Adaptation of rat fast‐twitch muscle to endurance activity is underpinned by changes to protein degradation as well as protein synthesis

Abstract

Muscle adaptations to exercise are underpinned by alterations to the abundance of
individual proteins, which may occur through a change either to the synthesis or
degradation of each protein. We used deuterium oxide (2H2O) labeling and chronic
low-frequency stimulation (CLFS) in vivo to investigate the synthesis, abundance,and degradation of individual proteins during exercise-induced muscle adaptation.
Independent groups of rats received CLFS (10 Hz, 24 h/d) and 2H2O for 0, 10, 20, or
30 days. The extensor digitorum longus (EDL) was isolated from stimulated (Stim)
and contralateral non-stimulated (Ctrl) legs. Proteomic analysis encompassed 38 my-
ofibrillar and 46 soluble proteins and the rates of change in abundance, synthesis, and
degradation were reported in absolute (ng/d) units. Overall, synthesis and degrada-
tion made equal contributions to the adaptation of the proteome, including instances
where a decrease in protein-specific degradation primarily accounted for the increase
in abundance of the protein.