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The availability of the limiting EAA will limit the rate of muscle protein synthesis, regardless of the availability of all the other EAAs and NEAAs. In the case of muscle from those in the lower body, and even those in the upper body (although less than in the lower body), muscle protein synthesis will be lower because protein synthesis will be blocked by EAA availability. It is important to realize that amino acids, particularly the EAAs, are involved in several signaling pathways. These include but are not limited to the following: EAA and NEAAs are involved in activation of AKT. AKT increases protein synthesis and mTOR signaling pathways [29]. Interestingly, this is accomplished via an activation of AMPK [30] and phosphorylation of AKT, which in turn is regulated via the ER-IGF-I pathway [3]. Indeed, phosphorylation of AMPK is activated by amino acids, which is supported by the fact that protein synthesis of amino acids and amino acid oxidation were reduced during the protein starvation test in this group [31]. The AKT activation is necessary for phosphorylation of the mTOR/S6K1 pathway. Maintaining an elevated level of MMPs leads to increased protein synthesis when protein synthesis was blocked in the earlier studies [31–35] but is not necessary for protein synthesis when protein synthesis is stimulated. EAA and NEAAs are involved in regulation of protein degradation and protein catabolism. These pathways are mediated by the eukaryotic initiation factor 2 (eIF2α/eIF2β). EAT and eIF2α are involved in protein catabolism and degradation (eNF2), but are also important in regulation of protein synthesis. eIF2α and eIF2β also are involved in regulation of mTOR and phosphorylation of mTOR through eIF2R [36–38]. Interestingly, the role of eIF2α has been shown to be associated with increased protein synthesis in skeletal muscle [37–39]. EAAs and NEAs are involved in the EBP which is responsible for protein uptake and degradation of muscle proteins [40–42]. However, the EBP does not directly target muscle proteins. EBP directly targets specific EAA, NEAAs, or both. Consequently, EAA and NEAAs also are involved in regulation of regulation of protein turnover. One of the most widely studied examples is mTOR regulation, since a large portion of the EAA content of muscle proteins directly targets mTOR/S6K1/ERK [43–45]. Because there is no Similar articles:

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