AMPK activation attenuates S6K1, 4E-BP1, and eEF2 signaling responses to high-frequency electrically stimulated skeletal muscle contractions

Thomson, David M.; Fick, Christopher A.; Gordon, Scott E.

doi:10.1152/japplphysiol.00915.2007

Cited by 153Metabolism, Diabetes, and CancerMuscle metabolism and nutritionMuscle Physiology and Disorders

AMPK activation attenuates S6K1, 4E-BP1, and eEF2 signaling responses to high-frequency electrically stimulated skeletal muscle contractions

Thomson, David M., Fick, Christopher A., Gordon, Scott E.·2008·Journal of Applied Physiology

DOI 10.1152/japplphysiol.00915.2007

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Abstract

Regulation of protein translation through Akt and the downstream mammalian target of rapamycin (mTOR) pathway is an important component of the cellular response to hypertrophic stimuli. It has been proposed that 5′-AMP-activated protein kinase (AMPK) activation during muscle contraction may limit the hypertrophic response to resistance-type exercise by inhibiting translational signaling. However, experimental manipulation of AMPK activity during such a stimulus has not been attempted. Therefore, we investigated whether AMPK activation can attenuate the downstream signaling response of the Akt/mTOR pathway to electrically stimulated lengthening muscle contractions. Extensor digitorum longus muscles ( n = 8/group) were subjected to a 22-min bout of lengthening contractions by high-frequency sciatic nerve electrical stimulation (STIM) in young adult (8 mo) Fischer 344 × Brown Norway male rats. Forty minutes before electrical stimulation, rats were subcutaneously injected with saline or 5-aminoimidazole-4-carboxamide-1–4-ribofuranoside (AICAR; 1 mg/g body wt), an AMPK activator. Stimulated and contralateral resting muscles were removed at 0, 20, and 40 min post-STIM, and AMPK, acetyl CoA carboxylase (ACC), Akt, eukaryotic initiation factor 4E-binding protein (4E-BP1), 70-kDa ribosomal protein S6 kinase (S6K1), and eukaryotic elongation factor 2 (eEF2) phosphorylations were assessed by Western blot. AICAR treatment increased ( P ≤ 0.05) post-STIM AMPK (Thr 172) and ACC phosphorylation (Ser 79/221), inhibited post-STIM S6K1 (Thr 389) and 4E-BP1 (gel shift) phosphorylation, and elevated post-STIM eEF2 phosphorylation (Thr 56). These findings suggest that translational signaling downstream of Akt/mTOR can be inhibited after lengthening contractions when preceded by AMPK activation and that energetic stress may be antagonistic to the hypertrophic translational signaling response to loaded muscle contractions.

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AICAR treatment blocked S6K phosphorylation.
“They went further using the AMP mimetic AICAR (5-aminoimidazole-4-carboxamide ribonucleotide) to activate AMPK in muscles before resistance exercise and, consistent with the hypothesis, AICAR treatment blocked S6K phosphorylation [47].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [47]
Studies in cell culture and animal models provide compelling evidence for cross-talk between AMPK and mTOR signaling pathways, and support the notion that activation of AMPK-related pathways suppresses translation through decreased S6K and 4E-BP phosphorylation.
“Studies in cell culture and animal models provide compelling evidence for the cross-talk between AMPK and mTOR signaling pathways, and support the notion that activation of AMPK-related pathways suppresses translation through decreased S6K and 4E-BP phosphorylation (Bolster et al., 2002;Thomson et al., 2008;Lantier et al., 2010;Egawa et al., 2014).”
From Concurrent exercise training: do opposites distract? (2017) · cites this paper as Thomson et al., 2008

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“They went further using the AMP mimetic AICAR (5-aminoimidazole-4-carboxamide ribonucleotide) to activate AMPK in muscles before resistance exercise and, consistent with the hypothesis, AICAR treatment blocked S6K phosphorylation [47].”
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AICAR suppresses p70S6k and eEF2 signaling after eccentric resistance exercise
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Authors: Thomson, D. M., Fick, C. A., & Gordon, S. E.
Affiliations: East Carolina University (US)
ORCID: Thomson, David M.
Venue: Journal of Applied Physiology
Publisher: American Physiological Society
Published: 2008-03
Volume: 104
Issue: 3
Pages: 625-632
ISSN: 0161-7567 (ISSN-L)
8750-7587
1522-1601
DOI: 10.1152/japplphysiol.00915.2007
OpenAlex: W2168947306
Cited by: 153
References: 58
Citations by year: 2026: 1 · 2025: 10 · 2024: 5 · 2023: 4 · 2022: 2 · 2021: 6 · 2020: 7 · 2019: 7 · 2018: 7 · 2017: 8 · 2016: 7 · 2015: 15 · 2014: 13 · 2013: 14 · 2012: 6
FWCI: 5.60
Type: journal article
Language: en
Open access: closed
Locations: Journal of Applied Physiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (1r15ag025101-01a1)
National Institute on Aging (AG025101)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
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
Keywords: AMPK activation, AICAR, S6K1, 4E-BP1, elongation factor 2, Akt/mTOR signaling, mRNA translation, skeletal muscle hypertrophy, eccentric contraction, electrical stimulation, extensor digitorum longus, acetyl-CoA carboxylase, energy stress, resistance training
MeSH terms: Acetyl-CoA Carboxylase, Aminoimidazole Carboxamide, Animals, Carrier Proteins, Electric Stimulation, Enzyme Activation, Hypertrophy, Injections, Subcutaneous, Male, Multienzyme Complexes, Muscle Contraction, Phosphoproteins, Phosphorylation, Protein Kinases, Rats, Inbred BN, Rats, Inbred F344, Ribonucleotides, Sciatic Nerve, Time Factors, Protein Biosynthesis, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Ribosomal Protein S6 Kinases, Enzyme Activators, Peptide Elongation Factor 2, Intracellular Signaling Peptides and Proteins, Proto-Oncogene Proteins c-akt, Rats, AMP-Activated Protein Kinases, TOR Serine-Threonine Kinases

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AMPK activation attenuates S6K1, 4E-BP1, and eEF2 signaling responses to high-frequency electrically stimulated skeletal muscle contractions

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