title: The effect of feeding during recovery from aerobic exercise on skeletal muscle intracellular signaling.
abstract: We previously reported an increase in skeletal muscle protein synthesis during fasted and fed recovery from nonexhaustive aerobic exercise (Harber et al., 2010). The current study examined skeletal muscle intracellular signaling in the same subjects to further investigate mechanisms of skeletal muscle protein metabolism with and without feeding following aerobic exercise. Eight males (VO₂peak: 52 ± 2 ml⁻¹·kg⁻¹·min⁻¹) performed 60-min of cycle ergometry at 72 ± 1% VO₂peak on two occasions in a counter-balanced design. Exercise trials differed only in the postexercise nutritional intervention: EX-FED (5 kcal, 0.83 g carbohydrate, 0.37 g protein, 0.03 g fat per kg body weight) and EX-FAST (noncaloric, isovolumic placebo) ingested immediately and one hour after exercise. Muscle biopsies were obtained from the vastus lateralis at rest (on a separate day) and two hours postexercise to assess intracellular signaling via western blotting of p70S6K1, eEF2, 4EBP1, AMPKα and p38 MAPK. p70S6K1 phosphorylation was elevated (p < .05) in EX-FED relative to REST and EX-FAST. eEF2, 4EBP1, AMPKα and p38 MAPK signaling were unaltered at 2 h after exercise independent of feeding status when expressed as the ratio of phosphorylated to total protein normalized to actin. These data demonstrate that feeding after a nonexhaustive bout of aerobic exercise stimulates skeletal muscle p70S6K1 intracellular signaling favorable for promoting protein synthesis which may, as recent literature has suggested, better prepare the muscle for subsequent exercise bouts. These data provide further support into the role of feeding on mechanisms regulating muscle protein metabolism during recovery from aerobic exercise.
authors: Human Performance Laboratory, Ball State University, Muncie IN.
authors: Paul T
authors: PT
authors: Reidy
authors: Adam R
authors: AR
authors: Konopka
authors: J Matthew
authors: JM
authors: Hinkley
authors: Miranda K
authors: MK
authors: Undem
authors: Matthew P
authors: MP
authors: Harber
mesh_terms: D055372:AMP-Activated Protein Kinases / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000328:Adult; D001642:Bicycling / Q000502:physiology; D001706:Biopsy; D004435:Eating; D002149:Energy Intake / Q000502:physiology*; D015444:Exercise / Q000502:physiology*; D005215:Fasting / Q000502:physiology*; D006801:Humans; D008297:Male; D009124:Muscle Proteins / Q000378:metabolism*; D020652:Peptide Elongation Factor 2 / Q000378:metabolism; D010766:Phosphorylation; D052097:Quadriceps Muscle / Q000378:metabolism / Q000502:physiology*; D016601:RNA-Binding Proteins / Q000378:metabolism; D012146:Rest / Q000502:physiology*; D038762:Ribosomal Protein S6 Kinases, 70-kDa / Q000378:metabolism; D015398:Signal Transduction; D055815:Young Adult; D048051:p38 Mitogen-Activated Protein Kinases / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D009124:Muscle Proteins; C101633:PA2G4 protein, human; D020652:Peptide Elongation Factor 2; D016601:RNA-Binding Proteins; D038762:Ribosomal Protein S6 Kinases, 70-kDa; D048051:p38 Mitogen-Activated Protein Kinases; D055372:AMP-Activated Protein Kinases; C526180:PRKAA1 protein, human