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Eliana H Akamine Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences
Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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Anderson C Marçal Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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João Paulo Camporez Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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Mara S Hoshida Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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Luciana C Caperuto Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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Estela Bevilacqua Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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Carla R O Carvalho Departments of, Physiology and Biophysics, Pharmacology, Cell and Development of Biology, Department of Biological Sciences, Institute of Biomedical Sciences

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phosphatidylinositol 3-kinase (PI3K; Backer et al . 1992 , Cheatham & Kahn 1995 , Patti et al . 1995 ). AKT is a key downstream target of PI3K, activated by serine and threonine phosphorylation ( Kohn et al . 1996 , Bandyopadhyay et al . 1997 ). The PI3K/AKT

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0461
Volume/Issue:
Volume 206: Issue 1
Free access
Maria Konstandi Department of Pharmacology, University of Ioannina, School of Health Sciences, Faculty of Medicine, Ioannina, Greece
National Institutes of Health, National Cancer Institute, Laboratory of Metabolism, Bethesda, Maryland, USA

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Christina E Andriopoulou Department of Pharmacology, University of Ioannina, School of Health Sciences, Faculty of Medicine, Ioannina, Greece

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Jie Cheng National Institutes of Health, National Cancer Institute, Laboratory of Metabolism, Bethesda, Maryland, USA

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Frank J Gonzalez National Institutes of Health, National Cancer Institute, Laboratory of Metabolism, Bethesda, Maryland, USA

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.001. Western blot analysis Immunoblot analyses of CYP2D6, CYP2D22, total and phosphorylated-AKT, STAT5b and FOXO1 apoprotein was carried out using microsomes, total cellular proteins or nuclear extracts of liver samples, respectively. RIPA buffer supplemented

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-19-0561
Volume/Issue:
Volume 245: Issue 2
Restricted access
Cathy A Guo Department of Nutrition and Food Science, College of Agriculture and Life Sciences, Texas A&M University, College Station, Texas, USA

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Shaodong Guo Department of Nutrition and Food Science, College of Agriculture and Life Sciences, Texas A&M University, College Station, Texas, USA

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substrates (IRS) in genetically engineered mouse models has provided major breakthroughs in our understanding of insulin-dependent control in cardiac energy metabolism and homeostasis, particularly for the role of protein kinase Akt ( Guo 2014 ). Through

Article Type:
Review Article
DOI:
https://doi.org/10.1530/JOE-16-0679
Volume/Issue:
Volume 233: Issue 3
Free access
Markus Meier Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, D- 23538 Lübeck, Germany
Department of Internal Medicine, University Clinic Bergmannsheil, Ruhr-University Bochum, Bochum, Germany
Curschmann-Klinik, Timmendorfer Strand, Germany

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Harald H Klein Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, D- 23538 Lübeck, Germany
Department of Internal Medicine, University Clinic Bergmannsheil, Ruhr-University Bochum, Bochum, Germany
Curschmann-Klinik, Timmendorfer Strand, Germany

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Jan Kramer Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, D- 23538 Lübeck, Germany
Department of Internal Medicine, University Clinic Bergmannsheil, Ruhr-University Bochum, Bochum, Germany
Curschmann-Klinik, Timmendorfer Strand, Germany

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Maren Drenckhan Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, D- 23538 Lübeck, Germany
Department of Internal Medicine, University Clinic Bergmannsheil, Ruhr-University Bochum, Bochum, Germany
Curschmann-Klinik, Timmendorfer Strand, Germany

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Morten Schütt Department of Internal Medicine I, University of Lübeck, Ratzeburger Allee 160, D- 23538 Lübeck, Germany
Department of Internal Medicine, University Clinic Bergmannsheil, Ruhr-University Bochum, Bochum, Germany
Curschmann-Klinik, Timmendorfer Strand, Germany

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necessary for the insulin-mediated stimulation of the serine/threonine kinase Akt which is activated by phosphorylation at the Thr 308 and Ser 473 residues ( Pirola et al. 2004 ). Upon activation, Akt phosphorylates and inactivates glycogen synthase

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.07087
Volume/Issue:
Volume 193: Issue 1
Free access
Chao Li Department of Surgery, The Second Affiliated Hospital of Zhejiang University, Hanghzou, Zhejiang, China

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Bin Yang Department of Surgery, The Second Affiliated Hospital of Zhejiang University, Hanghzou, Zhejiang, China

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Zhihao Xu Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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Eric Boivin Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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Mazzen Black Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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Wenlong Huang Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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Baoyou Xu Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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Ping Wu Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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Bo Zhang Department of Surgery, The Second Affiliated Hospital of Zhejiang University, Hanghzou, Zhejiang, China

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Xian Li Department of Horticulture, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou, Zhejiang, China

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Kunsong Chen Department of Horticulture, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou, Zhejiang, China

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Yulian Wu Department of Surgery, The Second Affiliated Hospital of Zhejiang University, Hanghzou, Zhejiang, China

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Gina R Rayat Department of Surgery, Ray Rajotte Surgical-Medical Research Institute, Alberta Diabetes Institute, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada

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1% Tween-20 (Sigma-Aldrich Canada Co.) and 2% BSA, the blots were incubated overnight at 4°C with the primary antibodies. The following primary antibodies and their respective dilutions were used: p-ERK1/2 (1:2000), ERK1/2 (1:1000), p-AKT (1

