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Alexander Hennebry AgResearch Ltd, Hamilton, New Zealand

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Jenny Oldham AgResearch Ltd, Hamilton, New Zealand

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Tea Shavlakadze School of Anatomy, Physiology & Human Biology, The University of Western Australia, Crawley, Western Australia, Australia

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Miranda D Grounds School of Anatomy, Physiology & Human Biology, The University of Western Australia, Crawley, Western Australia, Australia

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Philip Sheard Department of Physiology, University of Otago, Dunedin, New Zealand

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Marta L Fiorotto USDA/ARS Children’s Nutrition Research Center, Baylor College of Medicine, Houston, Texas, USA

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Shelley Falconer AgResearch Ltd, Hamilton, New Zealand

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Heather K Smith Department of Exercise Sciences, University of Auckland, Auckland, New Zealand

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Carole Berry AgResearch Ltd, Hamilton, New Zealand

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Ferenc Jeanplong AgResearch Ltd, Hamilton, New Zealand

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Jeremy Bracegirdle AgResearch Ltd, Hamilton, New Zealand

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Kenneth Matthews AgResearch Ltd, Hamilton, New Zealand

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Gina Nicholas AgResearch Ltd, Hamilton, New Zealand

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Mônica Senna-Salerno AgResearch Ltd, Hamilton, New Zealand

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Trevor Watson AgResearch Ltd, Hamilton, New Zealand

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Christopher D McMahon AgResearch Ltd, Hamilton, New Zealand

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binds and activates activin type 2B receptors to promote phosphorylation of Smad2/3 ( Rebbapragada et al. 2003 ), while IGF1 activates the IGF1 receptor and phosphorylates PI3 kinase (PI3K) and AKT ( Rommel et al. 2001 ). The PI3K/AKT pathway is

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-17-0032
Volume/Issue:
Volume 234: Issue 2
Free access
Toya M Albury-Warren Burnett School of Biomedical Sciences, Department of Head and Neck Surgery, College of Medicine, University of Central Florida, 6900 Lake Nona Boulevard, Orlando, Florida 32827, USA

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Veethika Pandey Burnett School of Biomedical Sciences, Department of Head and Neck Surgery, College of Medicine, University of Central Florida, 6900 Lake Nona Boulevard, Orlando, Florida 32827, USA

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Lina P Spinel Burnett School of Biomedical Sciences, Department of Head and Neck Surgery, College of Medicine, University of Central Florida, 6900 Lake Nona Boulevard, Orlando, Florida 32827, USA

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Michal M Masternak Burnett School of Biomedical Sciences, Department of Head and Neck Surgery, College of Medicine, University of Central Florida, 6900 Lake Nona Boulevard, Orlando, Florida 32827, USA
Burnett School of Biomedical Sciences, Department of Head and Neck Surgery, College of Medicine, University of Central Florida, 6900 Lake Nona Boulevard, Orlando, Florida 32827, USA

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Deborah A Altomare Burnett School of Biomedical Sciences, Department of Head and Neck Surgery, College of Medicine, University of Central Florida, 6900 Lake Nona Boulevard, Orlando, Florida 32827, USA

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Introduction AKT, a serine/threonine kinase, is downstream of phosphatidylinositol-3-kinase (PI3K) and growth factor receptors (e.g. epidermal growth factor receptor), and is a hallmark signaling protein predominantly recognized for regulation of

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-15-0288
Volume/Issue:
Volume 228: Issue 1
Free access
A Tsuchiya Division of Bioinformation, Department of Physiology, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya 663-8501, Japan

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T Kanno Division of Bioinformation, Department of Physiology, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya 663-8501, Japan

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T Nishizaki Division of Bioinformation, Department of Physiology, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya 663-8501, Japan

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Introduction Akt is a serine/threonine protein kinase bearing multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration. Akt includes three closely related isoforms Akt1, Akt2, and Akt3

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-13-0172
Volume/Issue:
Volume 220: Issue 1
Open access
Olivier Le Bacquer UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France

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Gurvan Queniat UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France

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Valery Gmyr UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France

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Julie Kerr-Conte UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France

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Bruno Lefebvre UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France

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François Pattou UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France
UMR859, INSERM UMR859, INSERM UMR837, CHU Lille, Faculty of Medicine, Université Lille Nord de France, 1 Place de Verdun, F-59000 Lille, France

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& Sonenberg 2004 , Wullschleger et al . 2006 ). mTORC1 and mTORC2 are two distinct complexes sharing mTOR as a catalytic subunit. mTORC1 is composed of mTOR, regulated associated protein of mTOR (raptor), proline-rich Akt substrate of 40 kDa (PRAS40), and G

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-12-0351
Volume/Issue:
Volume 216: Issue 1
Free access
Kimberley C W Wang Early Origins of Adult Health Research Group, School of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, Adelaide, South Australia, Australia

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Kimberley J Botting Early Origins of Adult Health Research Group, School of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, Adelaide, South Australia, Australia

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Song Zhang Early Origins of Adult Health Research Group, School of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, Adelaide, South Australia, Australia

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I Caroline McMillen Early Origins of Adult Health Research Group, School of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, Adelaide, South Australia, Australia

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Doug A Brooks Mechanisms in Cell Biology and Disease Research Group, School of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, Adelaide, South Australia, Australia

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Janna L Morrison Early Origins of Adult Health Research Group, School of Pharmacy and Medical Sciences, Sansom Institute for Health Research, University of South Australia, Adelaide, South Australia, Australia

