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首页> 外文期刊>Cell biology international. >Intracellular signal transduction pathways induced by leptin in C2C12 cells.
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Intracellular signal transduction pathways induced by leptin in C2C12 cells.

机译:瘦素在C2C12细胞中诱导的细胞内信号转导途径。

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As experimental evidence suggests that leptin may have direct effects on peripheral tissues, we investigated some of the transductional molecules induced by leptin in C2C12 cells. In immunoprecipitation experiments using anti-p85 antibodies (a regulatory subunit of phosphatidylinositol-3-kinase; PI3K), we observed a significant increase in PI3K activity. Immunoblot analyses showed that Akt, GSK3, ERK1, ERK2, and p38 mitogen-activated protein kinase (p38 MAPK) phosphorylation significantly increased after leptin treatment. Protein kinase C (PKC)-zeta was also activated by leptin, as documented by an immunocomplex kinase assay and immunoblotting experiments. The treatment of C2C12 cells with Wortmannin before leptin administration inhibited induction of the phosphorylation of ERKs (extracellular signal-regulated kinases) but not that of p38 MAPK, whereas pre-treatment with a PKC-zeta inhibitor partially decreased ERK phosphorylation. Taken together, our in vitro results further support the hypothesis that leptin acts acutely on skeletal muscle tissue through some of the components of insulin signalling, including PKC-zeta.
机译:由于实验证据表明瘦素可能对周围组织有直接作用,我们研究了瘦素在C2C12细胞中诱导的一些转导分子。在使用抗p85抗体(磷脂酰肌醇3-激酶的调节亚基; PI3K)的免疫沉淀实验中,我们观察到PI3K活性显着增加。免疫印迹分析表明,瘦素治疗后,Akt,GSK3,ERK1,ERK2和p38丝裂原活化蛋白激酶(p38 MAPK)磷酸化显着增加。蛋白激酶C(PKC)-zeta也被瘦素激活,如免疫复合激酶测定和免疫印迹实验所证明。瘦素给药前用Wortmannin处理C2C12细胞可抑制ERKs(细胞外信号调节激酶)磷酸化的诱导,但不能抑制p38 MAPK的磷酸化,而用PKC-zeta抑制剂预处理可部分降低ERK的磷酸化。综上所述,我们的体外研究结果进一步支持了以下假设:瘦素通过胰岛素信号的某些成分(包括PKC-zeta)对骨骼肌组织产生急性作用。

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