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Cited by 427Cardiovascular and exercise physiologyExercise and Physiological ResponsesMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.

Brief intense interval exercise activates AMPK and p38 MAPK signaling and increases the expression of PGC-1α in human skeletal muscle

Gibala, Martin J., McGee, Sean L., Garnham, Andrew P., Howlett, Kirsten F., Snow, Rodney J., Hargreaves, Mark·2009·Journal of Applied Physiology
DOI 10.1152/japplphysiol.90880.2008
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Abstract

From a cell signaling perspective, short-duration intense muscular work is typically associated with resistance training and linked to pathways that stimulate growth. However, brief repeated sessions of sprint or high-intensity interval exercise induce rapid phenotypic changes that resemble traditional endurance training. We tested the hypothesis that an acute session of intense intermittent cycle exercise would activate signaling cascades linked to mitochondrial biogenesis in human skeletal muscle. Biopsies (vastus lateralis) were obtained from six young men who performed four 30-s “all out” exercise bouts interspersed with 4 min of rest (<80 kJ total work). Phosphorylation of AMP-activated protein kinase (AMPK; subunits α1 and α2) and the p38 mitogen-activated protein kinase (MAPK) was higher ( P ≤ 0.05) immediately after bout 4 vs. preexercise. Peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) mRNA was increased approximately twofold above rest after 3 h of recovery ( P ≤ 0.05); however, PGC-1α protein content was unchanged. In contrast, phosphorylation of protein kinase B/Akt (Thr308 and Ser473) tended to decrease, and downstream targets linked to hypertrophy (p70 ribosomal S6 kinase and 4E binding protein 1) were unchanged after exercise and recovery. We conclude that signaling through AMPK and p38 MAPK to PGC-1α may explain in part the metabolic remodeling induced by low-volume intense interval exercise, including mitochondrial biogenesis and an increased capacity for glucose and fatty acid oxidation.

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Crossref · 10.1152/japplphysiol.90880.2008

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Metadata

Authors
Gibala, M. J., McGee, S. L., Garnham, A. P., Howlett, K. F., Snow, R. J., & Hargreaves, M.
Affiliations
McMaster University (CA)
ORCID
Venue
Journal of Applied Physiology
Publisher
American Physiological Society
Published
2009-03
Volume
106
Issue
3
Pages
929-934
ISSN
  • 0161-7567 (ISSN-L)
  • 8750-7587
  • 1522-1601
DOI
10.1152/japplphysiol.90880.2008
OpenAlex
W2163772556
Cited by
427
References
37
Citations by year
2026: 15 · 2025: 30 · 2024: 22 · 2023: 19 · 2022: 21 · 2021: 23 · 2020: 17 · 2019: 21 · 2018: 23 · 2017: 29 · 2016: 31 · 2015: 33 · 2014: 30 · 2013: 25 · 2012: 25
FWCI
61.49
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Applied Physiology (publishedVersion)
  • PubMed (publishedVersion)
  • Victoria University Research Repository (Victoria University) (submittedVersion)
Topics
  • Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
  • Health Sciences › Medicine › Physiology (medical) › Exercise and Physiological Responses
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords
high-intensity interval exercise, AMPK, p38 MAPK, PGC-1α, mitochondrial biogenesis, skeletal muscle, acute exercise, Akt signaling, vastus lateralis
MeSH terms
Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Bicycling, Heat-Shock Proteins, Humans, Male, Phosphorylation, Transcription Factors, Exercise, Gene Expression, Muscle, Skeletal, MAP Kinase Signaling System, p38 Mitogen-Activated Protein Kinases, Proto-Oncogene Proteins c-akt, AMP-Activated Protein Kinases, Young Adult

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