Search Results
Search for other papers by Li Li in
Google Scholar
PubMed
Department of Psychiatry and Behavioral Neurobiology, St Vincent Health System, Department of Animal Sciences, Division of Molecular and Cellular Pathology, Veterans Affairs Medical Center, The University of Alabama at Birmingham, 1720 University Boulevard, Birmingham, Alabama 35294, USA
Search for other papers by Xiaohua Li in
Google Scholar
PubMed
Department of Psychiatry and Behavioral Neurobiology, St Vincent Health System, Department of Animal Sciences, Division of Molecular and Cellular Pathology, Veterans Affairs Medical Center, The University of Alabama at Birmingham, 1720 University Boulevard, Birmingham, Alabama 35294, USA
Search for other papers by Wenjun Zhou in
Google Scholar
PubMed
Department of Psychiatry and Behavioral Neurobiology, St Vincent Health System, Department of Animal Sciences, Division of Molecular and Cellular Pathology, Veterans Affairs Medical Center, The University of Alabama at Birmingham, 1720 University Boulevard, Birmingham, Alabama 35294, USA
Search for other papers by Joseph L Messina in
Google Scholar
PubMed
). The protein concentrations of tissue lysates were determined by the BCA method (Pierce, Rockford, IL, USA). For immunoblotting, protein was separated by SDS–PAGE and analyzed by specific antibodies including anti-phosphothreonine 308-AKT, anti
Search for other papers by Márcio Pereira-da-Silva in
Google Scholar
PubMed
Search for other papers by Cláudio T De Souza in
Google Scholar
PubMed
Search for other papers by Alessandra L Gasparetti in
Google Scholar
PubMed
Search for other papers by Mário J A Saad in
Google Scholar
PubMed
Search for other papers by Lício A Velloso in
Google Scholar
PubMed
-pERK (αpERK/Tyr 204, detecting pERK42 and pERK44), anti-Akt1, and anti-phospho [Ser 473 ]Akt1 were from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Rabbit anti-p85/phosphatidylinositol-3 kinase (PI3-kinase) antiserum was from UBI (Lake Placid, NY, USA
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
Search for other papers by Te Du in
Google Scholar
PubMed
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
Search for other papers by Liu Yang in
Google Scholar
PubMed
Search for other papers by Xu Xu in
Google Scholar
PubMed
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
Search for other papers by Xiaofan Shi in
Google Scholar
PubMed
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
Search for other papers by Xin Xu in
Google Scholar
PubMed
Search for other papers by Jian Lu in
Google Scholar
PubMed
Search for other papers by Jianlu Lv in
Google Scholar
PubMed
Search for other papers by Xi Huang in
Google Scholar
PubMed
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
Search for other papers by Jing Chen in
Google Scholar
PubMed
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
Search for other papers by Heyao Wang in
Google Scholar
PubMed
Search for other papers by Jiming Ye in
Google Scholar
PubMed
Search for other papers by Lihong Hu in
Google Scholar
PubMed
School of Pharmacy, University of Chinese Academy of Sciences, Beijing, China
School of Medicine and Life Sciences, Nanjing University of Chinese Medicine, Nanjing, China
Search for other papers by Xu Shen in
Google Scholar
PubMed
-coupled receptors, Akt, IRS2, PTEN, Fas/FasL, NF-κb, Bcl2 family, caspase family, ion channels and so on are tightly associated with β-cell apoptosis ( Anuradha et al . 2014 , Reimann & Gribble 2016 ), and some of the β-cell apoptosis-related proteins have been
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Patrícia Oliveira Prada in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Michella Soares Coelho in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Henrique Gottardello Zecchin in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Miriam Sterman Dolnikoff in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Alessandra Lia Gasparetti in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Luzia Naôko Shinohara Furukawa in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Mario José Abdalla Saad in
Google Scholar
PubMed
Departamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil
Departamento de Clínica Médica, Divisão de Nefrologia, Laboratório de Hipertensão Experimental da Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
Search for other papers by Joel Claudio Heimann in
Google Scholar
PubMed
2002 ). Following tyrosine phosphorylation, IRS-1 and IRS-2 bind and activate the enzyme phosphatidylinositol 3-kinase (PI3-K) ( Folli et al. 1992 , Saltiel & Pessin 2002 ). The activation of PI3-K increases serine phosphorylation of Akt (protein
