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Study · In vitro (cells) · 2026

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Nicotinamide Ameliorates Deoxynivalenol-Induced Injury in Renal Cells via Inhibiting PARP1 Hyperactivation and Restoring NAD+ Homeostasis.

Chen C, Qin Y, Luo Z, Mu P, Wen J, Deng Y

Toxins10 May 2026Cited by 1 (Europe PMC)

PMID42188629 (opens in a new tab)PMCIDPMC13211343 (opens in a new tab)DOI10.3390/toxins18050227 (opens in a new tab)PepBankPUB-42188629
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Summary

Deoxynivalenol (DON) is a globally prevalent mycotoxin that threatens food and feed safety via severe multi-organ toxicity. Previous studies indicate that DON induces cellular energy metabolism dysregulation by triggering oxidative stress and impairing mitochondrial function. During this process, nicotinamide adenine dinucleotide (NAD+), a central coenzyme in cellular energy metabolism, frequently exhibits significantly decreased intracellular levels or even complete depletion. However, the molecular mechanisms underlying the disruption of NAD+ homeostasis by DON exposure, as well as the development of targeted countermeasures, remain elusive. Using human embryonic kidney 293T (HEK293T) cells as an in vitro renal toxicity model, we dissected DON-induced NAD+ dysregulation and evaluated the protective potential of nicotinamide (NAM). DON caused significant NAD+ depletion in porcine serum (in vivo) and HEK293T cells (in vitro), which was confirmed as a key driver of cytotoxicity. Mechanistically, although DON binds and inhibits nicotinamide phosphoribosyltransferase (NAMPT), the rate-limiting enzyme of the NAD+ salvage pathway, neither NAMPT knockdown and overexpression nor nicotinamide mononucleotide (NMN) supplementation rescued DON-induced toxicity. Instead, DON dose-dependently activated poly(ADP-ribose) polymerase 1 (PARP1), the primary intracellular NAD+-consuming enzyme, to accelerate NAD+ depletion. PARP1 knockdown markedly attenuated DON-induced cytotoxicity, identifying PARP1 hyperactivation as the core toxic mechanism. NAM dose-dependently suppressed PARP1 activity, replenished NAD+ pools, and reversed cell injury. These findings establish PARP1-driven NAD+ depletion as an important mechanism of DON-induced renal toxicity, providing a promising intervention candidate for mitigating DON toxicity in food safety.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study1

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Efficacy outcome

    In HEK293T cells, NMN supplementation did not rescue DON-induced toxicity.

    In plain wordsIn cells, NMN did not rescue toxicity caused by deoxynivalenol.

    Peptide
    NMN (nicotinamide mononucleotide)
    Outcome
    No significant changeDON-induced cytotoxicity
    Study

    humann: not reported in source

    DON-treated HEK293T cells
    Outcome group
    Kidney function · Kidney and urinary
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Mechanistically, although DON binds and inhibits nicotinamide phosphoribosyltransferase (NAMPT), the rate-limiting enzyme of the NAD+ salvage pathway, neither NAMPT knockdown and overexpression nor nicotinamide mononucleotide (NMN) supplementation rescued DON-induced toxicity.
    1 context sentence
    Summary · context
    Using human embryonic kidney 293T (HEK293T) cells as an in vitro renal toxicity model, we dissected DON-induced NAD+ dysregulation and evaluated the protective potential of nicotinamide (NAM).

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Version history

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  1. Version 2Current

    21 Oct 2026, 15:58 UTC

    Study results updated

  2. Version 1

    21 Oct 2026, 12:50 UTC

    First added · source update from Europe PMC

Subjects

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