NAD+ homeostasis in health and disease

doi:10.1038/s42255-019-0161-5

Review

. 2020 Jan;2(1):9-31.

doi: 10.1038/s42255-019-0161-5. Epub 2020 Jan 20.

NAD⁺ homeostasis in health and disease

Elena Katsyuba^{1

2}, Mario Romani^#¹, Dina Hofer^#^{1

3}, Johan Auwerx⁴

Affiliations

¹ Laboratory of Integrative Systems Physiology, Interfaculty Institute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
² Nagi Bioscience, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
³ Thermo Fisher Scientific, Zug, Switzerland.
⁴ Laboratory of Integrative Systems Physiology, Interfaculty Institute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland. admin.auwerx@epfl.ch.

^# Contributed equally.

PMID: 32694684
DOI: 10.1038/s42255-019-0161-5

Review

NAD⁺ homeostasis in health and disease

Elena Katsyuba et al. Nat Metab. 2020 Jan.

. 2020 Jan;2(1):9-31.

doi: 10.1038/s42255-019-0161-5. Epub 2020 Jan 20.

Authors

Elena Katsyuba^{1

2}, Mario Romani^#¹, Dina Hofer^#^{1

3}, Johan Auwerx⁴

Affiliations

¹ Laboratory of Integrative Systems Physiology, Interfaculty Institute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
² Nagi Bioscience, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
³ Thermo Fisher Scientific, Zug, Switzerland.
⁴ Laboratory of Integrative Systems Physiology, Interfaculty Institute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland. admin.auwerx@epfl.ch.

^# Contributed equally.

PMID: 32694684
DOI: 10.1038/s42255-019-0161-5

Abstract

The conceptual evolution of nicotinamide adenine dinucleotide (NAD⁺) from being seen as a simple metabolic cofactor to a pivotal cosubstrate for proteins regulating metabolism and longevity, including the sirtuin family of protein deacylases, has led to a new wave of scientific interest in NAD⁺. NAD⁺ levels decline during ageing, and alterations in NAD⁺ homeostasis can be found in virtually all age-related diseases, including neurodegeneration, diabetes and cancer. In preclinical settings, various strategies to increase NAD⁺ levels have shown beneficial effects, thus starting a competitive race to discover marketable NAD⁺ boosters to improve healthspan and lifespan. Here, we review the basics of NAD⁺ biochemistry and metabolism, and its roles in health and disease, and we discuss current challenges and the future translational potential of NAD⁺ research.

PubMed Disclaimer

Cited by

Potential Therapeutic Interventions Targeting NAD⁺ Metabolism for ALS.
Lundt S, Ding S. Lundt S, et al. Cells. 2024 Sep 9;13(17):1509. doi: 10.3390/cells13171509. Cells. 2024. PMID: 39273079 Free PMC article. Review.
NAD+ and Niacin Supplementation as Possible Treatments for Glaucoma and Age-Related Macular Degeneration: A Narrative Review.
Gemae MR, Bassi MD, Wang P, Chin EK, Almeida DRP. Gemae MR, et al. Nutrients. 2024 Aug 21;16(16):2795. doi: 10.3390/nu16162795. Nutrients. 2024. PMID: 39203931 Free PMC article. Review.
Nicotinamide: Bright Potential in Glaucoma Management.
Babighian S, Gattazzo I, Zanella MS, Galan A, D'Esposito F, Musa M, Gagliano C, Lapenna L, Zeppieri M. Babighian S, et al. Biomedicines. 2024 Jul 25;12(8):1655. doi: 10.3390/biomedicines12081655. Biomedicines. 2024. PMID: 39200120 Free PMC article. Review.
A Multi-Target Pharmacological Correction of a Lipoyltransferase LIPT1 Gene Mutation in Patient-Derived Cellular Models.
Gómez-Fernández D, Romero-González A, Suárez-Rivero JM, Cilleros-Holgado P, Álvarez-Córdoba M, Piñero-Pérez R, Romero-Domínguez JM, Reche-López D, López-Cabrera A, Ibáñez-Mico S, Castro de Oliveira M, Rodríguez-Sacristán A, González-Granero S, García-Verdugo JM, Sánchez-Alcázar JA. Gómez-Fernández D, et al. Antioxidants (Basel). 2024 Aug 22;13(8):1023. doi: 10.3390/antiox13081023. Antioxidants (Basel). 2024. PMID: 39199267 Free PMC article.
Metabolite signaling in the heart.
Flam E, Arany Z. Flam E, et al. Nat Cardiovasc Res. 2023 Jun;2(6):504-516. doi: 10.1038/s44161-023-00270-6. Epub 2023 May 25. Nat Cardiovasc Res. 2023. PMID: 39195876 Review.

