Modulation of Mitochondrial Membrane Potential and ROS Generation by Nicotinamide in a Manner Independent of SIRT1 and Mitophagy
Open accessAbstract
Nicotinamide (NAM) plays essential roles in physiology through facilitating NAD + redox homeostasis.Importantly, at high doses, it protects cells under oxidative stresses, and has shown therapeutic effectiveness in a variety of disease conditions.In our previous studies, NAM lowered reactive oxygen species (ROS) levels and extended cellular life span in primary human cells.In the treated cells, levels of NAD + /NADH and SIRT1 activity increased, while mitochondrial content decreased through autophagy activation.The remaining mitochondria were marked with low superoxide levels and high membrane potentials (ψ m ); we posited that the treatment of NAM induced an activation of mitophagy that is selective for depolarized mitochondria, which produce high levels of ROS.However, evidence for the selective mitophagy that is mediated by SIRT1 has never been provided.This study sought to explain the mechanisms by which NAM lowers ROS levels and increases ψ m .Our results showed that NAM and SIRT1 activation exert quite different effects on mitochondrial physiology.Furthermore, the changes in ROS and ψ m were not found to be mediated through autophagy or SIRT activation.Rather, NAM suppressed superoxide generation via a direct reduction of electron transport, and increased ψ m via suppression of mitochondrial permeability transition pore formation.Our results dissected the effects of cellular NAD + redox modulation, and emphasized the importance of the NAD + /NADH ratio in the mitochondria as well as the cytosol in maintaining mitochondrial quality.
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Even when mPTP opening is reversed and mitochondria recover, loss of NAD+ leaves the mitochondria more susceptible to a second opening of the pore.
“Therefore, even when the mPTP opening is reversed, and the mitochondria recover, the loss of NAD+ would leave the mitochondria more susceptible to a second opening of the pore [83].”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [83]
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- Authors
- Song, S. B., Jang, S.-Y., Kang, H. T., Wei, B., Jeoun, U.-W., Yoon, G. S., & Hwang, E. S.
- Affiliations
- University of Seoul (KR)
- Ajou University (KR)
- Corresponding author
- Hwang, Eun Seong
- Venue
- Molecules and Cells
- Publisher
- Elsevier BV
- Published
- 2017-07
- Volume
- 40
- Issue
- 7
- Pages
- 503-514
- ISSN
- 0219-1032 (ISSN-L)
- 1016-8478
- PMC
- PMC5547220
- OpenAlex
- W2763738314
- Cited by
- 114
- References
- 63
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 12 · 2023: 14 · 2022: 13 · 2021: 14 · 2020: 21 · 2019: 18 · 2018: 8
- FWCI
- 7.77
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecules and Cells (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- AJOU Open Repository (Ajou University) (submittedVersion, cc-by-nc-sa)
- Funders
- University of Seoul
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- nicotinamide, mitochondrial membrane potential, reactive oxygen species, superoxide, SIRT1, mitophagy, NAD+/NADH ratio, mitochondrial permeability transition pore, electron transport, autophagy, mitochondrial quality control, oxidative stress
- MeSH terms
- Peptidyl-Prolyl Isomerase F, Mitochondrial Permeability Transition Pore, PTEN-Induced Putative Kinase, Acetylation, Cytosol, Electron Transport, Heterocyclic Compounds, 4 or More Rings, Humans, Infant, Newborn, Male, Mitochondria, Models, Biological, Niacinamide, Protein Kinases, Reactive Oxygen Species, Cyclophilins, Mitochondrial Proteins, Mitochondrial Membrane Transport Proteins, Ubiquitin-Protein Ligases, Membrane Potential, Mitochondrial, Sirtuin 1, Mitophagy
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