Phorbol ester, serum, and rous sarcoma virus transforming gene product induce similar phosphorylations of ribosomal protein S6.
Phorbol ester, serum, and rous sarcoma virus transforming gene product induce similar phosphorylations of ribosomal protein S6.
复制标题
佛波酯、血清和劳斯肉瘤病毒转化基因产物诱导核糖体蛋白 S6 的类似磷酸化。
DOI：
10.1073/pnas.81.20.6408
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发表时间：
1984
影响因子：
11.1
通讯作者：
Erikson,RL
中科院分区：
文献类型：
--
作者：
Blenis,J;Spivack,JG;Erikson,RL
添加佛波醇12-肉豆蔻酸酯13-乙酸酯（PMA），一种有效的肿瘤促进剂，血清饥饿的静止鸡胚成纤维细胞（CEF）或C127小鼠细胞导致40 S核糖体蛋白S6的磷酸化增加。PMA对静止CEF中S6磷酸化的影响在约等于100 nM时为半最大，在16 nM时很容易观察到。此外，S6磷酸化增加血清饥饿CEF与二酰基甘油衍生物，1-油酰基-2-乙酰基甘油。通过磷酸化氨基酸分析、双向聚丙烯酰胺凝胶电泳、V8蛋白酶限制性蛋白水解和胰凝乳蛋白酶消化的双向薄层电泳，分析PMA刺激、血清刺激和血清饥饿的劳斯肉瘤病毒转化的CEF中S6磷酸化。通过这些方法比较S6磷酸化表明，PMA、血清或劳斯肉瘤病毒致癌转化刺激的S6磷酸化通过共同途径发生。这进一步得到了以下观察结果的支持：向CEF中同时加入PMA和血清，或向劳斯肉瘤病毒转化的CEF中同时加入PMA或血清，均未显著进一步增加磷酸盐掺入S6中。
The addition of phorbol 12-myristate 13-acetate (PMA), a potent tumor promoter, to serum-starved quiescent chicken embryo fibroblasts (CEF) or C127 murine cells resulted in increased phosphorylation of 40S ribosomal protein S6. The effect of PMA on S6 phosphorylation in quiescent CEF was half-maximal at approximately equal to 100 nM and was readily observed at 16 nM. In addition, S6 phosphorylation was increased in serum-starved CEF incubated with the diacylglycerol derivative, 1-oleoyl-2-acetylglycerol. S6 phosphorylation in PMA-stimulated, serum-stimulated, and serum-starved Rous sarcoma virus-transformed CEF was analyzed by phospho amino acid analysis, two-dimensional polyacrylamide gel electrophoresis, limited proteolysis with V8 protease, and two-dimensional thin-layer electrophoresis of chymotryptic digests. Comparison of S6 phosphorylation by these methods suggests that phosphorylation of S6 stimulated by PMA, serum, or oncogenic transformation with Rous sarcoma virus occurs through common pathways. This is further supported by the observation that the simultaneous addition of PMA and serum to CEF or of either PMA or serum to Rous sarcoma virus-transformed CEF did not significantly further increase the incorporation of phosphate into S6.