+ 55 to 65 to 3615 to 8765; Fax: +55 to 65 to 3615 to 8005. E-mail address: nairhonda@terra.com.br (N. H. Kawashita).
AbstractCompared with the extensor longus digitorum (EDL) muscle of control rats (C), the EDL muscle of rats fed a low-protein, high-carbohydrate (LPHC) diet showed a 36% reduction in mass. Muscle mass is determined by the balance between protein synthesis and proteolysis; thus, the aim of this work was to evaluate the components involved in these processes. Compared with the muscle from C rats, the EDL muscle from LPHC diet-fed rats showed a reduction (34%) in the in vitro basal protein synthesis and a 22% reduction in the in vitro basal proteolysis suggesting that the reduction in the mass can be associated with a change in the rate of the two processes. Soon after euthanasia, in the EDL muscles of the rats fed the LPHC or C diet for 15 days, the activity of caspase-3 and of components of the ubiquitin-proteasome system (atrogin-1 content and chymotrypsin-like activity) were decreased. The phosphorylation of p70 S6K and 4E-BP1, proteins involved in protein synthesis, was also decreased. We observed an increase in the insulin-stimulated protein content of p-Akt. Thus, the higher insulin sensitivity in the EDL muscle of LPHC rats seemed to contribute to the lower proteolysis in LPHC rats. However, even with the higher insulin sensitivity, the reduction in p-E4-BP1 and p70
S6Kindicates a reduction in protein synthesis, showing that factors other than insulin can have a greater effect on the control of protein synthesis.