Blunting of protein synthesis during exercise in rat skeletal muscle

在工作的骨骼肌中蛋白质合成受到抑制。从目的上讲，肌肉停止消耗ATP的构建过程，以便在紧急情况下腾出ATP用于收缩活动，这是有意义的。至少到目前为止，已经提出了两种机制来钝化工作肌肉中的蛋白质合成。其中之一是AMPK抑制mTORC1的故事，mTORC1可以说是蛋白质翻译起始步骤的主调节因子。另一个故事是钙离子依赖的eEF2失活，它调节eEF2的伸长步骤。文献中的报道表明，其他因素而不是AMPK和/或eEF2可能参与了蛋白质合成的钝化。我们已经证明，Redd1也可能是钝化肌肉中蛋白质合成的候选基因。对这些机制的了解可能会导致开发新的策略和治疗方法，不仅适用于运动员，也适用于患有肌肉萎缩状况的个人，如石棺减少症。

Protein synthesis is suppressed in working skeletal muscle. Teleologically, it makes sense that the muscle stops an ATP-consuming building process to spare ATP for contractile activity in an emergency. At least so far two mechanisms have been proposed for blunting protein synthesis in working muscle. One of them is a story that AMPK inhibits mTORC1, which is arguably a master regulator of initiation step in protein translation. Another story is that Ca2+-dependent inactivation of eEF2, which regulates elongation step in it. Reports in the literature suggest that other factors rather than AMPK and/or eEF2 would be involved in the blunting of protein synthesis. We have shown that REDD1 might be also a candidate for blunting protein synthesis in working muscle. Understanding of these mechanisms may lead to development of new strategies and treatments not only for athletes but also for individuals with muscle-wasting conditions such as sarcopenia.