The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Influence of muscle glycogen availability on ERK1/2 and Akt signaling after resistance exercise in human skeletal muscle
Abstract
Two pathways that have been implicated for cellular growth and development in response to muscle contraction are the extracellular signal-regulated kinase (ERK1/2) and Akt signaling pathways. Although these pathways are readily stimulated after exercise, little is known about how nutritional status may affect stimulation of these pathways in response to resistance exercise in human skeletal muscle. To investigate this, experienced cyclists performed 30 repetitions of knee extension exercise at 70% of one repetition maximum after a low (2%) or high (77%) carbohydrate (LCHO or HCHO) diet, which resulted in low or high (approximately 174 or approximately 591 mmol/kg dry wt) preexercise muscle glycogen content. Muscle biopsies were taken from the vastus lateralis before, approximately 20 s after, and 10 min after exercise. ERK1/2 and p90 ribosomal S6 kinase phosphorylation increased (P < or = 0.05) 10 min after exercise, regardless of muscle glycogen availability. Akt phosphorylation was elevated (P < 0.05) 10 min after exercise in the HCHO trial but was unaffected after exercise in the LCHO trial. Mammalian target of rapamycin phosphorylation was similar to that of Akt during each trial; however, change or lack of change was not significant. In conclusion, the ERK1/2 pathway appears to be unaffected by muscle glycogen content. However, muscle glycogen availability appears to contribute to regulation of the Akt pathway, which may influence cellular growth and adaptation in response to resistance exercise in a low-glycogen state.
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“Although the evidence is not unanimous, low levels of glycogen could inhibit the hypertrophic response to resistance training [18,19] and increase proteolysis [20,21].”
From Carbohydrate Availability and Physical Performance: Physiological Overview and Practical Recommendations (2019) · cites this paper as [19]
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Cites
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Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
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A comparison of three methods of glycogen measurement in tissues
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Transcriptional regulation of gene expression in human skeletal muscle during recovery from exercise
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The Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756
Wilson, J. M., Marin, P. J., Rhea, M. R., Wilson, S. M., Loenneke, J. P., & Anderson, J. C. (2012) · Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e31823a3e2d · Cited by 587
“Moreover, although resistance training increases myofibrillar protein synthesis for up to 72 hours after an intense training bout (12), moderate intensity endurance exercise immediately acts to inhibit important elongation factors (eef2) responsible for increasing protein synthesis and maintains this inhibition for th…”
BackgroundBurd, N. A., West, D. W. D., Staples, A. W., Atherton, P. J., Baker, J. M., Moore, D. R., Holwerda, A. M., Parise, G., Rennie, M. J., Baker, S. K., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012033 · Cited by 531
“Indeed, many investigations have established that Akt is transiently phosphorylated following exercise [14,41,42,43] or even no change [12,44,45].”
BackgroundExercise, MAPK, and NF-κB signaling in skeletal muscle
Kramer, H. F., & Goodyear, L. J. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00085.2007 · Cited by 375
“The magnitude of ERK1/2 phosphorylation during exercise correlates with the intensity of the protocol (87), and both endurance and resistance exercise (16, 46, 88) can increase ERK1/2 phosphorylation.”
Fyfe, J. J., Bishop, D. J., & Stepto, N. K. (2014) · Sports Medicine · doi:10.1007/s40279-014-0162-1 · Cited by 347
“For example, the availability of muscle glycogen has been reported to modulate early molecular responses to both endurance and resistance exercise in a divergent manner [82, 84, 137].”
Influential
Metadata
- Authors
- Creer, A., Gallagher, P., Slivka, D., Jemiolo, B., Fink, W., & Trappe, S.
- Affiliations
- Ball State University (US)
- Venue
- Journal of Applied Physiology
- Publisher
- American Physiological Society
- Published
- 2005-09
- Volume
- 99
- Issue
- 3
- Pages
- 950-956
- ISSN
- 0161-7567 (ISSN-L)
- 8750-7587
- 1522-1601
- OpenAlex
- W2166195206
- Cited by
- 150
- References
- 47
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 2 · 2020: 2 · 2019: 8 · 2018: 3 · 2017: 7 · 2016: 6 · 2015: 7 · 2014: 18 · 2013: 10 · 2012: 9
- FWCI
- 3.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Applied Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG 18409, R01AG018409)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- muscle glycogen, resistance training, ERK signaling, Akt signaling, p90 ribosomal S6 kinase, mTOR, skeletal muscle, dietary carbohydrates, muscle hypertrophy, vastus lateralis, exercise adaptation
- MeSH terms
- Adult, Dietary Carbohydrates, Glycogen, Humans, Knee Joint, Male, Muscle Contraction, Physical Endurance, Proto-Oncogene Proteins, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Proto-Oncogene Proteins c-akt
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