AIMS: Chemerin is a novel adipokine that is closely associated with cardiovascular diseases and glucose homeostasis. This study aimed to investigate the effects of chemerin on insulin resistance in rat cardiomyocytes. METHODS: Rat cardiomyocytes were treated with high concentrations of glucose and tumor necrosis factor-alpha (TNF-α), and chemerin and chemokine-like receptor 1 (CMKLR1) were measured by Western blot analysis. Then, the cardiomyocytes were treated with chemerin and insulin. Glucose uptake was evaluated using a fluorescence microplate reader. Western blot analysis was used to evaluate the phosphorylation of Akt, insulin receptor substrate-1, p38 mitogen-activated protein kinase (MAPK), as well as extracellular signal-regulated kinase (ERK)1/2. RESULTS: Chemerin and CMKLR1 were found to be expressed in rat cardiomyocytes. Pretreatment with chemerin caused decreases in glucose uptake and phosphorylation of Akt in insulin-stimulated cardiomyocytes. Furthermore, chemerin activated the phosphorylation of p38 MAPK and ERK1/2 in insulin-stimulated cardiomyocytes. Inhibition of ERK partially rescued chemerin-induced insulin resistance. CONCLUSION: Chemerin is a novel adipokine that induces insulin resistance in rat cardiomyocytes in part through the ERK1/2 pathway.
AIMS: Chemerin is a novel adipokine that is closely associated with cardiovascular diseases and glucose homeostasis. This study aimed to investigate the effects of chemerin on insulin resistance in rat cardiomyocytes. METHODS:Rat cardiomyocytes were treated with high concentrations of glucose and tumor necrosis factor-alpha (TNF-α), and chemerin and chemokine-like receptor 1 (CMKLR1) were measured by Western blot analysis. Then, the cardiomyocytes were treated with chemerin and insulin. Glucose uptake was evaluated using a fluorescence microplate reader. Western blot analysis was used to evaluate the phosphorylation of Akt, insulin receptor substrate-1, p38 mitogen-activated protein kinase (MAPK), as well as extracellular signal-regulated kinase (ERK)1/2. RESULTS:Chemerin and CMKLR1 were found to be expressed in rat cardiomyocytes. Pretreatment with chemerin caused decreases in glucose uptake and phosphorylation of Akt in insulin-stimulated cardiomyocytes. Furthermore, chemerin activated the phosphorylation of p38MAPK and ERK1/2 in insulin-stimulated cardiomyocytes. Inhibition of ERK partially rescued chemerin-induced insulin resistance. CONCLUSION:Chemerin is a novel adipokine that induces insulin resistance in rat cardiomyocytes in part through the ERK1/2 pathway.
Authors: Karla Bianca Neves; Aurelie Nguyen Dinh Cat; Rheure Alves-Lopes; Katie Yates Harvey; Rafael Menezes da Costa; Nubia Souza Lobato; Augusto Cesar Montezano; Ana Maria de Oliveira; Rhian M Touyz; Rita C Tostes Journal: Am J Physiol Heart Circ Physiol Date: 2018-09-14 Impact factor: 4.733
Authors: Alberto J Arribas; Andrea Rinaldi; Giorgia Chiodin; Ivo Kwee; Afua Adjeiwaa Mensah; Luciano Cascione; Davide Rossi; Meena Kanduri; Richard Rosenquist; Emanuele Zucca; Peter W Johnson; Gianluca Gaidano; Christopher C Oakes; Francesco Bertoni; Francesco Forconi Journal: Blood Adv Date: 2019-02-12
Authors: Rui Liu; Jun-Chun Tang; Meng-Xian Pan; Yang Zhuang; Ya Zhang; Hua-Bao Liao; Dan Zhao; Yang Lei; Rui-Xue Lei; Shu Wang; An-Chun Liu; Xing-Ping Qin; Juan Chen; Zhi-Feng Zhang; Qi Wan Journal: Neurochem Res Date: 2018-06-07 Impact factor: 3.996
Authors: Karla Bianca Neves; Augusto Cesar Montezano; Rheure Alves-Lopes; Thiago Bruder-Nascimento; Rafael Menezes Costa; Roberto S Costa; Rhian M Touyz; Rita C Tostes Journal: Int J Mol Sci Date: 2018-08-19 Impact factor: 5.923