ArticleBiochimica et biophysica acta2013
Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-κB transcriptional activity by preventing p65 de-acetylation.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
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- VEGF inhibitor-induced vascular dysfunction involves redox-sensitive PARP activation and SIRT1 disruption.Experimental physiology · 2026Article
- Oxidative Stress in Liver Metabolic Dysfunction and Diseases, with a Focus on Hepatogenic Diabetes: Effect of Alcohol Consumption.Antioxidants (Basel, Switzerland) · 2025Review
- Tripartite Interaction of Epigenetic Regulation, Brain Aging, and Neuroinflammation: Mechanistic Insights and Therapeutic Implications.Epigenomes · 2025Review
- Oral MIB-626 (β Nicotinamide Mononucleotide) Safely Raises Blood Nicotinamide Adenine Dinucleotide Levels in Hospitalized Patients With COVID-19 and Acute Kidney Injury: A Randomized Controlled Trial.FASEB bioAdvances · 2025Article
- Nicotinamide Adenine Dinucleotide (NADAntioxidants & redox signaling · 2023Review
- The therapeutic potential of targeting regulated non-apoptotic cell death.Nature reviews. Drug discovery · 2023Review
- Therapeutic Properties of Ayahuasca Components in Ischemia/Reperfusion Injury of the Eye.Biomedicines · 2022Article
- Mechanisms of Kaempferol in the treatment of diabetes: A comprehensive and latest review.Frontiers in endocrinology · 2022Review
- Emerging role of PARP-1 and PARthanatos in ischemic stroke.Journal of neurochemistry · 2022Review
- Kaempferol suppresses acetaminophen-induced liver damage by upregulation/activation of SIRT1.Pharmaceutical biology · 2021Article
- Nicotinamide adenine dinucleotide and the sirtuins caution: Pro-cancer functions.Aging medicine (Milton (N.S.W)) · 2021Review
- Targeting Parthanatos in Ischemic Stroke.Frontiers in neurology · 2021Review
- Review
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- Nicotinamide Mononucleotide: Exploration of Diverse Therapeutic Applications of a Potential Molecule.Biomolecules · 2019Review
- The emergence of the nicotinamide riboside kinases in the regulation of NAD+ metabolismJournal of molecular endocrinology · 2018Review
- Cellular and epigenetic drivers of stem cell ageing.Nature reviews. Molecular cell biology · 2018Review
- Bathing effects of east saline groundwater concentrates on allergic (atopic) dermatitis-like skin lesions induced by 2,4-dinitrochlorobenzene in hairless mice.Experimental and therapeutic medicine · 2017Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
NF-κB is a transcription factor that integrates pro-inflammatory and pro-survival responses in diverse cell types. The activity of NF-κB is regulated in part by acetylation of its p65 subunit at lysine 310, which is required for transcription complex formation. De-acetylation at this site is performed by sirtuin 1(SIRT1) and possibly other sirtuins in an NAD(+) dependent manner, such that SIRT1 inhibition promotes NF-κB transcriptional activity. It is unknown, however, whether changes in NAD(+) levels can influence p65 acetylation and cellular inflammatory responses. Poly(ADP-ribose)-1 (PARP-1) is an abundant nuclear enzyme that consumes NAD(+) in the process of forming (ADP-ribose)polymers on target proteins, and extensive PARP-1 activation can reduce intracellular NAD(+) concentrations. Here we tested the idea that PARP-1 activation can regulate NF-κB transcriptional activity by reducing NAD(+) concentrations and thereby inhibiting de-acetylation of p65. Primary astrocyte cultures were treated with the alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) to induce PARP-1 activation. This resulted in sustained acetylation of p65 and increased NF-κB transcriptional activity as monitored by a κB-driven eGFP reporter gene. These effects of MNNG were negated by a PARP-1 inhibitor, in PARP-1(-/-) cells, and in PARP-1(-/-) cells transfected with a catalytically inactive PARP-1 construct, thus confirming that these effects are mediated by PARP-1 catalytic activity. The effects of PARP-1 activation were replicated by a SIRT1 inhibitor, EX-527, and were reversed by exogenous NAD(+). These findings demonstrate that PARP-1-induced changes in NAD(+) levels can modulate NF-κB transcriptional activity through effects on p65 acetylation.
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