Normal hypertrophy accompanied by phosphoryation and activation of AMP‐activated protein kinase α1 following overload in LKB1 knockout mice

McGee, Sean L.; Mustard, Kirsty J.; Hardie, D. Grahame; Baar, Keith

doi:10.1113/jphysiol.2007.143685

Cited by 105Metabolism, Diabetes, and CancerMuscle Physiology and DisordersMuscle metabolism and nutrition

Normal hypertrophy accompanied by phosphoryation and activation of AMP‐activated protein kinase α1 following overload in LKB1 knockout mice

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McGee, Sean L., Mustard, Kirsty J., Hardie, D. Grahame, Baar, Keith·2008·The Journal of Physiology

DOI 10.1113/jphysiol.2007.143685PMC PMC2327866

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Abstract

The activation of the AMP‐activated protein kinase (AMPK) and inhibition of the mammalian target of rapamycin complex 1 (mTORC1) is hypothesized to underlie the fact that muscle growth following resistance exercise is decreased by concurrent endurance exercise. To directly test this hypothesis, the capacity for muscle growth was determined in mice lacking the primary upstream kinase for AMPK in skeletal muscle, LKB1. Following either 1 or 4 weeks of overload, there was no difference in muscle growth between the wild type (wt) and LKB1−/− mice (1 week: wt, 38.8 ± 7.75%; LKB1−/−, 27.8 ± 12.98%; 4 week: wt, 75.8 ± 15.2%; LKB1−/−, 85.0 ± 22.6%). In spite of the fact that the LKB1 had been knocked out in skeletal muscle, the phosphorylation and activity of the α1 isoform of AMPK were markedly increased in both the wt and the LKB1−/− mice. To identify the upstream kinase(s) responsible, we studied potential upstream kinases other than LKB1. The activity of both Ca 2+–calmodulin‐dependent protein kinase kinase α(CaMKKα) (5.05 ± 0.86‐fold) and CaMKKβ (10.1 ± 2.59‐fold) increased in the overloaded muscles, and this correlated with their increased expression. Phosphorylation of TAK‐1 also increased 10‐fold following overload in both the wt and LKB1 mice. Even though the α1 isoform of AMPK was activated by overload, there were no increases in expression of mitochondrial proteins or GLUT4, indicating that the α1 isoform is not involved in these metabolic adaptations. The phosphorylation of TSC2, an upstream regulator of the TORC1 pathway, at the AMPK site (Ser1345) was increased in response to overload, and this was not affected by LKB1 deficiency. Taken together, these data suggest that the α1 isoform of AMPK is preferentially activated in skeletal muscle following overload in the absence of metabolic adaptations, suggesting that this isoform might be important in the regulation of growth but not metabolism.

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The isoform of AMPK activated by concurrent training (α1) was not the form associated with endurance adaptations (α2), suggesting that during concurrent training a different form of AMPK was activated to prevent growth.
“We then used an animal model of concurrent training to show that the isoform of AMPK that was activated by concurrent training (α1) was not the form that was associated with endurance adaptations (α2), suggesting that during concurrent training a different form of AMPK was activated to prevent growth [48].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [48]

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Untitled work
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Authors: McGee, S. L., Mustard, K. J., Hardie, D. G., & Baar, K.
Affiliations: The University of Melbourne (AU)
University of Dundee (GB)
ORCID: McGee, Sean L.
Hardie, D. Grahame
Baar, Keith
Venue: The Journal of Physiology
Publisher: Wiley
Published: 2008-03-15
Volume: 586
Issue: 6
Pages: 1731-1741
ISSN: 0022-3751 (ISSN-L)
1469-7793
DOI: 10.1113/jphysiol.2007.143685
PMC: PMC2327866
OpenAlex: W2104701019
Cited by: 105
References: 46
Citations by year: 2026: 2 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 2 · 2019: 3 · 2018: 6 · 2017: 10 · 2016: 4 · 2015: 6 · 2014: 6 · 2013: 15 · 2012: 7
FWCI: 5.35
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 2 d)
Locations: The Journal of Physiology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (publishedVersion)
Funders: Wellcome Trust (077426, 080982)
Topics: 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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords: AMPK, skeletal muscle hypertrophy, muscle overload, resistance training, endurance exercise, CaMKKβ, TAK1, TSC2 phosphorylation, mTORC1, muscle growth regulation, muscle metabolism
MeSH terms: AMP-Activated Protein Kinase Kinases, Animals, Hypertrophy, Phosphorylation, Physical Endurance, Protein Kinases, Protein Serine-Threonine Kinases, Mice, Knockout, Muscle, Skeletal, Muscle Fatigue, Mice, AMP-Activated Protein Kinases

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Normal hypertrophy accompanied by phosphoryation and activation of AMP‐activated protein kinase α1 following overload in LKB1 knockout mice

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