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factor 2 receptor (IGF-2R) and angiotensin II type 1 receptor (AT 1 R)-mediated Akt signaling as molecular foundations for the association between low birth weight and cardiovascular disease in adulthood. Cardiomyocyte development during fetal life

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-17-0039
Volume/Issue:
Volume 233: Issue 2
Free access
Rupasri Ain Institute of Maternal-Fetal Biology and Division of Cancer and Developmental Biology, Departments of Pathology and Laboratory of Medicine, Molecular and Integrative Physiology, and Obstetrics and Gynecology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA

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Lindsey N Canham Institute of Maternal-Fetal Biology and Division of Cancer and Developmental Biology, Departments of Pathology and Laboratory of Medicine, Molecular and Integrative Physiology, and Obstetrics and Gynecology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA

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Michael J Soares Institute of Maternal-Fetal Biology and Division of Cancer and Developmental Biology, Departments of Pathology and Laboratory of Medicine, Molecular and Integrative Physiology, and Obstetrics and Gynecology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA

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the Ser/Thr protein kinase, Akt (also called protein kinase B) ( Chan et al. 1999 , Datta et al. 1999 ). Akt activation can stimulate changes in gene transcription, cell survival, cell division, and cell differentiation. In the present

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06039
Volume/Issue:
Volume 185: Issue 2
Free access
Shi-Yan Li Division of Pharmaceutical Sciences and Center for Cardiovascular Research and Alternative Medicine, University of Wyoming, Laramie, Wyoming 82071, USA

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Cindy X Fang Division of Pharmaceutical Sciences and Center for Cardiovascular Research and Alternative Medicine, University of Wyoming, Laramie, Wyoming 82071, USA

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Nicholas S Aberle II Division of Pharmaceutical Sciences and Center for Cardiovascular Research and Alternative Medicine, University of Wyoming, Laramie, Wyoming 82071, USA

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Bonnie H Ren Division of Pharmaceutical Sciences and Center for Cardiovascular Research and Alternative Medicine, University of Wyoming, Laramie, Wyoming 82071, USA

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Asli F Ceylan-Isik Division of Pharmaceutical Sciences and Center for Cardiovascular Research and Alternative Medicine, University of Wyoming, Laramie, Wyoming 82071, USA

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Jun Ren Division of Pharmaceutical Sciences and Center for Cardiovascular Research and Alternative Medicine, University of Wyoming, Laramie, Wyoming 82071, USA

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be triggered by activation of its upstream molecules phosphatidylinositol 3 (PI-3) kinase and the serine/threonine kinase PKB/Akt ( Hornberger et al. 2004 , Oudit et al. 2004 ). Meanwhile, increased levels of nutrients, growth factors such as

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06168
Volume/Issue:
Volume 186: Issue 3
Free access
Manon M Roustit
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Joan M Vaughan Department of Comparative Biomedical Sciences, Laboratory of Neuronal Structure and Function, Queen's Medical Research Institute, Royal Veterinary College, University of London, Royal College Street, London NW1 0TU, UK

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Pauline M Jamieson Department of Comparative Biomedical Sciences, Laboratory of Neuronal Structure and Function, Queen's Medical Research Institute, Royal Veterinary College, University of London, Royal College Street, London NW1 0TU, UK

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Mark E Cleasby
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/2, AKT and PKCε activation ( Brar et al . 2002 , 2004 , Lawrence et al . 2005 ). UCN2 and CRFR2 are both expressed in mouse skeletal muscle ( Chen et al . 2004 , Keipert et al . 2013 ), where they inhibit atrophy and promote hypertrophy ( Hinkle

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-14-0181
Volume/Issue:
Volume 223: Issue 2
Open access
Hong-Zhi Sun
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Tong-Wei Yang Key Laboratory of Environment and Genes Related to Diseases, First Affiliated Hospital of Jilin University, Ministry of Education, School of Medicine, Xi'an Jiaotong University, Xi'an 710061, People's Republic of China

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Wei-Jin Zang
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Shu-Fang Wu
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), suggesting that NFKB may regulate the expression of AR. The activation of AKT and NFKB has been involved in the progression of PCa from androgen dependence to independence ( Murillo et al . 2001 , Kikuchi et al . 2003 ). The phosphatidylinositol 3-kinase

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0270
Volume/Issue:
Volume 204: Issue 3
Free access
Hong Xu Department of Gastroenterology and Hepatology, Hangzhou Red Cross Hospital, Hangzhou, China

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Yang Zhou Liver Cirrhosis Section, Department of Hepatology, Shuguang Hospital Affiliated to Shanghai University of Traditional Chinese Medicine, Shanghai, China
Institute of Liver Diseases, Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Yongxia Liu Department of Clinical Laboratory, Hangzhou Red Cross Hospital, Hangzhou, China

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Jian Ping Liver Cirrhosis Section, Department of Hepatology, Shuguang Hospital Affiliated to Shanghai University of Traditional Chinese Medicine, Shanghai, China
Institute of Liver Diseases, Shanghai University of Traditional Chinese Medicine, Shanghai, China

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Qiyang Shou Experimental Animal Research Center, Zhejiang Chinese Medical University, Hangzhou, China

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Fangming Chen Experimental Animal Research Center, Zhejiang Chinese Medical University, Hangzhou, China

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Ru Ruo Department of Pathology, Hangzhou Red Cross Hospital, Hangzhou, China

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( Ahmadieh & Azar 2014 ). In the liver, the insulin receptor substrate 2 (IRS2)/phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt) signaling transduction pathway plays a pivotal role in modulating the glucose metabolic actions of insulin ( Pessin

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-15-0409
Volume/Issue:
Volume 229: Issue 2
Free access