Hindlimb unloading and denervation in rats produced alterations in translation factors, with regulation differing between the models of atrophy and the specific muscles evaluated.
Hindlimb unloading and denervation in rats alter protein translation factors differently depending on the atrophy model and specific muscle evaluated.
In the rat, denervation and hindlimb unloading are two commonly employed models used to study skeletal muscle atrophy. In these models, muscle atrophy is generally produced by a decrease in protein synthesis and an increase in protein degradation. The decrease in protein synthesis has been suggested to occur by an inhibition at the level of protein translation. To better characterize the regulation of protein translation, we investigated the changes that occur in various translation initiation and elongation factors. We demonstrated that both hindlimb unloading and denervation produce alterations in the phosphorylation and/or total amount of the 70-kDa ribosomal S6 kinase, eukaryotic initiation factor 2 alpha-subunit, and eukaryotic elongation factor 2. Our findings indicate that the regulation of these protein translation factors differs between the models of atrophy studied and between the muscles evaluated (e.g., soleus vs. extensor digitorum longus).
Hornberger et al. (Sun,) conducted a other in Skeletal muscle atrophy. Hindlimb unloading and denervation was evaluated on Changes in translation initiation and elongation factors (70-kDa ribosomal S6 kinase, eIF2 alpha-subunit, and eEF2). Hindlimb unloading and denervation in rats produced alterations in translation factors, with regulation differing between the models of atrophy and the specific muscles evaluated.