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This Article Full Text Full Text (PDF) All Versions of this Article: 583/2/785    most recent jphysiol.2007.138529v1 Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rose, A. J. Articles by Richter, E. A. Search for Related Content PubMed PubMed Citation Articles by Rose, A. J. Articles by Richter, E. A. Related Collections Skeletal Muscle and Exercise

¹ Copenhagen Muscle Research Centre, Department of Exercise and Sport Sciences, Section of Human Physiology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark 2100

Here the hypothesis that skeletal muscle Ca²⁺–calmodulin-dependent kinase II (CaMKII) expression and signalling would be modified by endurance training was tested. Eight healthy, young men completed 3 weeks of one-legged endurance exercise training with muscle samples taken from both legs before training and 15 h after the last exercise bout. Along with an 40% increase in mitochondrial F₁-ATP synthase expression, there was an 1-fold increase in maximal CaMKII activity and CaMKII kinase isoform expression after training in the active leg only. Autonomous CaMKII activity and CaMKII autophosphorylation were increased to a similar extent. However, there was no change in -CaMKII anchoring protein expression with training. Nor was there any change in expression or Thr¹⁷ phosphorylation of the CaMKII substrate phospholamban with training. However, another CaMKII substrate, serum response factor (SRF), had an 60% higher phosphorylation at Ser¹⁰³ after training, with no change in SRF expression. There were positive correlations between the increases in CaMKII expression and SRF phosphorylation as well as F₁ATPase expression with training. After training, there was an increase in cyclic-AMP response element binding protein phosphorylation at Ser¹³³, but not expression, in muscle of both legs. Taken together, skeletal muscle CaMKII kinase isoform expression and SRF phosphorylation is higher with endurance-type exercise training, adaptations that are restricted to active muscle. This may contribute to greater Ca²⁺ mediated regulation during exercise and the altered muscle phenotype with training.

(Received 14 June 2007; accepted after revision 12 July 2007; first published online 12 July 2007)
Corresponding author A. J. Rose: Copenhagen Muscle Research Centre, Department of Exercise and Sport Sciences, Sect. of Human Physiology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark, 2100. Email: arose{at}ifi.ku.dk

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