Insulin activates a PD 098059-sensitive kinase that is involved in the regulation of p70S6K and PHAS-I.
Insulin activates a PD 098059-sensitive kinase that is involved in the regulation of p70S6K and PHAS-I.
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胰岛素激活 PD 098059 敏感激酶，该激酶参与 p70S6K 和 PHAS-I 的调节。
DOI：
10.1016/s0014-5793(97)00500-0
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发表时间：
1997
期刊：
影响因子：
3.5
通讯作者：
LawrenceJr,JC
中科院分区：
文献类型：
--
作者：
Scott,PH;LawrenceJr,JC
无论是中国仓鼠卵巢(CHO)细胞还是3T3-L1脂肪细胞与胰岛素孵育均可增加eIF-4E结合蛋白PHAS-I的磷酸化。胰岛素还激活了p70S6K以及丝裂原激活蛋白激酶(MAP)的Erk-1和Erk-2亚型。然而，激活MAP激酶所需的激素浓度是增加PHAS-I磷酸化和p70S6K活性所需激素浓度的10-100倍。用MAP激酶(MEK)激活抑制剂PD098059孵育细胞，可阻断低浓度胰岛素对PHAS-I和p70S6K的影响。该抑制剂的作用可通过增加胰岛素浓度来克服。结果表明，胰岛素激活了参与调节p70S6K和PHAs-I的PD098059敏感的激酶。
Incubating either Chinese hamster ovary (CHO) cells or 3T3-L1 adipocytes with insulin increased the phosphorylation of the eIF-4E-binding protein, PHAS-I. Insulin also activated p70S6Kand the Erk-1 and Erk-2 isoforms of mitogen-activated protein kinase (MAP kinase). However, the concentrations of the hormone needed to activate MAP kinase were 10–100 times higher than those needed to increase PHAS-I phosphorylation and p70S6Kactivity. Incubating cells with the inhibitor of MAP kinase kinase (MEK) activation, PD098059, blocked the effects of low concentrations of insulin on PHAS-I and p70S6K. The effects of the inhibitor were overcome by increasing concentrations of insulin. The results indicate that insulin activates a PD098059-sensitive kinase that is involved in the regulation of both p70S6Kand PHAS-I.