Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis

Bergeron, Raynald; Ren, Jian Ming; Cadman, Kevin S.; Moore, Irene K.; Perret, Pascale; Pypaert, Marc; Young, Lawrence H.; Semenkovich, Clay F.; Shulman, Gerald I.

doi:10.1152/ajpendo.2001.281.6.e1340

Cited by 561Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismMitochondrial Function and Pathology

Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis

Bergeron, Raynald, Ren, Jian Ming, Cadman, Kevin S., Moore, Irene K., Perret, Pascale, Pypaert, Marc, Young, Lawrence H., Semenkovich, Clay F. +1 more·2001·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.2001.281.6.e1340

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Abstract

The underlying mechanism by which skeletal muscle adapts to exercise training or chronic energy deprivation is largely unknown. To examine this question, rats were fed for 9 wk either with or without β-guanadinopropionic acid (β-GPA; 1% enriched diet), a creatine analog that is known to induce muscle adaptations similar to those induced by exercise training. Muscle phosphocreatine, ATP, and ATP/AMP ratios were all markedly decreased and led to the activation of AMP-activated protein kinase (AMPK) in the β-GPA-fed rats compared with control rats. Under these conditions, nuclear respiratory factor-1 (NRF-1) binding activity, measured using a cDNA probe containing a sequence encoding for the promoter of δ-aminolevulinate (ALA) synthase, was increased by about eightfold in the muscle of β-GPA-fed rats compared with the control group. Concomitantly, muscle ALA synthase mRNA and cytochrome ccontent were also increased. Mitochondrial density in both extensor digitorum longus and epitrochlearis from β-GPA-fed rats was also increased by more than twofold compared with the control group. In conclusion, chronic phosphocreatine depletion during β-GPA supplementation led to the activation of muscle AMPK that was associated with increased NRF-1 binding activity, increased cytochrome c content, and increased muscle mitochondrial density. Our data suggest that AMPK may play an important role in muscle adaptations to chronic energy stress and that it promotes mitochondrial biogenesis and expression of respiratory proteins through activation of NRF-1.

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Authors: Bergeron, R., Ren, J. M., Cadman, K. S., Moore, I. K., Perret, P., Pypaert, M., Young, L. H., Semenkovich, C. F., & Shulman, G. I.
Affiliations: Departments of Internal Medicine,
Bristol-Myers Squibb (United States) (US)
Cell Biology, and
Washington University in St. Louis (US)
Howard Hughes Medical Institute (US)
ORCID: Perret, Pascale
Young, Lawrence H.
Semenkovich, Clay F.
Shulman, Gerald I.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2001-12-01
Volume: 281
Issue: 6
Pages: E1340-E1346
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.2001.281.6.e1340
OpenAlex: W2184995059
Cited by: 561
References: 45
Citations by year: 2026: 5 · 2025: 20 · 2024: 12 · 2023: 19 · 2022: 22 · 2021: 21 · 2020: 23 · 2019: 14 · 2018: 14 · 2017: 26 · 2016: 20 · 2015: 32 · 2014: 34 · 2013: 29 · 2012: 30
FWCI: 5.70
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (R01HL063811, HL-63811)
National Institute of Diabetes and Digestive and Kidney Diseases (P30DK45735, R01-DK40936, R01DK040936, P30DK045735)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: AMPK, NRF1, mitochondrial biogenesis, skeletal muscle, phosphocreatine depletion, energy deprivation, training effects, delta-aminolevulinic acid synthase, cytochrome c, mitochondrial density, AMP/ATP ratio
MeSH terms: Adenylate Kinase, 5-Aminolevulinate Synthetase, Animals, Cell Nucleus, Cytochrome c Group, DNA-Binding Proteins, Energy Metabolism, Enzyme Activation, Male, Microscopy, Electron, Mitochondria, Muscle, RNA, Messenger, Blotting, Northern, Trans-Activators, Rats, Sprague-Dawley, Muscle, Skeletal, Nuclear Respiratory Factors, NF-E2-Related Factor 1, Nuclear Respiratory Factor 1, Rats

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Chronic activation of AMP kinase results in NRF-1 activation and mitochondrial biogenesis

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