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Department of Endocrinology, The Second Affiliated Hospital, Chongqing Medical University, Chongqing, China
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Department of Endocrinology, The Second Affiliated Hospital, Chongqing Medical University, Chongqing, China
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Technology Cat# 3024, RRID:AB_331253), anti-AKT kinase (AKT) (Cell Signaling Technology Cat# 9272, RRID:AB_329827)/anti-phospho-AKT (Cell Signaling Technology Cat# 9271, RRID:AB_329825), anti-mammalian target of rapamycin (mTOR) (Cell Signaling Technology Cat
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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
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Institute of Liver Diseases, Shanghai University of Traditional Chinese Medicine, Shanghai, China
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Institute of Liver Diseases, Shanghai University of Traditional Chinese Medicine, Shanghai, 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
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lifespan of this murine model of metabolic syndrome without affecting body weight by attenuating AKT signaling and chronic low-grade inflammation. Materials and Methods Animals KK/Ta mice and C57BL/6N mice as a control were purchased from CLEA Japan (Tokyo
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activated by BK in MCF-7 cells, paying attention to those pathways previously highlighted in primary normal and cancerous breast cells (i.e. PKCs, PI3K/Akt and ERK1/2 signalling) ( Greco et al. 2004 , 2005 ); furthermore, the possibility that BK is
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suggest the ability of the hormone to activate extranuclear receptors ( Bjornstrom & Sjoberg 2005 ). Among the rapid non-transcriptional actions of E 2 , the activation of the phosphatidylinositol 3-kinase (PI3K)/Akt pathway has been shown in various
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consensus sequence for phosphorylation by Akt, and Akt kinase enhances the human telomerase activity through phosphorylation of hTERT ( Kang et al. 1999 ). In addition, it was recently reported that estrogen protects against Aβ- ( Zhang et al. 2001 ) or
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). Anti-BCL2 (sc492), anti-signal transducer and activator of transcription 3 (STAT3) (sc483), anti-phospho-STAT3 Tyr (sc8059), anti-CHOP (sc575 and sc793), anti-phospho-AKT1/2/3 Ser (sc33437), anti-tribble3 (TRIB3) (sc34212), and anti
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roles of the AKT–MTOR and ERK cascades in the regulation of VEGF and endoglin production under hypoxic conditions in the trophoblast-derived cell line, BeWo. Materials and Methods Materials The phosphatidylinositol 3-kinase (PI3K) inhibitor, LY294002
Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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Department of Molecular and Cellular Biology,
Department of Medicine, The Breast Center, Baylor College of Medicine, USDA/ARS Children’s Nutrition Research Center, 1100 Bates Street, Houston, Texas 77030, USA
Department of Metabolic Diseases, Graduate School of Medicine, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8655, Japan
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the serine threonine kinase Akt ( Datta et al. 1997 ). The activation of Akt in response to insulin or IGF-I stimulation mediates the ability of these two hormones to inhibit apoptosis ( Datta et al. 1997 ). However, activation of Akt has also