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Magnus F G Grøndahl Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark

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Jonatan I Bagger Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark
Clinical Research, Steno Diabetes Center Copenhagen, Herlev, Denmark

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Malte P Suppli Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark

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Gerrit Van Hall Department of Clinical Biochemistry, Clinical Metabolomics Core Facility, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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Nicolai J W Albrechtsen Department of Clinical Biochemistry, University Hospital Copenhagen, Bispebjerg, Copenhagen, Denmark

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Jens J Holst Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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Tina Vilsbøll Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark
Clinical Research, Steno Diabetes Center Copenhagen, Herlev, Denmark

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Mikkel B Christensen Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark
Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Department of Clinical Pharmacology, Copenhagen University Hospital – Bispebjerg and Frederiksberg, Copenhagen, Denmark
Copenhagen Center for Translational Research, Copenhagen University Hospital – Bispebjerg and Frederiksberg, University of Copenhagen, Copenhagen, Denmark

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Asger B Lund Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark

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Filip K Knop Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark
Clinical Research, Steno Diabetes Center Copenhagen, Herlev, Denmark
Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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glucagon’s well-known effects on glucose metabolism, the hormone is also involved in amino acid metabolism. Glucagon secretion is stimulated by glucagonotropic amino acids and glucagon in turn stimulates hepatic amino acid breakdown ( 2 ). Elevated levels

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Iben Rix Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark
Zealand Pharma A/S, Søborg, Denmark

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Marie L Johansen Department of Medicine, Herlev Hospital, University of Copenhagen, Herlev, Denmark

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Asger Lund Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark

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Malte P Suppli Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark

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Elizaveta Chabanova Department of Radiology, Herlev Hospital, University of Copenhagen, Herlev, Denmark

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Gerrit van Hall Clinical Metabolomics Core Facility, Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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Jens J Holst Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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Nicolai J Wewer Albrechtsen Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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Caroline Kistorp Department of Endocrinology, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark
Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

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Filip K Knop Center for Clinical Metabolic Research, Gentofte Hospital, University of Copenhagen, Hellerup, Denmark
Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Steno Diabetes Center Copenhagen, Herlev, Denmark

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, substrate availability, and the autonomic nervous system. Potent regulators of glucagon secretion include hypoglycaemia, insulin, and certain amino acids ( 4 , 5 ). A feedback loop between the liver and the pancreas, the liver–α-cell axis, controls amino

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Julia Otten Department of Public Health and Clinical Medicine, Umeå University, Umeå, Sweden

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Andreas Stomby Department of Public Health and Clinical Medicine, Umeå University, Umeå, Sweden
Region Jönköping County, Jönköping, Sweden

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Maria Waling Department of Food, Nutrition and Culinary Science, Umeå University, Umeå, Sweden

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Elin Chorell Department of Public Health and Clinical Medicine, Umeå University, Umeå, Sweden

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Mats Ryberg Department of Public Health and Clinical Medicine, Umeå University, Umeå, Sweden

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Michael Svensson Department of Community Medicine and Rehabilitation, Section for Sports Medicine, Umeå University, Umeå Sweden

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Jens Juul Holst NNF Center for Basic Metabolic Research and Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark

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Tommy Olsson Department of Public Health and Clinical Medicine, Umeå University, Umeå, Sweden

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endogenous glucose production even further ( 1 , 2 ). Glucagon action is critical for correcting hypoglycemia but other potent stimulators of glucagon secretion are high amino acid levels, which may be an even more effective stimulus than low blood glucose

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Yang Yu Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Hairong Hao Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Linghui Kong Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Jie Zhang Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Feng Bai Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Fei Guo Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Pan Wei Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Rui Chen Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Wen Hu Department of Endocrinology and Metabolism, Huai’an Hospital Affiliated to Xuzhou Medical University and Huai’an Second People’s Hospital, Huai’an, Jiangsu, China

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Introduction Branched-chain amino acids (BCAAs) are neutral amino acids containing branched aliphatic hydrocarbon chains on the α-carbon, including l -leucine, l -isoleucine and l -valine, which are essential amino acids that cannot be

