Contraction intensity and feeding affect collagen and myofibrillar protein synthesis rates differently in human skeletal muscle

Holm, Lars; van Hall, Gerrit; Rose, Adam J.; Miller, Benjamin F.; Doessing, Simon; Richter, Erik A.; Kjaer, Michael

doi:10.1152/ajpendo.00609.2009

Cited by 132Muscle metabolism and nutritionMuscle Physiology and DisordersCardiovascular and exercise physiology

Contraction intensity and feeding affect collagen and myofibrillar protein synthesis rates differently in human skeletal muscle

Holm, Lars, van Hall, Gerrit, Rose, Adam J., Miller, Benjamin F., Doessing, Simon, Richter, Erik A., Kjaer, Michael·2010·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00609.2009

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Abstract

Exercise stimulates muscle protein fractional synthesis rate (FSR), but the importance of contractile intensity and whether it interplays with feeding is not understood. This was investigated following two distinct resistance exercise (RE) contraction intensities using an intrasubject design in the fasted ( n = 10) and fed ( n = 10) states. RE consisted of 10 sets of knee extensions. One leg worked against light load (LL) at 16% of one-repetition maximum (1RM), the other leg against heavy load (HL) at 70% 1RM, with intensities equalized for total lifted load. Males were infused with [13 C]leucine, and vastus lateralis biopsies were obtained bilaterally at rest as well as 0.5, 3, and 5.5 h after RE. Western blots were run on muscle lysates and phosphospecific antibodies used to detect phosphorylation status of targets involved in regulation of FSR. The intramuscular collagen FSR was evenly increased following LL- and HL-RE and was not affected by feeding. Myofibrillar FSR was unaffected by LL-RE, whereas HL-RE resulted in a delayed improvement (0.14 ± 0.02%/h, P < 0.05). Myofibrillar FSR was increased at rest by feeding ( P < 0.05) and remained elevated late in the postexercise period compared with the fasting condition. The Rp-s6k-4E-binding protein-1 (BP1) and the mitogen-activated protein kinase (MAPk) pathways were activated by the HL intensity and were suggested to be responsible for regulating myofibrillar FSR in response to adequate contractile activity. Feeding predominantly affected Rp-s6k and eukaryotic elongation factor 2 phosphorylations in correspondence with the observed changes in myofibrillar FSR, whereas 4E-BP1 remained to respond only to the HL contraction intensity. Thus the study design allows us to conclude that the MAPk- and mammalian target of rapamycin-dependent signaling responds to contractile activity, whereas elongation mainly was found to respond to feeding. Furthermore, although functionally linked, the contractile and the supportive matrix structures upregulate their protein synthesis rate quite differently in response to feeding and contractile activity and intensity.

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Some studies show an impaired acute muscle protein synthetic response when training with lower loads, while others report similar increases in mixed and myofibrillar protein synthesis rates.
“Some studies show an impaired acute MPS response when training with lower loads [37,38] while others report similar increases in mixed and myofibrillar protein synthesis rates [39].”
From Loading recommendations for muscle strength, hypertrophy, and local endurance: a re-examination of the repetition continuum. (2021) · cites this paper as [38]
Studies showing an impairment in the anabolic response with light loads employed work-matched protocols whereby participants stopped the low-load sets well short of fatigue.
“Specifically, studies showing an impairment in the anabolic response with light loads employed work-matched protocols whereby participants stopped the low-load sets well short of fatigue [37,38].”
From Loading recommendations for muscle strength, hypertrophy, and local endurance: a re-examination of the repetition continuum. (2021) · cites this paper as [38]

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Authors: Holm, L., van Hall, G., Rose, A. J., Miller, B. F., Doessing, S., Richter, E. A., & Kjaer, M.
Affiliations: University of Copenhagen (DK)
Department of Biomedical Sciences, Faculty of Health Sciences, and
Bispebjerg Hospital (DK)
Institute of Sports Medicine, Bispebjerg Hospital and Center of Healthy Aging,
Corresponding author: Holm, Lars
ORCID: Holm, Lars
Rose, Adam J.
Miller, Benjamin F.
Richter, Erik A.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2010-02
Volume: 298
Issue: 2
Pages: E257-E269
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00609.2009
OpenAlex: W2120048383
Cited by: 132
References: 19
Citations by year: 2026: 4 · 2025: 4 · 2024: 9 · 2023: 4 · 2022: 6 · 2021: 9 · 2020: 7 · 2019: 12 · 2018: 6 · 2017: 5 · 2016: 11 · 2015: 5 · 2014: 7 · 2013: 13 · 2012: 14
FWCI: 4.15
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Complementary and alternative medicine › Cardiovascular and exercise physiology
Keywords: resistance training, contraction intensity, feeding, muscle protein synthesis, collagen synthesis, myofibrillar protein synthesis, vastus lateralis, mTOR signaling, MAPK signaling, 4E-BP1, eEF2 phosphorylation, post-exercise recovery, knee extension
MeSH terms: Adult, Collagen, Physical Exertion, Fasting, Humans, Male, Muscle Contraction, Myofibrils, Reference Values, Protein Biosynthesis, Second Messenger Systems, Muscle, Skeletal, Young Adult

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Contraction intensity and feeding affect collagen and myofibrillar protein synthesis rates differently in human skeletal muscle

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