Exercise intensity-dependent regulation of peroxisome proliferator-activated receptor γ coactivator-1α mRNA abundance is associated with differential activation of upstream signalling kinases in human skeletal muscle: Exercise intensity and PGC-1α regulation
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Skeletal muscle contraction increases intracellular ATP turnover, calcium flux, and mechanical stress, initiating signal transduction pathways that modulate peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC-1alpha)-dependent transcriptional programmes. The purpose of this study was to determine if the intensity of exercise regulates PGC-1alpha expression in human skeletal muscle, coincident with activation of signalling cascades known to regulate PGC-1alpha transcription. Eight sedentary males expended 400 kcal (1674 kj) during a single bout of cycle ergometer exercise on two separate occasions at either 40% (LO) or 80% (HI) of . Skeletal muscle biopsies from the m. vastus lateralis were taken at rest and at +0, +3 and +19 h after exercise. Energy expenditure during exercise was similar between trials, but the high intensity bout was shorter in duration (LO, 69.9 +/- 4.0 min; HI, 36.0 +/- 2.2 min, P < 0.05) and had a higher rate of glycogen utilization (P < 0.05). PGC-1alpha mRNA abundance increased in an intensity-dependent manner +3 h after exercise (LO, 3.8-fold; HI, 10.2-fold, P < 0.05). AMP-activated protein kinase (AMPK) (2.8-fold, P < 0.05) and calcium/calmodulin-dependent protein kinase II (CaMKII) phosphorylation (84%, P < 0.05) increased immediately after HI but not LO. p38 mitogen-activated protein kinase (MAPK) phosphorylation increased after both trials (2.0-fold, P < 0.05), but phosphorylation of the downstream transcription factor, activating transcription factor-2 (ATF-2), increased only after HI (2.4-fold, P < 0.05). Cyclic-AMP response element binding protein (CREB) phosphorylation was elevated at +3 h after both trials (80%, P < 0.05) and class IIa histone deacetylase (HDAC) phosphorylation increased only after HI (2.0-fold, P < 0.05). In conclusion, exercise intensity regulates PGC-1alpha mRNA abundance in human skeletal muscle in response to a single bout of exercise. This effect is mediated by differential activation of multiple signalling pathways, with ATF-2 and HDAC phosphorylation proposed as key intensity-dependent mediators.
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High-intensity exercise activates both AMPK and PGC-1α to a greater extent than low-intensity exercise in skeletal muscle.
“High-intensity exercise activates both AMPK and peroxisome proliferator-activated receptor co-activator (PGC-1α) to a greater extent than low-intensity exercise in skeletal muscle”
From Effect of Exercise Training on Fat Loss—Energetic Perspectives and the Role of Improved Adipose Tissue Function and Body Fat Distribution (2021) · cites this paper as Egan et al., 2010
The Abstract reports greater AMPK phosphorylation after high- than low-intensity exercise and a larger increase in PGC-1α mRNA abundance (10.2-fold versus 3.8-fold). It does not establish greater activation of PGC-1α itself; the discussion says further work is needed to determine whether the mRNA difference produces divergent PGC-1α protein levels. (LLM, conf=0.88)
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Mitochondrial and performance adaptations to exercise training in mice lacking skeletal muscle LKB1
Tanner, C. B., Madsen, S. R., Hallowell, D. M., Goring, D. M. J., Moore, T. M., Hardman, S. E., Heninger, M. R., Atwood, D. R., & Thomson, D. M. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00227.2013 · Cited by 47 · see citing works
Kuang, J., McGinley, C., Lee, M. J.-C., Saner, N. J., Garnham, A., & Bishop, D. J. (2022) · PeerJ · doi:10.7717/peerj.12856 · Cited by 45 · see citing works
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Regular exercise prevents non-cognitive disturbances in a rat model of Alzheimer's disease
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Skeletal muscle signaling response to sprint exercise in men and women
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Postexercise High-Fat Feeding Suppresses p70S6K1 Activity in Human Skeletal Muscle
HAMMOND, K. M., IMPEY, S. G., CURRELL, K., MITCHELL, N., SHEPHERD, S. O., JEROMSON, S., HAWLEY, J. A., CLOSE, G. L., HAMILTON, L. D., SHARPLES, A. P., et al. (2016) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001009 · Cited by 30 · see citing works
- Authors
- Egan, B., Carson, B. P., Garcia-Roves, P. M., Chibalin, A. V., Sarsfield, F. M., Barron, N., McCaffrey, N., Moyna, N. M., Zierath, J. R., & O’Gorman, D. J.
- Affiliations
- Dublin City University (IE)
- Karolinska Institutet (SE)
- Corresponding author
- O’Gorman, Donal J.
- ORCID
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2010-05-14
- Volume
- 588
- Issue
- 10
- Pages
- 1779-1790
- ISSN
- 0022-3751 (ISSN-L)
- PMC
- PMC2887994
- OpenAlex
- W1585179940
- Cited by
- 373
- References
- 61
- Citations by year
- 2026: 23 · 2025: 16 · 2024: 24 · 2023: 17 · 2022: 27 · 2021: 31 · 2020: 19 · 2019: 26 · 2018: 23 · 2017: 28 · 2016: 26 · 2015: 32 · 2014: 21 · 2013: 25 · 2012: 19
- FWCI
- 12.98
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journal of Physiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Health Sciences › Medicine › Complementary and alternative medicine › Cardiovascular and exercise physiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- PGC-1α, exercise intensity, skeletal muscle, AMPK, CaMKII, p38 MAPK, CREB, ATF2, histone deacetylase, transcriptional regulation, cycle ergometry, vastus lateralis, gene expression, energy expenditure, glycogen utilization, post-exercise recovery
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Adult, Biopsy, Diet, Exercise Test, Gene Expression Regulation, Glycogen, Heat-Shock Proteins, Humans, Male, Muscle Proteins, Phosphorylation, RNA, Messenger, Transcription Factors, Signal Transduction, Exercise, Cyclic AMP Response Element-Binding Protein, Cyclic AMP-Dependent Protein Kinases, Muscle, Skeletal, p38 Mitogen-Activated Protein Kinases, Activating Transcription Factor 2, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Young Adult
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