Skip to content

Study · In vitro (cells) · 1996

4 results

Enzymatic activities affecting exogenous nicotinamide adenine dinucleotide in human skin fibroblasts.

Aleo MF, Sestini S, Pompucci G, Preti A

Journal of cellular physiology1 Apr 1996Cited by 4 (Europe PMC)

PMID8698835 (opens in a new tab)DOI10.1002/(sici)1097-4652(199604)167:1<173::aid-jcp20>3.0.co;2-b (opens in a new tab)PepBankPUB-08698835
Publisher pagePubMedAsk about this study
Jump to 4 results

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study4

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

  1. 01LabIn vitro (cells)Mechanism

    In human skin fibroblasts, membrane nucleotide pyrophosphatase hydrolyzed extracellular NAD to yield nicotinamide mononucleotide.

    In plain wordsIn cells, a membrane enzyme broke down extracellular NAD to produce nicotinamide mononucleotide.

    Peptide
    NAD+ (nicotinamide adenine dinucleotide)
    Outcome
    Not applicableNAD pyrophosphoric bond hydrolysis
    Study

    humann: not reported in source

    Intact human skin fibroblasts
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Two enzymatic activities affecting extracellular NAD were detected on the plasma membrane, one hydrolyzing the pyrophosphoric bond and yielding nicotinamide mononucleotide (nucleotide pyrophosphatase)
    1 context sentence
    Summary · context
    The fate of nicotinamide adenine dinucleotide (NAD), AMP, and ADP-ribose supplied to intact human skin fibroblasts was monitored, and the concentrations of intra- and extracellular pyridine and purine compounds were determined by HPLC analysis.
  2. 02LabIn vitro (cells)Mechanism

    In human skin fibroblasts, membrane NAD-glycohydrolase cleaved extracellular NAD to release nicotinamide.

    In plain wordsIn cells, NAD-glycohydrolase broke down extracellular NAD to release nicotinamide.

    Peptide
    NAD+ (nicotinamide adenine dinucleotide)
    Outcome
    Not applicableNAD glycoside link cleavage
    Study

    humann: not reported in source

    Intact human skin fibroblasts
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Two enzymatic activities affecting extracellular NAD were detected on the plasma membrane, one hydrolyzing the pyrophosphoric bond and yielding nicotinamide mononucleotide (nucleotide pyrophosphatase) and the other cleaving the glycoside link and releasing nicotinamide (NAD-glycohydrolase).
    1 context sentence
    Summary · context
    The fate of nicotinamide adenine dinucleotide (NAD), AMP, and ADP-ribose supplied to intact human skin fibroblasts was monitored, and the concentrations of intra- and extracellular pyridine and purine compounds were determined by HPLC analysis.
  3. 03LabIn vitro (cells)Mechanism

    In human skin fibroblasts incubated with NAD, extracellular AMP was absent because it was completely catabolized to hypoxanthine.

    In plain wordsIn cells incubated with NAD, no extracellular AMP remained because it was broken down to hypoxanthine.

    Peptide
    NAD+ (nicotinamide adenine dinucleotide)
    Outcome
    Not applicableExtracellular AMP
    Study

    humann: not reported in source

    Intact human skin fibroblasts
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    No AMP or ADP-ribose was found in the extracellular medium of cells incubated with NAD, the former being completely catabolized to hypoxanthine and the latter degraded to adenine and hypoxanthine.
    1 context sentence
    Summary · context
    The fate of nicotinamide adenine dinucleotide (NAD), AMP, and ADP-ribose supplied to intact human skin fibroblasts was monitored, and the concentrations of intra- and extracellular pyridine and purine compounds were determined by HPLC analysis.
  4. 04LabIn vitro (cells)Mechanism

    In human skin fibroblasts incubated with NAD, extracellular ADP-ribose was absent because it degraded to adenine and hypoxanthine.

    In plain wordsIn cells incubated with NAD, no extracellular ADP-ribose remained because it was broken down to adenine and hypoxanthine.

    Peptide
    NAD+ (nicotinamide adenine dinucleotide)
    Outcome
    Not applicableExtracellular ADP-ribose
    Study

    humann: not reported in source

    Intact human skin fibroblasts
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    No AMP or ADP-ribose was found in the extracellular medium of cells incubated with NAD, the former being completely catabolized to hypoxanthine and the latter degraded to adenine and hypoxanthine.
    1 context sentence
    Summary · context
    The fate of nicotinamide adenine dinucleotide (NAD), AMP, and ADP-ribose supplied to intact human skin fibroblasts was monitored, and the concentrations of intra- and extracellular pyridine and purine compounds were determined by HPLC analysis.

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

    14 Oct 2026, 05:02 UTC

    Study results updated

  2. Version 1

    14 Oct 2026, 01:46 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

PepBank is a research reference. Talk to a doctor before you use any peptide.