Search for other papers by Ida Alenkvist in
Google Scholar
PubMed
Search for other papers by Oleg Dyachok in
Google Scholar
PubMed
Search for other papers by Geng Tian in
Google Scholar
PubMed
Search for other papers by Jia Li in
Google Scholar
PubMed
Search for other papers by Saba Mehrabanfar in
Google Scholar
PubMed
Search for other papers by Yang Jin in
Google Scholar
PubMed
Search for other papers by Bryndis Birnir in
Google Scholar
PubMed
Search for other papers by Anders Tengholm in
Google Scholar
PubMed
Search for other papers by Michael Welsh in
Google Scholar
PubMed
FAK activity, which in turn acts as a scaffold in focal adhesions and activates various downstream signaling pathways, such as AKT and ERK ( Parsons 2003 ). In β-cells, FAK has been shown to convey signals from the extracellular matrix ( Hammar et al
Search for other papers by Sattar Gorgani-Firuzjaee in
Google Scholar
PubMed
Search for other papers by Salar Bakhtiyari in
Google Scholar
PubMed
Search for other papers by Abolfazl Golestani in
Google Scholar
PubMed
Department of Biochemistry, Department of Clinical Biochemistry, Endocrinology and Metabolism Research Centre, Faculty of Medicine, Tehran University of Medical Sciences, Tehran, Islamic Republic of Iran
Search for other papers by Reza Meshkani in
Google Scholar
PubMed
carried out through overnight incubation at 4 °C with 5% nonfat dry milk in TBS with 0.5% Tween 20. Blots were incubated with antibodies against LAR, p-IRS1 (Tyr632), and IRS1 (Santa Cruz Biotechnology); Akt and phospho-Akt (Ser473) (Cell Signaling
Search for other papers by Hikari Hirakida in
Google Scholar
PubMed
Search for other papers by Taiga Okumura in
Google Scholar
PubMed
Search for other papers by Ryosuke Fujita in
Google Scholar
PubMed
Search for other papers by Yoshiki Kuse in
Google Scholar
PubMed
Search for other papers by Takahiro Mizoguchi in
Google Scholar
PubMed
Search for other papers by Satoshi Inagaki in
Google Scholar
PubMed
Search for other papers by Shinsuke Nakamura in
Google Scholar
PubMed
Lab. of Collaborative Research for Innovative Drug Discovery, Gifu Pharmaceutical University, Gifu, Japan
Search for other papers by Masamitsu Shimazawa in
Google Scholar
PubMed
Lab. of Collaborative Research for Innovative Drug Discovery, Gifu Pharmaceutical University, Gifu, Japan
Search for other papers by Hideaki Hara in
Google Scholar
PubMed
:1000; Santa Cruz Biotechnology, catalogue sc-365397), mouse anti-β-actin (1:2000; Sigma-Aldrich, catalogue A2228), rabbit anti-phospho-Akt (1:1000; Cell Signaling, catalogue 4058), rabbit anti-total-Akt (1:1000; Cell Signaling, catalogue 9272), rabbit anti
Search for other papers by Kai Wang in
Google Scholar
PubMed
Search for other papers by Jing Zheng in
Google Scholar
PubMed
specific receptors that have cytoplasmic tyrosine kinase domains. Upon activation, these receptor-tyrosine kinases initiate a cascade of cellular protein phosphorylation by protein kinases (PKs), including ERK1/2, AKT1, and p38 MAPK ( Cobb 1999 , Boilly
Chronic Disease Program, Departments of Medicine and of Biochemistry, Ottawa Health Research Institute, 725 Parkdale Avenue, Ottawa, Ontario, Canada K1Y 4E9
Search for other papers by AnneMarie Gagnon in
Google Scholar
PubMed
Chronic Disease Program, Departments of Medicine and of Biochemistry, Ottawa Health Research Institute, 725 Parkdale Avenue, Ottawa, Ontario, Canada K1Y 4E9
Search for other papers by Anne Landry in
Google Scholar
PubMed
Chronic Disease Program, Departments of Medicine and of Biochemistry, Ottawa Health Research Institute, 725 Parkdale Avenue, Ottawa, Ontario, Canada K1Y 4E9
Search for other papers by Alexander Sorisky in
Google Scholar
PubMed
a nitrocellulose membrane. Non-specific binding sites were blocked and membranes were incubated with antibodies specific for actin (0.4 μg/ml; Santa Cruz Biotech., Santa Cruz, CA, USA), AKT (clone C-20; 2 μg/ml; Santa Cruz Biotech.), fatty acid
Search for other papers by Ewa Ocłoń in
Google Scholar
PubMed
Search for other papers by Anna Latacz in
Google Scholar
PubMed
Search for other papers by Joanna Zubel–Łojek in
Google Scholar
PubMed
Search for other papers by Krystyna Pierzchała–Koziec in
Google Scholar
PubMed
. miRNAs Significant pathways P -value Target genes mir-144-3p miR-675-5p miR-193a-3p Insulin signaling pathway (04910) 0.006 GSK3B, SOS2, CALM1, SOCS2, PIK3CB, PPP1CC, PCK2, KRAS, TSC2, EIF4E, MAPK8, PRKX, PRKAA1, AKT3, MTOR miR