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首页> 外文期刊>Life sciences >AMP-activated protein kinase regulates PDGF-BB-stimulated interleukin-6 synthesis in osteoblasts: Involvement of mitogen-activated protein kinases
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AMP-activated protein kinase regulates PDGF-BB-stimulated interleukin-6 synthesis in osteoblasts: Involvement of mitogen-activated protein kinases

机译：AMP激活的蛋白激酶调节成骨细胞中PDGF-BB刺激的白介素6合成：促分裂原激活的蛋白激酶的参与

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Aim: We have previously reported that platelet-derived growth factor (PDGF)-BB stimulates synthesis of interleukin-6 (IL-6), a potent bone resorptive agent, in osteoblast-like MC3T3-E1 cells, and that the activation of p44/p42 mitogen-activated protein (MAP) kinase, p38MAP kinase and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) is implicated in the IL-6 synthesis. In the present study,we investigated the involvement of AMP-activated protein kinase (AMPK), a regulator of energy metabolism, in the PDGF-BB-stimulated IL-6 synthesis in MC3T3-E1 cells. Main methods: The levels of IL-6 were measured by ELISA. The phosphorylation of each protein kinases was analyzed by Western blotting. The mRNA levels of IL-6 were determined by real-time RT-PCR. Key findings: PDGF-BB time-dependently induced the phosphorylation of AMPK. Compound C, an inhibitor of AMPK, which reduced PDGF-BB-induced acetyl-CoA carboxylase phosphorylation, dose-dependently suppressed the PDGF-BB-stimulated IL-6 release. In addition, the PDGF-BB-stimulated IL-6 release in human osteoblasts was also inhibited by compound C. The mRNA expression of IL-6 induced by PDGF-BB was markedly reduced by compound C. The PDGF-BB-induced phosphorylation of p44/p42 MAP kinase, p38 MAP kinase and SAPK/JNK was inhibited by compound C. Significance: These results strongly suggest that AMPK positively regulates PDGF-BB-stimulated IL-6 synthesis via the MAP kinases in osteoblasts.
机译：目的：我们先前曾报道过血小板衍生的生长因子（PDGF）-BB刺激成骨细胞样MC3T3-E1细胞中白细胞介素6（IL-6）（一种有效的骨吸收剂）的合成，并且p44的激活/ p42丝裂原活化蛋白（MAP）激酶，p38MAP激酶和应激活化蛋白激酶/ c-Jun N末端激酶（SAPK / JNK）与IL-6合成有关。在本研究中，我们调查了AMP活化蛋白激酶（AMPK），一种能量代谢调节剂，参与PDGF-BB刺激的MC3T3-E1细胞中IL-6的合成。主要方法：采用ELISA法测定IL-6水平。通过蛋白质印迹分析每种蛋白激酶的磷酸化。通过实时RT-PCR测定IL-6的mRNA水平。主要发现：PDGF-BB随时间诱导AMPK磷酸化。化合物C是AMPK的抑制剂，可减少PDGF-BB诱导的乙酰辅酶A羧化酶磷酸化，其剂量依赖性地抑制PDGF-BB刺激的IL-6释放。此外，化合物C还抑制了PDGF-BB刺激的成骨细胞中IL-6的释放。化合物C显着降低了PDGF-BB诱导的IL-6的mRNA表达。PDGF-BB诱导的成骨细胞的磷酸化。 p44 / p42 MAP激酶，p38 MAP激酶和SAPK / JNK被化合物C抑制。这些结果强烈表明AMPK通过MAP激酶在成骨细胞中正调控PDGF-BB刺激的IL-6合成。

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