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Study · Animal study (in vivo) · mouse · 2022

6 results

Nicotinamide Mononucleotide Administration Amends Protein Acetylome of Aged Mouse Liver.

Luo C, Ding W, Zhu S, Chen Y, Liu X, Deng H

Cells16 May 2022Cited by 23 (Europe PMC)

Summary

It is known that the activities of nicotine adenine dinucleotide (NAD+)-dependent deacetylase decline in the aging mouse liver, and nicotinamide mononucleotide (NMN)-mediated activation of deacetylase has been shown to increase healthspans. However, age-induced changes of the acetylomic landscape and effects of NMN treatment on protein acetylation have not been reported. Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation. In total, 7773 acetylated peptides assigned to 1997 proteins were commonly identified from young and aged livers treated with vehicle or NMN. The major biological processes associated with proteins exhibiting increased acetylation from aged livers were oxidation-reduction and metabolic processes. Proteins with decreased acetylation from aged livers mostly participated in transport and translation processes. Furthermore, NMN treatment inhibited the aging-related increase of acetylation on proteins regulating fatty acid β oxidation, the tricarboxylic acid (TCA) cycle and valine degradation. In particular, NAD (P) transhydrogenase (NNT) was markedly hyperacetylated at K70 in aged livers, and NMN treatment decreased acetylation intensity without altering protein levels. Acetylation at cytochrome 3a25 (Cyp3a25) at K141 was also greatly increased in aged livers, and NMN treatment totally arrested this increase. Our extensive identification and analysis provide novel insight and potential targets to combat aging and aging-related functional decline.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study6

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

  1. 01AnimalAnimal study (in vivo)Mechanism

    In aged mouse liver, NMN inhibited increased acetylation of proteins that regulate fatty acid β oxidation.

    In plain wordsIn mice, NMN reduced the aging-related increase in acetylation of liver proteins that regulate fatty acid breakdown.

    Outcome
    DecreaseAcetylation of fatty acid β-oxidation proteins
    Study

    mousen: not reported in source

    Aged mouse liver
    Outcome group
    Protein and amino acid metabolism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Furthermore, NMN treatment inhibited the aging-related increase of acetylation on proteins regulating fatty acid β oxidation, the tricarboxylic acid (TCA) cycle and valine degradation.
    1 context sentence
    Summary · context
    Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation.
  2. 02AnimalAnimal study (in vivo)Mechanism

    In aged mouse liver, NMN inhibited increased acetylation of proteins that regulate the TCA cycle.

    In plain wordsIn mice, NMN reduced the aging-related increase in acetylation of liver proteins that regulate the TCA cycle.

    Outcome
    DecreaseAcetylation of TCA cycle proteins
    Study

    mousen: not reported in source

    Aged mouse liver
    Outcome group
    Protein and amino acid metabolism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Furthermore, NMN treatment inhibited the aging-related increase of acetylation on proteins regulating fatty acid β oxidation, the tricarboxylic acid (TCA) cycle and valine degradation.
    1 context sentence
    Summary · context
    Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation.
  3. 03AnimalAnimal study (in vivo)Mechanism

    In aged mouse liver, NMN inhibited increased acetylation of proteins that regulate valine degradation.

    In plain wordsIn mice, NMN reduced the aging-related increase in acetylation of liver proteins that regulate valine degradation.

    Outcome
    DecreaseAcetylation of valine degradation proteins
    Study

    mousen: not reported in source

    Aged mouse liver
    Outcome group
    Protein and amino acid metabolism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Furthermore, NMN treatment inhibited the aging-related increase of acetylation on proteins regulating fatty acid β oxidation, the tricarboxylic acid (TCA) cycle and valine degradation.
    1 context sentence
    Summary · context
    Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation.
  4. 04AnimalAnimal study (in vivo)Mechanism

    In aged mouse liver, NMN decreased NNT K70 acetylation intensity.

    In plain wordsIn mice, NMN reduced NNT K70 acetylation in aged liver.

    Outcome
    DecreaseNNT K70 acetylation
    Study

    mousen: not reported in source

    Aged mouse liver
    Outcome group
    Protein and amino acid metabolism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In particular, NAD (P) transhydrogenase (NNT) was markedly hyperacetylated at K70 in aged livers, and NMN treatment decreased acetylation intensity without altering protein levels.
    1 context sentence
    Summary · context
    Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation.
  5. 05AnimalAnimal study (in vivo)Mechanism

    In aged mouse liver, NMN did not alter NNT protein levels.

    In plain wordsIn mice, NMN did not alter NNT protein levels in aged liver.

    Outcome
    No significant changeNNT protein levels
    Study

    mousen: not reported in source

    Aged mouse liver
    Outcome group
    Protein and amino acid metabolism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In particular, NAD (P) transhydrogenase (NNT) was markedly hyperacetylated at K70 in aged livers, and NMN treatment decreased acetylation intensity without altering protein levels.
    1 context sentence
    Summary · context
    Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation.
  6. 06AnimalAnimal study (in vivo)Mechanism

    In aged mouse liver, NMN completely arrested the aging-related increase in Cyp3a25 K141 acetylation.

    In plain wordsIn mice, NMN prevented the aging-related increase in liver Cyp3a25 K141 acetylation.

    Outcome
    DecreaseCyp3a25 K141 acetylation
    Study

    mousen: not reported in source

    Aged mouse liver
    Outcome group
    Protein and amino acid metabolism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Acetylation at cytochrome 3a25 (Cyp3a25) at K141 was also greatly increased in aged livers, and NMN treatment totally arrested this increase.
    1 context sentence
    Summary · context
    Here, we performed immunoprecipitation coupled with label-free quantitative LC-MS/MS (IPMS) to identify the acetylome and investigate the effects of aging and NMN on liver protein acetylation.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  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

Terms as the source lists them.

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