Meal feeding regulates S6K1 phosjjhorylation but not that of 4E-BP1 in rainbow trout (Oncorhynchus mykiss) muscle

摘要

The synthesis of skeletal muscle proteins is rapidly stimulated after oral intake of nutrients, through an acceleration of mKNA translation initiation (Yoshizawa et al, 1998). This activation involves the phosphorylation of two key intracellular kinases, i.e. p70 S6 kinase (S6K1) and the translational represser eukaryotic initiation factor 4E binding protein (4E-BP1), regulated by the mammalian target of rapamycin (mTOR) signalling pathway (Shah et al., 2000). The mechanisms by which meal feeding modulates this cellular pathway are beginning to be elucidated and increasing evidence points out a broad role for amino acids in this process (Kimball and Jefferson, 2006). However, the molecular mechanisms implicated are complex and little understood.