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-17-0141
Volume/Issue:
Volume 235: Issue 3
Free access
Lei Zhang School of Medicine, Centre for Endocrine and Diabetes Sciences, Cardiff University, Heath Park, Cardiff CF14 4XN, UK

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Carol Paddon School of Medicine, Centre for Endocrine and Diabetes Sciences, Cardiff University, Heath Park, Cardiff CF14 4XN, UK

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Mark D Lewis School of Medicine, Centre for Endocrine and Diabetes Sciences, Cardiff University, Heath Park, Cardiff CF14 4XN, UK

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Fiona Grennan-Jones School of Medicine, Centre for Endocrine and Diabetes Sciences, Cardiff University, Heath Park, Cardiff CF14 4XN, UK

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Marian Ludgate School of Medicine, Centre for Endocrine and Diabetes Sciences, Cardiff University, Heath Park, Cardiff CF14 4XN, UK

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Signalling Technology unless otherwise stated): anti phospho-CREB (Ser 133, 1:2000 overnight; 4 °C); anti total-CREB (1:1000, room temperature, 1 h; Santa CruzBiotechnology, Santa Cruz, CA, USA); anti phospho-Akt (Thr 308, 1:1000, 4 °C, overnight); anti total-Akt

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0099
Volume/Issue:
Volume 202: Issue 2
Open access
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Elaine Cristina Lima de Souza Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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Álvaro Souto Padrón Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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William Miranda Oliveira Braga Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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Bruno Moulin de Andrade Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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Mário Vaisman Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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Luiz Eurico Nasciutti Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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Andrea Claudia Freitas Ferreira Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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Denise Pires de Carvalho Laboratório de Fisiologia Endócrina Doris Rosenthal, Serviço de Endocrinologia, Laboratório de Interações Celulares do Programa de Pesquisa em Biologia Celular e do Desenvolvimento, Instituto de Biofísica Carlos Chagas Filho

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). Concerning the differentiation of thyroid cells, the activation of PI3K by IGF1 inhibits the expression of NIS that is stimulated by TSH and cAMP ( Garcia & Santisteban 2002 ). Moreover, TSH stimulates AKT phosphorylation in a PI3K-dependent and cAMP

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0436
Volume/Issue:
Volume 206: Issue 1
Free access
Donato A Rivas
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Ben B Yaspelkis III Exercise Metabolism Group, Exercise Biochemistry Lab, School of Medical Sciences, RMIT University, Bundoora, Victoria 3083, Australia

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John A Hawley
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Sarah J Lessard
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; Tremblay & Marette 2001 ). In contrast, mTORC2 is a positive regulator of insulin signal transduction through its phosphorylation of protein kinase B/Akt on its serine 473 activation site ( Hresko & Mueckler 2005 , Sarbassov et al . 2005 ). Its ability to

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0202
Volume/Issue:
Volume 202: Issue 3
Free access
Lin Xia
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Zhongqiu Wang Center for Molecular Metabolism, Department of Radiology, Department of Biochemistry and Molecular Biology, Nanjing University of Science and Technology, B508, #364, 200 Xiaolingwei Street, Nanjing 210094, China

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Ying Zhang Center for Molecular Metabolism, Department of Radiology, Department of Biochemistry and Molecular Biology, Nanjing University of Science and Technology, B508, #364, 200 Xiaolingwei Street, Nanjing 210094, China

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Xiao Yang
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Yibei Zhan
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Rui Cheng
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Shiming Wang
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Jianfa Zhang
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PI3K/AKT pathway is a key regulator of insulin signaling ( Whiteman et al . 2002 ). In adipose and muscle cells, AKT (AKT1) overexpression results in an increased insulin-sensitive glucose transporter GLUT4 translocation and glucose uptake ( Kohn et

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-14-0501
Volume/Issue:
Volume 224: Issue 3
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Liza Margareth Medeiros de Carvalho Sousa Department of Surgery, School of Veterinary Medicine and Animal Science, University of São Paulo, São Paulo, Brazil

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Renata dos Santos Silva Department of Surgery, School of Veterinary Medicine and Animal Science, University of São Paulo, São Paulo, Brazil

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Vanessa Uemura da Fonseca Department of Surgery, School of Veterinary Medicine and Animal Science, University of São Paulo, São Paulo, Brazil

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Rafael Magdanelo Leandro Department of Surgery, School of Veterinary Medicine and Animal Science, University of São Paulo, São Paulo, Brazil

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Thiago Senna Di Vincenzo Department of Surgery, School of Veterinary Medicine and Animal Science, University of São Paulo, São Paulo, Brazil

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Ana Bárbara Alves-Wagner Department of Physiology and Biophysics, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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Ubiratan Fabres Machado Department of Physiology and Biophysics, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil

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Paula de Carvalho Papa Department of Surgery, School of Veterinary Medicine and Animal Science, University of São Paulo, São Paulo, Brazil

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.05). Additionally, we verified that despite unchanged total AKT content, insulin increased ( P  < 0.001) the AKT phosphorylation ( Fig. 1A and B ). GLUT4 and GLUT1 staining revealed that both were present in luteal cells; however, only GLUT4 showed a qualitative

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-16-0173
Volume/Issue:
Volume 231: Issue 3
Free access