia

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Harald Sourij Trials Unit for Interdisciplinary Metabolic Medicine, Division of Endocrinology and Diabetolgoy, Medical University of Graz, Graz, Austria

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Andreas F H Pfeiffer Department of Endocrinology and Metabolic Medicine, Campus Benjamin Franklin, Charité University Medicine, Hindenburgdamm, Berlin, Germany

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Valdis Pīrāgs Pauls Stradiņš Clinical University Hospital, Riga, Latvia
Faculty of Medicine, University of Latvia, Riga, Latvia

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utilization of glycogen and lipids, resulting in glucose and fatty acids production. Glucagon in the absence of GLP-1 increases appetite. Conversely, both glucagon and glucose stimulate insulin secretion, facilitating glucose uptake and storage in organs. This

Article Type:
Review Article
Collections:
Metabolic Syndrome and Diabetes
DOI:
https://doi.org/10.1530/EC-23-0529
Volume/Issue:
Volume 13: Issue 5
Open access
Wouter W de Herder Section of Endocrinology, Department of Internal Medicine, Erasmus MC, 's Gravendijkwal 230, 3015 CE Rotterdam, The Netherlands

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and Gerty T Cori Radnitz Catalytic conversion of glycogen 1947 (PM) Bernardo A Houssay Anterior pituitary and carbohydrate metabolism 1939 (Ch) Adolf F J Butenandt Sex hormones 1923 (PM) Frederick G Banting, John J R Macleod Discovery of insulin 1909

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-14-0070
Volume/Issue:
Volume 3: Issue 3
Open access
Peter Wolf Division of Endocrinology and Metabolism, Department of Internal Medicine III, Medical University of Vienna, Vienna, Austria

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Yvonne Winhofer Division of Endocrinology and Metabolism, Department of Internal Medicine III, Medical University of Vienna, Vienna, Austria

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Martin Krššák Division of Endocrinology and Metabolism, Department of Internal Medicine III, Medical University of Vienna, Vienna, Austria
High Field MR Centre, Department of Biomedical Imaging and Image-guided Therapy, Medical University of Vienna, Vienna, Austria

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Michael Krebs Division of Endocrinology and Metabolism, Department of Internal Medicine III, Medical University of Vienna, Vienna, Austria

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. Expression of GLUT-4 is stimulated by insulin and activation of AMP-activated protein kinase (AMPK) due to cardiac stress ( 9 ). Similar to free FA, an overload of carbohydrates can be stored as glycogen in the myocardium, but glycogen stores in the heart are

Article Type:
Review Article
DOI:
https://doi.org/10.1530/EC-17-0031
Volume/Issue:
Volume 6: Issue 4
Open access
Flavia Letícia Martins Peçanha Instituto de Bioquímica Médica Leopoldo de Meis, Laboratório de Adaptações Metabólicas, Programa de Bioquímica e Biofísica Celular, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, Rio de Janeiro, Brazil

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Reinaldo Sousa dos Santos Instituto de Bioquímica Médica Leopoldo de Meis, Laboratório de Adaptações Metabólicas, Programa de Bioquímica e Biofísica Celular, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, Rio de Janeiro, Brazil

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Wagner Seixas da-Silva Instituto de Bioquímica Médica Leopoldo de Meis, Laboratório de Adaptações Metabólicas, Programa de Bioquímica e Biofísica Celular, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, Rio de Janeiro, Brazil

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by AKT ( 30 ). However, glycogen synthase kinase 3β (GSK3B), a downstream target of AKT, can negatively affect the mitochondria-HK interaction by phosphorylating VDAC. Thus, although part of the same pathway, AKT and GSK3B have opposing effects on the

Article Type:
Research Article
DOI:
https://doi.org/10.1530/EC-17-0059
Volume/Issue:
Volume 6: Issue 5
Open access