Similar to Karlsson, our lab has observed increased rpS6 phosphor

Similar to Karlsson, our lab has observed increased rpS6 phosphorylation 45 minutes after cycling exercise after both placebo and carbohydrate-protein beverages, although rpS6 phosphorylation was significantly higher after carbohydrate-protein compared to the placebo beverage [47]. Our lab has also observed timing of rpS6 phosphorylation in rats that was highly correlated to insulin [15]. rpS6 phosphorylation was higher 30 minutes post exercise in GSK923295 mw animals given carbohydrate-protein post exercise compared to

fasted, exercised controls. Interestingly, rpS6 phosphorylation was significantly increased at 90 minutes in animals that did not receive supplementation. At both time points, insulin was elevated in the respective animal groups compared to exercised controls. In the current study, we would expect the higher insulin and mTOR phosphorylation at 60 minutes after Cereal to

result in higher rpS6 phosphorylation compared to Drink, but that did not occur, possibly due to the amount of see more supplementation provided or biopsy timing. The nearly identical increase in rpS6 phosphorylation for both Cereal and Drink suggest that these changes were due to exercise and independent of supplementation. www.selleckchem.com/products/nutlin-3a.html For translation initiation to occur, mTOR must increase phosphorylation of eukaryotic translation initiation factor 4E (eIF4E) binding protein 1 (4E-BP1), releasing eIF4E to bind to eIF4G, forming the eIF4F complex. Phosphorylation of eIF4E may be affected by phosphorylation of MAP kinase interacting serine/threonine kinase 1 and 2 (MNK1/MNK2) [52]. Ueda et al. [52] established that changes in p38 MAPK phosphorylation of MNK1 directly influenced the levels of eIF4E phosphorylation while ERK1/2 activates both MNK1 and MNK2, but primarily affects the basal level of 5-Fluoracil eIF4E phosphorylation. The role of phosphorylated eIF4E in protein synthesis is unclear; while some studies have concluded that

phosphorylation of eIF4E is necessary for translation [53] others have not [52, 54, 55]. We observed a slight, insignificant decrease in phosphorylation of eIF4E after both Drink and Cereal, with no difference between treatments (Figure 6). This lack of change in phosphorylation of eIF4E between treatments agrees with the findings of Gautsch et al. [31], who observed no change in post-exercised rats that consumed saline, carbohydrate or a mixed meal. In addition, there was no difference in phosphorylation of eIF4E between fasted-rested rats and all exercise groups, suggesting that exercise did not affect eIF4E phosphorylation. The form of our recovery foods did not seem to affect our results, although the rate of gastric emptying would be expected to be lower for solid food versus liquid food. Reed et al.

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