Regulation of GLUT4 mRNA stability by tumor necrosis factor-alpha: alterations in both protein binding to the 3' untranslated region and initiation of translation.
Regulation of GLUT4 mRNA stability by tumor necrosis factor-alpha: alterations in both protein binding to the 3' untranslated region and initiation of translation.
复制标题
肿瘤坏死因子-α 对 GLUT4 mRNA 稳定性的调节：蛋白质与 3 非翻译区的结合和翻译起始的改变。
DOI：
10.1006/bbrc.1996.0512
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Pekala,PH
中科院分区：
文献类型：
--
作者：
Long,SD;Pekala,PH
我们实验室先前的研究表明，3 T3-L1脂肪细胞暴露于TNF导致GLUT 4 mRNA的半衰期从9.5小时（对照）减少50%至4.5小时（处理细胞）（1）。在目前的研究中，我们报告说，与信息半衰期的改变相一致，TNF处理导致蛋白质与3′UTR近端200个碱基的结合增加。此外，GLUT 4 mRNA在多核糖体中的分布也发生了改变，从而使信息以40 S前起始复合物的形式积累，这与起始的衰减一致。总之，我们的数据表明，GLUT 4 mRNA的衰减增强可能是通过一种机制发生的，该机制涉及40 s前起始复合物的积累，该复合物与3′UTR的蛋白结合增加相关。
Previous studies from our laboratory have demonstrated that exposure of the 3T3-L1 adipocytes to TNF resulted in a 50% decrease in the half-life of the GLUT4 mRNA from 9.5h (control) to 4.5h (treated cells) (1). In the current study we report that coincident with the alteration of the half-life of the message, TNF treatment resulted in an increase in the binding of a protein to the proximal 200 bases of the 3′UTR. In addition the distribution of GLUT4 mRNA in polysome profiles was altered such that message accumulated as a 40S preinitiation complex, consistent with an attenuation of initiation. In summary, our data suggest that enhanced decay of the GLUT4 mRNA may occur through a mechanism involving accumulation of a 40s preinitiation complex which correlates with increased protein binding to the 3′UTR.