Abstract
Exercise dynamically changes skeletal muscle protein synthesis to respond and adapt to the external and internal stimuli. Many studies have focused on overall protein synthesis to understand how exercise regulates the muscular adaptation. However, despite the probability that each gene transcript may have its own unique translational characteristics and would be differentially regulated at translational level, little attention has been paid to how exercise affects translational regulation of individual genes at a genome-wide scale. Here, we conducted a genome-wide translational analysis using ribosome profiling to investigate the effect of a single bout of treadmill running (20 m/min for 60 min) on mouse gastrocnemius. Global translational profiles largely differed from those in transcription even at a basal resting condition as well as immediately after exercise. As for individual gene, Slc25a25 (Solute carrier family 25, member 25), localized in mitochondrial inner membrane and maintaining ATP homeostasis and endurance performance, showed significant up-regulation at translational level. However, multiple regression analysis suggests that Slc25a25 protein degradation may also have a role in mediating Slc25a25 protein abundance in the basal and early stages after acute endurance exercise.
Highlights
The regulation and dynamics of protein synthesis and amino acid metabolism have been intensively investigated to understand the underlying mechanisms of muscle adaptation to exercise
5 ́ end of aligned ribosome-protected fragments (RPF) results in uneven distribution, in which the strongest peak at a coding frame indicates the main coding frame [12,20]. This striking feature was only present in ribosome profiling but not in mRNA-Seq
It is known that when harvesting cells without flash-freezing or no translational inhibitor, the RPF peak near start codon disappears due to the failure of successful stall of ribosomes [12]
Summary
The regulation and dynamics of protein synthesis and amino acid metabolism have been intensively investigated to understand the underlying mechanisms of muscle adaptation to exercise. The use of stable isotope tracers, for example, has advanced our understanding of the regulation of overall muscular metabolism of amino acids and protein synthesis [1,2,3,4]. It has been known that during acute endurance exercise global muscular protein synthesis decreases in human and rodents [5,6]. Despite the intensive studies of global protein synthesis, some individual synthesis rates of proteins, and related signaling cascades [9,10], few studies have focused on the skeletal muscle protein synthesis or translational regulation of individual.
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