The adipokine zinc-α2-glycoprotein activates AMP kinase in human primary skeletal muscle cells
The adipokine zinc-α2-glycoprotein activates AMP kinase in human primary skeletal muscle cells
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DOI：
10.3109/13813455.2011.560950
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发表时间：
2011-05-01
影响因子：
3
通讯作者：
Eckel, Juergen
中科院分区：
文献类型：
--
作者：
Eckardt, Kristin;Schober, Annette;Eckel, Juergen
内容：锌-α 2-糖蛋白（ZAG）通过上调UCP亚型和GLUT 4诱导脂肪组织（AT）脂质动员并刺激AT和骨骼肌的能量利用。目的：我们的研究旨在探讨ZAG是否激活人骨骼肌细胞（SkMc）中能量代谢的重要调节因子AMPK α。用重组ZAG处理SkMc，分析AMPK α和ACC的活化、GLUT 4的蛋白丰度以及UCP 2和UCP 3基因表达。用ZAG处理SkMc可诱导AMPKa和ACC的短时间磷酸化，并且AMPKa磷酸化在24 h后升高，而对于ACC没有观察到活化。GLUT 4水平增加了1.3倍。然而，UCP 2和UCP 3表达保持不变。讨论和结论：这些结果表明，ZAG导致AMPKa和ACC的磷酸化，从而激活调节能量代谢的中心途径。这种机制可能参与介导ZAG与增加能量利用有关的作用。
Context: Zinc-alpha 2-glycoprotein (ZAG) induces lipid mobilization in adipose tissue (AT) and stimulates energy utilization in AT and skeletal muscle by up-regulation of UCP isoforms and GLUT4.Objective: Our study aimed to investigate whether ZAG activates AMPK alpha, an important regulator of energy metabolism, in human skeletal muscle cells (SkMc).Materials and Methods: SkMc were treated with recombinant ZAG, and activation of AMPK alpha and ACC, protein abundance of GLUT4, and UCP2 and UCP3 gene expression were analysed.Results: Treatment of SkMc with ZAG induced short-time phosphorylation of AMPKa and ACC. Furthermore, AMPKa phosphorylation was elevated after 24 h, while for ACC no activation was observed. GLUT4 level was increased by 1.3-fold. However, UCP2 and UCP3 expression remained unaltered. Discussion andConclusion: These results show that ZAG leads to phosphorylation of AMPKa and ACC, thereby activating a pathway central to the regulation of energy metabolism. This mechanism may be involved in mediating the effects of ZAG in relation to increased energy utilization.