Possible involvement of AMP-activated protein kinase in PGE1-induced synthesis of osteoprotegerin in osteoblasts
Possible involvement of AMP-activated protein kinase in PGE1-induced synthesis of osteoprotegerin in osteoblasts
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DOI：
10.3892/etm.2016.3099
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发表时间：
2016-05-01
影响因子：
2.7
通讯作者：
Tokuda, Haruhiko
中科院分区：
文献类型：
--
作者：
Kainuma, Shingo;Otsuka, Takanobu;Tokuda, Haruhiko
AMP激活的蛋白激酶（AMPK）是细胞能量平衡的重要调节因子。我们以前曾报道前列腺素E-1（PGE（1））通过p38丝裂原活化蛋白（MAP）激酶和应激活化蛋白激酶/c-Jun N-末端激酶（SAPK/JNK）刺激成骨样细胞MC 3 T3-E1合成骨保护素。本研究探讨AMPK参与PGE（1）诱导的MC 3 T3-E1细胞骨保护素合成。采用酶联免疫吸附试验测定骨保护素水平，采用蛋白质印迹法分析AMPK、乙酰辅酶A羧化酶、p38 MAP激酶和SAPK/JNK的磷酸化。此外，通过逆转录-定量聚合酶链反应测定骨保护素的mRNA表达水平。结果表明，PGE（1）可显著诱导AMPK α和β亚基的磷酸化，并呈时间依赖性（P
AMP-activated protein kinase (AMPK) is firmly established as a central regulator of cellular energy homeostasis. We have previously reported that prostaglandin E-1 (PGE(1)) stimulates the synthesis of osteoprotegerin through p38 mitogen-activated protein (MAP) kinase and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in osteoblast-like MC3T3-E1 cells. The present study investigated the involvement of AMPK in PGE(1)-induced osteoprotegerin synthesis in MC3T3-E1 cells. The levels of osteoprotegerin were measured using an enzyme-linked immunosorbent assay, while the phosphorylation of AMPK, acetyl-CoA carboxylase, p38 MAP kinase and SAPK/JNK were analyzed by western blotting. In addition, the mRNA expression levels of osteoprotegerin were determined by a reverse transcription-quantitative polymerase chain reaction. It was revealed that PGE(1) significantly induced the phosphorylation of the alpha and beta subunits of AMPK in a time-dependent manner (P