The nuclear receptor PPARβ/δ programs muscle glucose metabolism in cooperation with AMPK and MEF2

Gan, Zhenji; Burkart-Hartman, Eileen M.; Han, Dong-Ho; Finck, Brian; Leone, Teresa C.; Smith, Emily Y.; Ayala, Julio E.; Holloszy, John; Kelly, Daniel P.

doi:10.1101/gad.178434.111

Cited by 139Peroxisome Proliferator-Activated ReceptorsMetabolism, Diabetes, and CancerAdipose Tissue and Metabolism

The nuclear receptor PPARβ/δ programs muscle glucose metabolism in cooperation with AMPK and MEF2

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Gan, Zhenji, Burkart-Hartman, Eileen M., Han, Dong-Ho, Finck, Brian, Leone, Teresa C., Smith, Emily Y., Ayala, Julio E., Holloszy, John +1 more·2011·Genes & Development

DOI 10.1101/gad.178434.111PMC PMC3248683

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Abstract

To identify new gene regulatory pathways controlling skeletal muscle energy metabolism, comparative studies were conducted on muscle-specific transgenic mouse lines expressing the nuclear receptors peroxisome proliferator-activated receptor α (PPARα; muscle creatine kinase [MCK]-PPARα) or PPARβ/δ (MCK-PPARβ/δ). MCK-PPARβ/δ mice are known to have enhanced exercise performance, whereas MCK-PPARα mice perform at low levels. Transcriptional profiling revealed that the lactate dehydrogenase b (Ldhb)/Ldha gene expression ratio is increased in MCK-PPARβ/δ muscle, an isoenzyme shift that diverts pyruvate into the mitochondrion for the final steps of glucose oxidation. PPARβ/δ gain- and loss-of-function studies in skeletal myotubes demonstrated that PPARβ/δ, but not PPARα, interacts with the exercise-inducible kinase AMP-activated protein kinase (AMPK) to synergistically activate Ldhb gene transcription by cooperating with myocyte enhancer factor 2A (MEF2A) in a PPARβ/δ ligand-independent manner. MCK-PPARβ/δ muscle was shown to have high glycogen stores, increased levels of GLUT4, and augmented capacity for mitochondrial pyruvate oxidation, suggesting a broad reprogramming of glucose utilization pathways. Lastly, exercise studies demonstrated that MCK-PPARβ/δ mice persistently oxidized glucose compared with nontransgenic controls, while exhibiting supranormal performance. These results identify a transcriptional regulatory mechanism that increases capacity for muscle glucose utilization in a pattern that resembles the effects of exercise training.

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PPARβ activation results in an increase in lipid oxidation and glucose metabolism and improves insulin sensitivity via PGC-1α.
“PPARβ activation results in an increase in lipid oxidation and glucose metabolism, as previously reported (45), and improves insulin sensitivity via PGC-1α (46).”
From TFAM Enhances Fat Oxidation and Attenuates High-Fat Diet–Induced Insulin Resistance in Skeletal Muscle (2019) · cites this paper as [45]
PPARβ mediates glucose uptake and glycolysis.
“PPARβ and PGC-1α increased the use of FA by PDK4 (pyruvate dehydrogenase kinase 4) (49,50), and PPARβ also is reported to mediate glucose uptake and glycolysis (45); thus, TFAM overexpression in muscle results in an increase in β-oxidation as well as glycolysis, as noted by increased lactate levels (Fig. 2).”
From TFAM Enhances Fat Oxidation and Attenuates High-Fat Diet–Induced Insulin Resistance in Skeletal Muscle (2019) · cites this paper as [45]

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지구성 운동에 의한 AMPK 활성은 MEF2A 통하여 PPARβ/δ의 발현을 조절한다
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Authors: Gan, Z., Burkart-Hartman, E. M., Han, D.-H., Finck, B., Leone, T. C., Smith, E. Y., Ayala, J. E., Holloszy, J., & Kelly, D. P.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
Washington University in St. Louis (US)
ORCID: Gan, Zhenji
Han, Dong-Ho
Finck, Brian
Ayala, Julio E.
Kelly, Daniel P.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2011-12-01
Volume: 25
Issue: 24
Pages: 2619-2630
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.178434.111
PMC: PMC3248683
OpenAlex: W2129266853
Semantic Scholar: 76f056cec59aae15858af9dd317cafade639983e
Cited by: 138
References: 60
Citations by year: 2026: 5 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 10 · 2021: 11 · 2020: 14 · 2019: 10 · 2018: 14 · 2017: 10 · 2016: 10 · 2015: 10 · 2014: 6 · 2013: 21 · 2012: 6
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
Funders: Alvin J. Siteman Cancer Center (CA91842, #P30 CA91842)
National Institutes of Health (CA91842)
Washington University School of Medicine in St. Louis
National Institute on Aging (R37AG000425)
National Cancer Institute (CA91842, P30CA091842)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK045416, P30DK020579)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
Keywords: PPARδ, PPARα, AMPK, MEF2A, skeletal muscle glucose metabolism, pyruvate oxidation, muscle creatine kinase, transcriptional regulation, exercise performance, GLUT4, glycogen, muscle energy metabolism, exercise training
MeSH terms: AMP-Activated Protein Kinase Kinases, Animals, Cells, Cultured, Female, Glucose, Male, Oxidation-Reduction, Physical Conditioning, Animal, Protein Kinases, Transcriptional Activation, Myogenic Regulatory Factors, Muscle, Skeletal, Lactate Dehydrogenases, PPAR alpha, PPAR delta, Mice

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The nuclear receptor PPARβ/δ programs muscle glucose metabolism in cooperation with AMPK and MEF2

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