European Journal of Applied Physiology

, Volume 111, Issue 7, pp 1297–1305 | Cite as

Training in the fasted state facilitates re-activation of eEF2 activity during recovery from endurance exercise

  • K. Van Proeyen
  • K. De Bock
  • P. HespelEmail author
Original Article


Nutrition is an important co-factor in exercise-induced training adaptations in muscle. We compared the effect of 6 weeks endurance training (3 days/week, 1–2 h at 75% VO2peak) in either the fasted state (F; n = 10) or in the high carbohydrate state (CHO, n = 10), on Ca2+-dependent intramyocellular signalling in young male volunteers. Subjects in CHO received a carbohydrate-rich breakfast before each training session, as well as ingested carbohydrates during exercise. Before (pretest) and after (posttest) the training period, subjects performed a 2 h constant-load exercise bout (~70% of pretest VO2peak) while ingesting carbohydrates (1 g/kg h−1). A muscle biopsy was taken from m. vastus lateralis immediately before and after the test, and after 4 h of recovery. Compared with pretest, in the posttest basal eukaryotic elongation factor 2 (eEF2) phosphorylation was elevated in CHO (P < 0.05), but not in F. In the pretest, exercise increased the degree of eEF2 phosphorylation about twofold (P < 0.05), and values returned to baseline within the 4 h recovery period in each group. However, in the posttest dephosphorylation of eEF2 was negated after recovery in CHO, but not in F. Independent of the dietary condition training enhanced the basal phosphorylation status of Phospholamban at Thr17, 5′-AMP-activated protein kinase α (AMPKα), and Acetyl CoA carboxylase β (ACCβ), and abolished the exercise-induced increase of AMPKα and ACCβ (P < 0.05). In conclusion, training in the fasted state, compared with identical training with ample carbohydrate intake, facilitates post-exercise dephosphorylation of eEF2. This may contribute to rapid re-activation of muscle protein translation following endurance exercise.


Nutritional status Metabolic adaptations AMP-activated protein kinase Ca2+-calmodulin-dependent protein kinase Eukarotic elongation factor 2 



The authors thank Erik A. Richter and Adam J. Rose, Copenhagen Muscle Research Centre, Institute of Exercise and Sports Sciences, University of Copenhagen, Copenhagen, Denmark Research Centre, for researching data. Monique Ramaekers, Research Centre for Exercise and Health, Department of Biomedical Kinesiology, K.U. Leuven, is also greatly acknowledged for all efforts she has put in this study. This study was supported by grant OT/05/53 from the Katholieke Universiteit Leuven and grant G.0233.05 F from the Fund for Scientific Research-Flanders, Belgium (F.W.O.-Vlaanderen).

Conflict of interest

There is no conflict of interest.


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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  1. 1.Department of Biomedical Kinesiology, Research Centre for Exercise and HealthFaBeR-K.U. LeuvenLeuven, HeverleeBelgium

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