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Though its mechanism of action is unclear, studies suggest that it can increase glucose uptake in muscle cells, thereby supporting recoveryfrom fatigue. As discussed in our previous publication in Cell, it appears to have a biphasic action that is associated with fatigue, with its effect reduced only by training. In addition, although it increases resting oxygen uptake in skeletal muscle by up to 6%, it does not stimulate skeletal muscle protein synthesis. Our findings demonstrate that the protein synthetic activity is the determining factor in the increased rate of amino acid incorporation.Our previous work on the mechanisms of exercise on muscle protein synthesis (López-Jaramillo et al. ., 2014; Azzouni et al. , 2014) suggested that protein synthesis is controlled by intracellular signaling pathways. For example, it has been shown that muscle insulin resistance and muscle protein breakdown are influenced by exercise-induced activation of CREB and PGC-1α, respectively (Morris et al. , 2011). We have shown that in skeletal muscle, the CREB-PGC-1α pathway is activated post exercise to inhibit protein synthesis during subsequent post-exercise recovery (López-Carmio et al. , 2009; Azzouni et al. , 2014). We observed a similar pattern of post-exercise inhibition of protein synthesis as observed for resistance training, which is thought to be mediated by activation of signaling pathways known as MAPK/ERK (Garrido et al. , 2014). Additionally, this same pathway was shown to be inhibited in the skeletal muscle of elderly persons on protein-supplemented amino acid (PA) diets (López-Jaramillo et al. , 2013). The recent review conducted by Garrido and colleagues concluded that PA diets may have a direct effect on the phosphorylation of proteins in skeletal muscle (Garrido et al. , 2014). Because our current results are consistent with our previous work and their conclusion that PA diets reduce protein synthesis, the fact that we observed a decrease in the rate of protein synthesis following exercise-induced activation of the protein synthetic pathway supports that the effects are specific to protein synthesis.The fact that training-induced phosphorylation of the PGC-1α pathway was inhibited is also consistent with a large body of literature (Azzouni et al. , 2014), which showed that exercise, but not resistance exercise, significantly reduces PGC-1α phosphorylation and protein synthetic activity in human skeletal muscle (López-Jaramillo et al. , 2009; Azzouni et al. , 2014; Borsheim etRelated Article: