Sale E M, Atkinson P P, Arnott C H, Chad J E, Sale G J
Division of Biochemistry and Molecular Biology, School of Biological Sciences, Southampton, UK.
FEBS Lett. 1999 Mar 5;446(1):122-6. doi: 10.1016/s0014-5793(99)00193-3.
The signalling pathways by which insulin triggers protein synthesis were studied using an antisense strategy to deplete ERK1/ERK2 and rapamycin to inhibit the p70S6K pathway. The results indicated that ERK1/ERK2 principally regulated the amount of the protein synthesis machinery available in the cell while the p70S6K pathway contributed to modulating its activation in response to insulin. ERK1/ERK2 also mediated in a small proportion of insulin-stimulated protein synthesis which included the induction of c-fos protein. When c-fos induction was blocked the majority of insulin-stimulated protein synthesis still occurred and thus did not require transcriptional regulation of c-fos or its targets.
利用反义策略去除细胞外调节蛋白激酶1/2（ERK1/ERK2）以及使用雷帕霉素抑制p70核糖体蛋白S6激酶（p70S6K）信号通路，对胰岛素触发蛋白质合成的信号通路进行了研究。结果表明，ERK1/ERK2主要调节细胞内可用的蛋白质合成机制的数量，而p70S6K信号通路则有助于调节其对胰岛素的反应激活。ERK1/ERK2也介导了一小部分胰岛素刺激的蛋白质合成，其中包括c-fos蛋白的诱导。当c-fos诱导被阻断时，大部分胰岛素刺激的蛋白质合成仍然发生，因此不需要c-fos或其靶标的转录调控。
