Endothelial AMPK Activation Induces Mitochondrial Biogenesis and Stress Adaptation via eNOS-Dependent Mtorc1 Signaling
Open accessAbstract
Metabolic stress sensors like AMP-activated protein kinase (AMPK) are known to confer stress adaptation and promote longevity in lower organisms. This study demonstrates that activating the metabolic stress sensor AMP-activated protein kinase (AMPK) in endothelial cells helps maintain normal cellular function by promoting mitochondrial biogenesis and stress adaptation. To better define the mechanisms whereby AMPK promotes endothelial stress resistance, we used 5-aminoimidazole-4-carboxamide riboside (AICAR) to chronically activate AMPK and observed stimulation of mitochondrial biogenesis in wild type mouse endothelium, but not in endothelium from endothelial nitric oxide synthase knockout (eNOS-null) mice. Interestingly, AICAR-enhanced mitochondrial biogenesis was blocked by pretreatment with the mammalian target of rapamycin complex 1 (mTORC1) inhibitor, rapamycin. Further, AICAR stimulated mTORC1 as determined by phosphorylation of its known downstream effectors in wild type, but not eNOS-null, endothelial cells. Together these data indicate that eNOS is needed to couple AMPK activation to mTORC1 and thus promote mitochondrial biogenesis and stress adaptation in the endothelium. These data suggest a novel mechanism for mTORC1 activation that is significant for investigations in vascular dysfunction.
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AMPK has been implicated in regulation of mitochondrial biogenesis, providing a link between metformin, AMPK, and improved mitochondrial function.
“AMPK has also been implicated in the regulation of mitochondrial biogenesis, thus providing another link between metformin, AMPK, and improved mitochondrial function (149, 150).”
From A Critical Review of the Evidence That Metformin Is a Putative Anti-Aging Drug That Enhances Healthspan and Extends Lifespan (2021) · cites this paper as [150]
If metformin can offset the decline in mitochondrial function, then this effect could contribute to enhancing both healthspan and lifespan.
“If metformin can offset the decline in mitochondrial function, as some studies suggest, then this effect could contribute to enhancing both healthspan and lifespan (138, 149, 150).”
From A Critical Review of the Evidence That Metformin Is a Putative Anti-Aging Drug That Enhances Healthspan and Extends Lifespan (2021) · cites this paper as [150]
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- Authors
- Li, C., Reif, M. M., Craige, S. M., Kant, S., & Keaney, J. F.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Kant, Shashi
- Keaney, John F.
- Venue
- Nitric Oxide
- Publisher
- Elsevier BV
- Published
- 2016-05
- Volume
- 55-56
- Pages
- 45-53
- ISSN
- 1089-8603 (ISSN-L)
- PMC
- PMC4860108
- OpenAlex
- W2299490336
- Cited by
- 34
- References
- 46
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 8 · 2019: 2 · 2018: 5 · 2017: 1
- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nitric Oxide (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- NHLBI (R01HL092122, R01HL098407)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- AMPK, endothelial cells, mitochondrial biogenesis, endothelial nitric oxide synthase, mTORC1 signaling, AICAR, rapamycin, vascular dysfunction
- MeSH terms
- Calcimycin, Mechanistic Target of Rapamycin Complex 1, Adaptation, Physiological, Aminoimidazole Carboxamide, Animals, Organelle Biogenesis, Cells, Cultured, Endothelium, Vascular, Humans, Hydrogen Peroxide, Mitochondria, Ribonucleotides, Signal Transduction, Mice, Knockout, Oxidative Stress, Sirolimus, Enzyme Activators, Endothelial Cells, Rats, Nitric Oxide Synthase Type III, AMP-Activated Protein Kinases
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