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Xu-Ting Song Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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Jia-Nan Zhang Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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Duo-Wei Zhao Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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Yu-Fei Zhai Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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Qi Lu Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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Mei-Yu Qi Institute of Animal Husbandry, Heilongjiang Academy of Agricultural Sciences, Harbin, China

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Ming-Hai Lu Department of Animal Science, Heilongjiang State Farms Science Technology Vocational College, Harbin, China

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Shou-Long Deng CAS Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China

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Hong-Bing Han Beijing Key Laboratory of Animal Genetic Improvement, China Agricultural University, Beijing, China

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Xiu-Qin Yang Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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Yu-Chang Yao Key Laboratory of Animal Genetics, Breeding and Reproduction, Education Department of Heilongjiang Province, College of Animal Science and Technology

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, Beijing, China). The products were cloned by pMD18-T vector (Takara) and sequenced (GENEWIZ, Nanjing, China). The open reading frames (ORFs) of IGF1 splice variants of sheep were analyzed and translated into amino acid sequences. The potential signal

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Elena Pardi Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Stefano Mariotti Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Natalia S Pellegata Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Katiuscia Benfini Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Simona Borsari Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Federica Saponaro Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Liborio Torregrossa Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Antonello Cappai Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Chiara Satta Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Marco Mastinu Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Claudio Marcocci Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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Filomena Cetani Endocrine Unit 2, Endocrinology Unit, Institute of Pathology, Department of Surgical, Department of Clinical and Experimental Medicine, University Hospital of Pisa, University of Pisa, Via Paradisa 2, Pisa, Italy

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,6 (15, 16) . P27 harbors a CDK-binding domain in the N-terminal half of the protein, which is necessary for the mediation of the CDK-inhibitory functions. Moreover, P27 contains a bipartite nuclear localization signal (NLS) at amino acids 152/153 and 166

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Teresa Lam School of Medicine, Western Sydney University, Penrith, New South Wales, Australia
Department of Diabetes and Endocrinology, Blacktown Hospital, Blacktown, New South Wales, Australia
Department of Diabetes and Endocrinology, Westmead Hospital, Westmead, New South Wales, Australia

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Mark McLean School of Medicine, Western Sydney University, Penrith, New South Wales, Australia
Department of Diabetes and Endocrinology, Blacktown Hospital, Blacktown, New South Wales, Australia

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Amy Hayden Department of Radiation Oncology, Blacktown Hospital, Blacktown, New South Wales, Australia
Crown Princess Mary Cancer Centre, Westmead Hospital, Westmead, New South Wales, Australia

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Anne Poljak Bioanalytical Mass Spectrometry Facility and School of Medical Sciences, UNSW Sydney, Sydney, New South Wales, Australia

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Birinder Cheema School of Science and Health, Western Sydney University, Penrith, New South Wales, Australia

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Howard Gurney Crown Princess Mary Cancer Centre, Westmead Hospital, Westmead, New South Wales, Australia

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Glenn Stone School of Computing, Engineering and Mathematics, Western Sydney University, Penrith, New South Wales, Australia

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Neha Bahl School of Medicine, Western Sydney University, Penrith, New South Wales, Australia

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Navneeta Reddy Department of Diabetes and Endocrinology, Blacktown Hospital, Blacktown, New South Wales, Australia
Garvan Institute of Medical Research, Darlinghurst, New South Wales, Australia

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Haleh Shahidipour School of Medicine, Western Sydney University, Penrith, New South Wales, Australia
Department of Diabetes and Endocrinology, Blacktown Hospital, Blacktown, New South Wales, Australia
School of Medicine, UNSW Sydney, Sydney, New South Wales, Australia
Translational Health Research Institute, Penrith, New South Wales, Australia

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Vita Birzniece School of Medicine, Western Sydney University, Penrith, New South Wales, Australia
Department of Diabetes and Endocrinology, Blacktown Hospital, Blacktown, New South Wales, Australia
Garvan Institute of Medical Research, Darlinghurst, New South Wales, Australia
School of Medicine, UNSW Sydney, Sydney, New South Wales, Australia
Translational Health Research Institute, Penrith, New South Wales, Australia

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.9% ( P  < 0.05) ( Fig. 1 ) increase in leucine oxidized as a proportion of LRa (percent Lox/LRa), which represents the proportion of amino acids irreversibly lost when adjusted for changes in protein turnover. Conversely, the rate of leucine incorporation

