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Jie Miao UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France
Department of Molecules and Circuits, CNRS UMR 9197, Molecular Neuroendocrinology of Food Intake, Paris-Saclay Institute of Neuroscience, Orsay, France
Department of Geriatrics, Ruijin Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai, China

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Yacir Benomar UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France
Department of Molecules and Circuits, CNRS UMR 9197, Molecular Neuroendocrinology of Food Intake, Paris-Saclay Institute of Neuroscience, Orsay, France

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Sarah Al Rifai UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France

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Ghislaine Poizat UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France
Department of Molecules and Circuits, CNRS UMR 9197, Molecular Neuroendocrinology of Food Intake, Paris-Saclay Institute of Neuroscience, Orsay, France

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Laure Riffault UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France
Department of Molecules and Circuits, CNRS UMR 9197, Molecular Neuroendocrinology of Food Intake, Paris-Saclay Institute of Neuroscience, Orsay, France

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Delphine Crépin UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France
Department of Molecules and Circuits, CNRS UMR 9197, Molecular Neuroendocrinology of Food Intake, Paris-Saclay Institute of Neuroscience, Orsay, France

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Mohammed Taouis UMR 9197, Molecular Neuroendocrinology of Food Intake, University Paris-Sud, University Paris-Saclay, Orsay, France
Department of Molecules and Circuits, CNRS UMR 9197, Molecular Neuroendocrinology of Food Intake, Paris-Saclay Institute of Neuroscience, Orsay, France

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all antibodies were from Cell Signaling Technology: LC3A/B, ATG7, P62, phospho (p)-AKT (ser473), AKT, p-mTOR (ser2448), mTOR, AMPK, p-AMPK, β-tubulin and TLR4. Blots were then incubated with secondary mouse or rabbit antibodies coupled to horseradish

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Véronique Serre-Beinier Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Christian Toso Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Philippe Morel Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Carmen Gonelle-Gispert Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Christelle Veyrat-Durebex Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Françoise Rohner-Jeanrenaud Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Thierry Calandra Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Thierry Roger Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Richard W James Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Xavier Montet Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery
Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery
Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Léo Bühler Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Domenico Bosco Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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Thierry Berney Surgical Research Unit, Department of Surgery, Laboratory of Metabolism, Infectious Diseases Service, Clinical Diabetes Unit, Radiology, Cell Physiology and Metabolism, Internal Medicine, Department of Surgery

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for 1 h at room temperature in a 10 mmol/l Tris–HCl buffer (pH 7.4) containing 150 mmol/l NaCl, 0.1% (v/v) Tween-20, and 5% BSA, and then incubated overnight at 4 °C with antibody. Antibodies against AKT and phospho-AKT (Ser 473 ) were obtained from

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Yoshimitsu Kuwabara Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Akira Katayama Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Ryoko Tomiyama Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Hu Piao Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Sachiko Kurihara Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan
Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Shuichi Ono Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Katsuya Mine Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Shigeo Akira Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Hideo Orimo Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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Toshiyuki Takeshita Departments of Obstetrics and Gynecology, Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5, Sendagi, Bunkyo-ku, Tokyo 113-8603, Japan

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(Cayman Chemical Company, Ann Arbor, MI, USA; cat #582601) according to the manufacturer's instructions. Western blotting analysis To analyze AKT phosphorylation, 10 μg of control or OPN-treated cell lysate was separated on a 4–20% SDS–polyacrylamide gel

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Bo Qian Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China
Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Haiyan Wang Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Xiuli Men Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Wenjian Zhang Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Hanqing Cai Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Shiqing Xu Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Yaping Xu Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Liya Ye Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Claes B Wollheim Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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Jinning Lou Graduate School of Peking Union Medical College, Institute of Clinical Medical Sciences, Department of Cell Physiology and Metabolism, Beijing 100730, People's Republic of China

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attracted interest in diabetes research as it has emerged as an endogenous inhibitor of Akt (PKB), which plays a key role in insulin signaling ( Du et al . 2003 ). In addition, the mRNA levels of TRIB3 are elevated in the liver of db/db mice ( Matsushima

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Ana Carolina Ronda Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, Bahía Blanca 8000, Argentina

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Andrea Vasconsuelo Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, Bahía Blanca 8000, Argentina

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Ricardo Boland Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, Bahía Blanca 8000, Argentina

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exerts antiapoptotic effects in the C2C12 muscle cell line upon exposure to H 2 O 2 or etoposide involving the phosphatidylinositol 3-kinase (PI3K)/AKT/BAD pathway ( Vasconsuelo et al . 2008 ). Also, the antiapoptotic action of the steroid hormone has

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Graziela R Stoppa
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Maristela Cesquini
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Erika A Roman
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Patrícia O Prada Departamento de Bioquímica, Departamento de Clinica Médica, Universidade Braz Cubas, IB, Universidade Estadual de Campinas, Campinas, SP, Brazil

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Adriana S Torsoni Departamento de Bioquímica, Departamento de Clinica Médica, Universidade Braz Cubas, IB, Universidade Estadual de Campinas, Campinas, SP, Brazil

