Increased p70s6k phosphorylation during intake of a protein–carbohydrate drink following resistance exercise in the fasted state

Louise Deldicque, Katrien De Bock, Michael Maris, Monique Ramaekers, Henri Nielens, Marc Francaux, Peter Hespel

The present study aimed at comparing the responses of myogenic regulatory factors and signaling pathways involved in muscle protein synthesis after a resistance training session performed in either the fasted or fed state. According to a randomized crossover study design, six young male subjects participated in two experimental sessions separated by 3 weeks. In each session, they performed a standardized resistance training. After the sessions, they received during a 4-h recovery period 6 ml/kg b.w. h of a solution containing carbohydrates (50 g/l), protein hydrolysate (33 g/l), and leucine (16.6 g/l). On one occasion, the resistance exercise session was performed after the intake of a carbohydrate-rich breakfast (B), whereas in the other session they remained fasted (F). Needle biopsies from m. vastus lateralis were obtained before (Rest), and 1 h (+1h) and 4 h (+4h) after exercise. Myogenin, MRF4, and MyoD1 mRNA contents were determined by RT-PCR. Phosphorylation of PKB (protein kinase B), GSK3, p70(s6k) (p70 ribosomal S6 kinase), eIF2B, eEF2 (eukaryotic elongation factor 2), ERK1/2, and p38 was measured via western blotting. Compared with F, the pre-exercise phosphorylation states of PKB and p70(s6k) were higher in B, whereas those of eIF2B and eEF2 were lower. During recovery, the phosphorylation state of p70(s6k) was lower in B than in F (p = 0.02). There were no differences in basal mRNA contents between B and F. However, compared with F at +1h, MyoD1 and MRF4 mRNA contents were lower in B (p < 0.05). Our results indicate that prior fasting may stimulate the intramyocellular anabolic response to ingestion of a carbohydrate/protein/leucine mixture following a heavy resistance training session.