See all "Cited by" articles

References

1. Harden, A. & Young, W. The alcoholic ferment of yeast‐juice. Proc. R. Soc. Lond. B 77, 405–420 (1906). - DOI
1. von Euler, H. & Myrbäck, K. Co‐zymase. XVII. Hoppe-Seyler’s Z. Physiol. Chem. 190, 93–100 (1930). - DOI
1. Warburg, O. & Christian, W. Pyridine, the hydrogen transfusing component of fermentative enzymes. Helv. Chim. Acta 19, 79–88 (1936). - DOI
1. Imai, S., Armstrong, C. M., Kaeberlein, M. & Guarente, L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795–800 (2000). - DOI
1. Haigis, M. C. & Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253–295 (2010). - DOI - PubMed - PMC

Publication types

Actions
Actions
Actions

MeSH terms

Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions

Substances

Actions
Actions
Actions

Grants and funding

R01 AG043930/AG/NIA NIH HHS/United States

LinkOut - more resources

Full Text Sources
- Nature Publishing Group
Other Literature Sources
- The Lens - Patent Citations

[1] Harden, A. & Young, W. The alcoholic ferment of yeast‐juice. Proc. R. Soc. Lond. B 77, 405–420 (1906). - DOI

[2] Harden, A. & Young, W. The alcoholic ferment of yeast‐juice. Proc. R. Soc. Lond. B 77, 405–420 (1906). - DOI

[3] von Euler, H. & Myrbäck, K. Co‐zymase. XVII. Hoppe-Seyler’s Z. Physiol. Chem. 190, 93–100 (1930). - DOI

[4] von Euler, H. & Myrbäck, K. Co‐zymase. XVII. Hoppe-Seyler’s Z. Physiol. Chem. 190, 93–100 (1930). - DOI

[5] Warburg, O. & Christian, W. Pyridine, the hydrogen transfusing component of fermentative enzymes. Helv. Chim. Acta 19, 79–88 (1936). - DOI

[6] Warburg, O. & Christian, W. Pyridine, the hydrogen transfusing component of fermentative enzymes. Helv. Chim. Acta 19, 79–88 (1936). - DOI

[7] Imai, S., Armstrong, C. M., Kaeberlein, M. & Guarente, L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795–800 (2000). - DOI

[8] Imai, S., Armstrong, C. M., Kaeberlein, M. & Guarente, L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795–800 (2000). - DOI

[9] Haigis, M. C. & Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253–295 (2010). - DOI - PubMed - PMC

[10] Haigis, M. C. & Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253–295 (2010). - DOI - PubMed - PMC

Save citation to file

Email citation

Add to Collections

Add to My Bibliography

Your saved search

Create a file for external citation management software

Your RSS Feed

NAD⁺ homeostasis in health and disease

Affiliations

NAD⁺ homeostasis in health and disease

Authors

Affiliations

Abstract

Similar articles

Cited by

References

Publication types

MeSH terms

Substances

Grants and funding

LinkOut - more resources

Full Text Sources

Other Literature Sources

Abstract

Similar articles

Cited by

References

Publication types

MeSH terms

Substances

Related information

Grants and funding

LinkOut - more resources

Full Text Sources

Other Literature Sources