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This Article Full Text Full Text (PDF) All Versions of this Article: 297/3/E749    most recent 00130.2009v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Ljubicic, V. Articles by Hood, D. A. PubMed PubMed Citation Articles by Ljubicic, V. Articles by Hood, D. A.

Specific attenuation of protein kinase phosphorylation in muscle with a high mitochondrial content

School of Kinesiology and Health Science, Muscle Health Research Centre, York University, Toronto, Ontario, Canada

Submitted 26 February 2009 ; accepted in final form 17 June 2009

Acute contractile activity increases the activation of protein kinases involved in signal transduction. We hypothesized that the contractile activity-induced kinase phosphorylation would occur to a lesser degree in muscle with elevated mitochondrial content. We compared red and white sections of tibialis anterior (TA) muscle with two- to threefold differences in mitochondrial volume, and we increased the mitochondrial content in the TA muscle by 40% with unilateral chronic stimulation-induced contractile activity (10 Hz, 7 days, 3 h/day). Both the chronically stimulated and the contralateral control muscles were then acutely stimulated in situ for 15 min (10 Hz). We investigated 1) the total protein content and 2) the phosphorylation of kinases important for mitochondrial biogenesis in skeletal muscle, including AMPK and p44, p42, and p38 MAPKs, as well as Akt by immunoblotting. In response to chronic stimulation, a selective upregulation of kinase protein content was observed, suggesting unique transcriptional/translational processing for these enzymes. Inverse relationships were observed between mitochondrial volume and 1) kinase protein content and 2) basal levels of kinase phosphorylation. In general, the kinase phosphorylation response to acute exercise depended, in part, on the oxidative capacity of the fiber type, evidenced by a greater absolute level of acute contractile activity-induced kinase signaling in muscle with a lower mitochondrial volume. The attenuation of contraction-evoked kinase phosphorylation in muscle with high mitochondrial content suggests that these proteins may become less sensitive to upstream signaling and require greater stimulation for activation to propagate these adaptive cues downstream toward transcription or translation events.

exercise signaling; fiber type; adenosine 5'-monophosphate-activated protein kinase; p38 mitogen-activated protein kinase