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Charlotte Höybye Department of Endocrinology, Department of Molecular Medicine and Surgery, Metabolism and Diabetology, Karolinska University Hospital, 171 76 Stockholm, Sweden
Department of Endocrinology, Department of Molecular Medicine and Surgery, Metabolism and Diabetology, Karolinska University Hospital, 171 76 Stockholm, Sweden

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Erik Wahlström Department of Endocrinology, Department of Molecular Medicine and Surgery, Metabolism and Diabetology, Karolinska University Hospital, 171 76 Stockholm, Sweden

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Petra Tollet-Egnell Department of Endocrinology, Department of Molecular Medicine and Surgery, Metabolism and Diabetology, Karolinska University Hospital, 171 76 Stockholm, Sweden

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Gunnar Norstedt Department of Endocrinology, Department of Molecular Medicine and Surgery, Metabolism and Diabetology, Karolinska University Hospital, 171 76 Stockholm, Sweden

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metabolites in the serum of ten patients with growth hormone deficiency (GHD) ( n =10) and ten age and gender matched-controls ( n =10) showing well-known effects of GH on amino acids and fatty acids. GHD-0, baseline; GHD-1, after 1 month of GH replacement

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Luis Eduardo Barbalho de Mello Genetic Bases of Thyroid Tumors Laboratory, Division of Genetics, Department of Morphology and Genetics, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil
Postgraduate Program in Health Sciences, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil

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Thaise Nayane Ribeiro Carneiro Genetic Bases of Thyroid Tumors Laboratory, Division of Genetics, Department of Morphology and Genetics, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil

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Aline Neves Araujo Genetic Bases of Thyroid Tumors Laboratory, Division of Genetics, Department of Morphology and Genetics, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil

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Camila Xavier Alves Postgraduate Program in Health Sciences, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil

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Pedro Alexandre Favoretto Galante Centro de Oncologia Molecular, Hospital Sírio-libanês, São Paulo, São Paulo, Brazil

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Vanessa Candiotti Buzatto Centro de Oncologia Molecular, Hospital Sírio-libanês, São Paulo, São Paulo, Brazil

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Maria das Graças de Almeida Postgraduate Program in Health Sciences, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil
Department of Clinical and Toxicological Analyses, Natal, Rio Grande do Norte, Brazil

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Karina Marques Vermeulen-Serpa Postgraduate Program in Health Sciences, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil

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Sancha Helena de Lima Vale Department of Clinical and Toxicological Analyses, Natal, Rio Grande do Norte, Brazil
Department of Nutrition, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil

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Fernando José de Pinto Paiva Postgraduate Program in Health Sciences, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil

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José Brandão-Neto Postgraduate Program in Health Sciences, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte, Brazil

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Janete Maria Cerutti Genetic Bases of Thyroid Tumors Laboratory, Division of Genetics, Department of Morphology and Genetics, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil

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and sequenced using the BigDye Terminator (Life Technologies) in the ABI 3100 Genetic Analyzer (Applied Biosystems). In silico analysis The effect of the amino acid substitution on NID1 protein structure and function was performed using various

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Beril Erdem Department of Biology, Faculty of Science, Hacettepe University, Ankara, Turkey

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Angela Schulz Rudolf Schönheimer Institute of Biochemistry, Faculty of Medicine, Leipzig University, Leipzig, Germany

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Emel Saglar Department of Biology, Faculty of Science, Hacettepe University, Ankara, Turkey

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Ferhat Deniz Department of Endocrinology, SBÜ Sultan Abdülhamid Han Teaching Hospital, Istanbul, Turkey

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Torsten Schöneberg Rudolf Schönheimer Institute of Biochemistry, Faculty of Medicine, Leipzig University, Leipzig, Germany

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Hatice Mergen Department of Biology, Faculty of Science, Hacettepe University, Ankara, Turkey

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is based on mutations in the AVPR2 , which is located on Xq28 ( 3 ). The coding sequence of AVPR2 is distributed on three exons encoding a protein of 371 amino acids. As a member of the superfamily of G protein-coupled receptors, the protein has

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