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Talita Romanatto Departamento de Bioquímica, Departamento de Clinica Médica, Universidade Braz Cubas, IB, Universidade Estadual de Campinas, Campinas, SP, Brazil

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Mario J Saad Departamento de Bioquímica, Departamento de Clinica Médica, Universidade Braz Cubas, IB, Universidade Estadual de Campinas, Campinas, SP, Brazil

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Licio A Velloso Departamento de Bioquímica, Departamento de Clinica Médica, Universidade Braz Cubas, IB, Universidade Estadual de Campinas, Campinas, SP, Brazil

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Marcio A Torsoni Departamento de Bioquímica, Departamento de Clinica Médica, Universidade Braz Cubas, IB, Universidade Estadual de Campinas, Campinas, SP, Brazil

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(endovenous, EV). Protein expression was evaluated through immunoblotting with anti total-IR, anti total-IRS1, anti total-IRS2, and anti total-AKT. Protein expression did not change in either tissue (epididymal fat pad and skeletal muscle) after insulin

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Michelle Keramidas Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France

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Caroline Faudot Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France

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Agnès Cibiel Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France

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Jean-Jacques Feige Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France

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Michaël Thomas Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France
Institut National de la Santé et de la Recherche Médicale, Commissariat à l'Energie Atomique, Université Joseph Fourier, Unité 878, Grenoble, France

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hydrochloride), and 1 mM sodium orthovanadate) and separated by SDS-PAGE. After electrophoretic transfer onto a nitrocellulose membrane, the phosphorylated forms of ERK1/2 and Akt were analyzed by western blotting using phosphorylation site-specific antibodies

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Victor Wong Department of Medicine, Division of Endocrinology and Metabolism and the Department of Physiology, University of Toronto, Toronto, Ontario, Canada

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Linda Szeto Department of Medicine, Division of Endocrinology and Metabolism and the Department of Physiology, University of Toronto, Toronto, Ontario, Canada

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Kristine Uffelman Department of Medicine, Division of Endocrinology and Metabolism and the Department of Physiology, University of Toronto, Toronto, Ontario, Canada

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I George Fantus Department of Medicine, Division of Endocrinology and Metabolism and the Department of Physiology, University of Toronto, Toronto, Ontario, Canada

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Gary F Lewis Department of Medicine, Division of Endocrinology and Metabolism and the Department of Physiology, University of Toronto, Toronto, Ontario, Canada

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Biotechnology, Inc. (Santa Cruz, CA, USA). Agarose-conjugated anti-insulin receptor substrate-1 (anti-IRS-1) and anti-p85 subunit of phosphatidylinositol 3-kinase (PI3K) antibodies were purchased from Upstate Biotechnology, Inc. (Lake Placid, NY, USA). Anti-AKT

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Piotr Zabielski Department of Medical Biology, Medical University of Bialystok, Bialystok, Poland
Department of Physiology, Medical University of Bialystok, Bialystok, Poland

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Marta Chacinska Department of Physiology, Medical University of Bialystok, Bialystok, Poland
Department of Hygiene, Epidemiology and Metabolic Disorders, Medical University of Bialystok, Bialystok, Poland

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Karol Charkiewicz Department of Physiology, Medical University of Bialystok, Bialystok, Poland
Department of Perinatology, Medical University of Bialystok, Bialystok, Poland

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Marcin Baranowski Department of Physiology, Medical University of Bialystok, Bialystok, Poland

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Jan Gorski Department of Physiology, Medical University of Bialystok, Bialystok, Poland

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Agnieszka U Blachnio-Zabielska Department of Physiology, Medical University of Bialystok, Bialystok, Poland
Department of Hygiene, Epidemiology and Metabolic Disorders, Medical University of Bialystok, Bialystok, Poland

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isoenzymes ( Itani et al . 2002 ), whereas accumulation of Cer can inhibit the insulin signaling pathway via protein phosphatase 2A (PPA2)-mediated inhibition of Akt/PKB ( Schmitz-Peiffer et al . 1999 ) ( Fig. 1 ). Figure 1 Mechanism of FFA

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Jonathan M Mudry Section for Integrative Physiology, Section for Integrative Physiology, Department of Molecular Medicine and Surgery

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Julie Massart Section for Integrative Physiology, Section for Integrative Physiology, Department of Molecular Medicine and Surgery

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Ferenc L M Szekeres Section for Integrative Physiology, Section for Integrative Physiology, Department of Molecular Medicine and Surgery

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Anna Krook Section for Integrative Physiology, Section for Integrative Physiology, Department of Molecular Medicine and Surgery
Section for Integrative Physiology, Section for Integrative Physiology, Department of Molecular Medicine and Surgery

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641 (p-GS) (#3891), ACC (#3676), ACC phosphorylated on serine 79 (p-ACC) (#3661), AKT (or protein kinase B (PKB)) (#9272), and its phosphorylated form on serine 473 (p-AKT) (#9271) were purchased from Cell Signaling (Danvers, MA, USA), GAPDH (#sc

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