Assessment of NAD(+)metabolism in human cell cultures, erythrocytes, cerebrospinal fluid and primate skeletal muscle
Open accessAbstract
The reduction-oxidation state of NAD+/NADH is critical for cellular health with NAD+ and its metabolites playing critical roles in aging and pathologies. Given the inherent autooxidation of reduced dinucleotides (i.e. NADH/NADPH), and the well-established differential stability, the accurate measurement of NAD+ and its metabolites is technically challenging. Moreover, sample processing, normalization and measurement strategies can profoundly alter results. Here we developed a rapid and sensitive liquid chromatography mass spectrometry-based method to quantify the NAD+ metabolome with careful consideration of these intrinsic chemical instabilities. Utilizing this method we assess NAD+ metabolite stabilities and determine the presence and concentrations of NAD+ metabolites in clinically relevant human samples including cerebrospinal fluid, erythrocytes, and primate skeletal muscle.
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Increased NAD+, through overexpressed NAD+ synthetic enzymes or NAD+ precursor supplementation, promotes cancer cell proliferation, migration, and resistance to anticancer chemo- or radiotherapy.
“increased NAD+, through either overexpressed NAD+ synthetic enzymes or supplementation with NAD+ precursors, promotes cancer cell proliferation, migration, and resistance to anticancer chemo-/radiotherapy”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Demarest et al., 2019
Major NAD+ metabolic enzymes iNAMPT, eNAMPT, and/or NMNAT2 are overexpressed in many cancers, including breast, pancreatic, prostate, and colorectal cancers.
“Major NAD+ metabolic enzymes, e.g., iNAMPT, eNAMPT, and/or NMNAT2, are overexpressed in a broad variety of cancers including breast, pancreatic, prostate, and colorectal cancers”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Demarest et al., 2019
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- Authors
- Demarest, T. G., Truong, G. T. D., Lovett, J., Mohanty, J. G., Mattison, J. A., Mattson, M. P., Ferrucci, L., Bohr, V. A., & Moaddel, R.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Moaddel, Ruin
- ORCID
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 572
- Pages
- 1-8
- ISSN
- 0003-2697 (ISSN-L)
- PMC
- PMC6685425
- OpenAlex
- W2915579808
- Cited by
- 48
- References
- 24
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 10 · 2023: 4 · 2022: 11 · 2021: 5 · 2020: 5 · 2019: 3
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Analytical Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- NAD+ metabolism, NAD+/NADH redox state, cerebrospinal fluid, erythrocytes, skeletal muscle, aging
- MeSH terms
- Acrylamides, Animals, Chromatography, High Pressure Liquid, Erythrocytes, Humans, NAD, Niacinamide, Piperidines, Primates, Pyridinium Compounds, Muscle, Skeletal, Tandem Mass Spectrometry, Metabolome, HEK293 Cells
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