Evidence map›Paper›PMID 30875389›Full record

ArticlePloS one2019

Quantitative analysis of the effects of nicotinamide phosphoribosyltransferase induction on the rates of NAD+ synthesis and breakdown in mammalian cells using stable isotope-labeling combined with mass spectrometry.

Nobumasa Hara, Harumi Osago, Mineyoshi Hiyoshi, Mikiko Kobayashi-Miura, Mikako Tsuchiya

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of and challenges in targeting NADNature reviews. Molecular cell biology · 2024
    Review
  4. Review
  5. Article
  6. A duplex structure of SARM1 octamers stabilized by a new inhibitor.Cellular and molecular life sciences : CMLS · 2022
    Article
  7. Review
  8. Dihydronicotinamide Riboside Is a Potent NADFrontiers in immunology · 2022
    Article
  9. Article
  10. Article
  11. NADFrontiers in physiology · 2020
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Nobumasa HaraDepartment of Biochemistry, Shimane University Faculty of Medicine, Izumo, Shimane, Japan.ORCID 0000-0002-3007-8808
Harumi OsagoDepartment of Biochemistry, Shimane University Faculty of Medicine, Izumo, Shimane, Japan.
Mineyoshi HiyoshiDepartment of Biochemistry, Shimane University Faculty of Medicine, Izumo, Shimane, Japan.
Mikiko Kobayashi-MiuraDepartment of Biochemistry, Shimane University Faculty of Medicine, Izumo, Shimane, Japan.
Mikako TsuchiyaDepartment of Biochemistry, Shimane University Faculty of Medicine, Izumo, Shimane, Japan.
Shimane University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NAD+ is mainly synthesized from nicotinamide (Nam) by the rate-limiting enzyme Nam phosphoribosyltransferase (Nampt) and degraded to Nam by NAD+-degrading enzymes in mammals. Numerous studies report that tissue NAD+ levels decrease during aging and age-related diseases and suggest that NAD+ replenishment promotes healthy aging. Although increased expression of Nampt might be a promising intervention for healthy aging, forced expression of Nampt gene, inducing more than 10-fold increases in the enzyme protein level, has been reported to elevate NAD+ levels only 40-60% in mammalian cells. Mechanisms underlying the limited increases in NAD+ levels remain to be determined. Here we show that Nampt is inhibited in cells and that enhanced expression of Nampt activates NAD+ breakdown. Combined with the measurement of each cell's volume, we determined absolute values (μM/h) of the rates of NAD+ synthesis (RS) and breakdown (RB) using a flux assay with a 2H (D)-labeled Nam, together with the absolute NAD+ concentrations in various mammalian cells including primary cultured cardiomyocytes under the physiological conditions and investigated the relations among total cellular Nampt activity, RS, RB, and the NAD+ concentration. NAD+ concentration was maintained within a narrow range (400-700 μM) in the cells. RS was much smaller than the total Nampt activity, indicating that NAD+ synthesis from Nam in the cells is suppressed. Forced expression of Nampt leading to 6-fold increase in total Nampt activity induced only a 1.6-fold increase in cellular NAD+ concentration. Under the conditions, RS increased by 2-fold, while 2-fold increase in RB was also observed. The small increase in cellular NAD+ concentration is likely due to both inhibited increase in the NAD+ synthesis and the activation of its breakdown. Our findings suggest that cellular NAD+ concentrations do not vary dramatically by the physiological fluctuation of Nampt expression and show the tight link between the NAD+ synthesis and its breakdown.

Indexed as

AnimalsCells, CulturedCell SizeHumansIsotope LabelingKineticsMiceMyocytes, CardiacNADNicotinamide PhosphoribosyltransferaseRatsTandem Mass SpectrometryNADNicotinamide Phosphoribosyltransferase

Identifiers

PMID30875389
PMCPMC6420012
OpenAlexW2922434422

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.