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首页> 外文期刊>Life sciences >Adiponectin-mediated stimulation of AMP-activated protein kinase (AMPK) in pancreatic beta cells.
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Adiponectin-mediated stimulation of AMP-activated protein kinase (AMPK) in pancreatic beta cells.

机译：脂联素介导的胰腺β细胞中AMP激活的蛋白激酶（AMPK）的刺激。

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摘要

The adipocyte-derived hormone adiponectin was recently shown to stimulate glucose-utilization and to increase fatty acid oxidation in liver and muscle. The effects were ascribed to adiponectin-receptor mediated activation of the key metabolic regulator AMP-activated protein kinase (AMPK). In pancreatic beta cells, AMPK-activation is known to affect cellular function. We therefore investigated a possible adiponectin-induced activation of AMPK in beta cells. RT-PCR analysis confirmed the expression of adiponectin receptor subtypes 1 and 2 in rat beta cells and showed their expression in insulin-secreting MIN6 cells. Culture with physiological concentrations (2.5 microg/ml) of globular adiponectin was found to increase the phosphorylation of both AMPK and acetylcoA carboxylase (ACC) in these cell types. Like the pharmacological AMPK activator 5-amino-imidazole-4-carboxamide-riboside (AICAR), adiponectin activated AMPK in beta cells and MIN6 cells. In short-term incubations of MIN6 cells with either adiponectin (2.5 microg/ml) or AICAR (1 mM), the flux of glucose-carbon to acyl CoA/cholesterol biosynthetic intermediates was reduced. We conclude that adiponectin induces an activation of AMPK in beta cells, which inhibits their cataplerosis of glucose-carbon to lipids.
机译：最近显示，源自脂肪细胞的激素脂联素可以刺激葡萄糖利用，并增加肝脏和肌肉中的脂肪酸氧化。影响归因于脂联素受体介导的关键代谢调节剂AMP激活的蛋白激酶（AMPK）的激活。在胰腺β细胞中，已知AMPK激活会影响细胞功能。因此，我们研究了可能的脂联素诱导的β细胞中AMPK的激活。 RT-PCR分析证实了脂联素受体亚型1和2在大鼠beta细胞中的表达，并显示了它们在分泌胰岛素的MIN6细胞中的表达。发现在这些细胞类型中，以生理浓度（2.5微克/毫升）的球状脂联素进行培养可增加AMPK和乙酰辅酶A羧化酶（ACC）的磷酸化。像药理AMPK激活剂5-氨基咪唑-4-羧酰胺-核糖核苷（AICAR）一样，脂联素激活β细胞和MIN6细胞中的AMPK。在MIN6细胞与脂联素（2.5 microg / ml）或AICAR（1 mM）的短期孵育中，葡萄糖碳到酰基CoA /胆固醇生物合成中间体的通量减少。我们得出的结论是，脂联素诱导了β细胞中AMPK的激活，从而抑制了其葡萄糖-碳对脂质的分解。

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