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Specific attenuation of protein kinase phosphorylation in muscle with a high mitochondrial content.
Am J Physiol Endocrinol Metab. 2009 Sep; 297(3):E749-58.AJ

Abstract

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 AMPKalpha 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.

Authors+Show Affiliations

School of Kinesiology and Health Science, Muscle Health Research Centre, York University, Toronto, ON M3J 1P3, Canada.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19549794

Citation

Ljubicic, Vladimir, and David A. Hood. "Specific Attenuation of Protein Kinase Phosphorylation in Muscle With a High Mitochondrial Content." American Journal of Physiology. Endocrinology and Metabolism, vol. 297, no. 3, 2009, pp. E749-58.
Ljubicic V, Hood DA. Specific attenuation of protein kinase phosphorylation in muscle with a high mitochondrial content. Am J Physiol Endocrinol Metab. 2009;297(3):E749-58.
Ljubicic, V., & Hood, D. A. (2009). Specific attenuation of protein kinase phosphorylation in muscle with a high mitochondrial content. American Journal of Physiology. Endocrinology and Metabolism, 297(3), E749-58. https://doi.org/10.1152/ajpendo.00130.2009
Ljubicic V, Hood DA. Specific Attenuation of Protein Kinase Phosphorylation in Muscle With a High Mitochondrial Content. Am J Physiol Endocrinol Metab. 2009;297(3):E749-58. PubMed PMID: 19549794.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Specific attenuation of protein kinase phosphorylation in muscle with a high mitochondrial content. AU - Ljubicic,Vladimir, AU - Hood,David A, Y1 - 2009/06/23/ PY - 2009/6/25/entrez PY - 2009/6/25/pubmed PY - 2009/10/1/medline SP - E749 EP - 58 JF - American journal of physiology. Endocrinology and metabolism JO - Am. J. Physiol. Endocrinol. Metab. VL - 297 IS - 3 N2 - 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 AMPKalpha 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. SN - 1522-1555 UR - https://www.unboundmedicine.com/medline/citation/19549794/Specific_attenuation_of_protein_kinase_phosphorylation_in_muscle_with_a_high_mitochondrial_content_ L2 - http://www.physiology.org/doi/full/10.1152/ajpendo.00130.2009?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -