Evidence map›Paper›PMID 22404107›Full record

ArticleBiochemistry2012

Aldehyde oxidase functions as a superoxide generating NADH oxidase: an important redox regulated pathway of cellular oxygen radical formation.

Tapan K Kundu, Murugesan Velayutham, Jay L Zweier

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 95 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Review
  5. Article
  6. Article
  7. Review
  8. Enzyme Kinetics, Pharmacokinetics, and Inhibition of Aldehyde Oxidase.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. PeerJ · 2018
    Article
  18. Article
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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

3 authors at 1 institution in 1 country.

Tapan K KunduCenter for Biomedical EPR Spectroscopy and Imaging, the Davis Heart and Lung Research Institute, and Division of Cardiovascular Medicine, Department of Internal Medicine, The Ohio State University College of Medicine, Columbus, Ohio 43210, United States.
Murugesan Velayutham
Jay L Zweier
The Ohio State University · US

Funding

Stat3 in Post-Ischemic Myocardial InflammationP01HL065608 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI BECKER, LEWIS C · 2000 to 2011
$22.0M
OXYGEN RADICALS AND NITRIC OXIDE IN POSTISCHEMIC INJURYR01HL063744 · NHLBI · OHIO STATE UNIVERSITY · PI ZWEIER, JAY LOUIS · 2000 to 2009
$5.2M
MEASURE OF FREE RADICAL GENERATION IN HEARTR01HL038324 · NHLBI · OHIO STATE UNIVERSITY · PI ZWEIER, JAY LOUIS · 1992 to 2010
$3.5M
MEASUREMENT OF FREE RADICAL GENERATION IN THE HEARTR29HL038324 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI ZWEIER, JAY LOUIS · 1987 to 1991
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NHLBI NIH HHS HL38324NHLBI NIH HHS HL63744NHLBI NIH HHS HL65608NHLBI NIH HHS P01 HL065608NHLBI NIH HHS R01 HL038324NHLBI NIH HHS R01 HL063744
6 · The paper itself

Abstract

The enzyme aldehyde oxidase (AO) is a member of the molybdenum hydroxylase family that includes xanthine oxidoreductase (XOR); however, its physiological substrates and functions remain unclear. Moreover, little is known about its role in cellular redox stress. Utilizing electron paramagnetic resonance spin trapping, we measured the role of AO in the generation of reactive oxygen species (ROS) through the oxidation of NADH and the effects of inhibitors of AO on NADH-mediated superoxide (O(2)(•−)) generation. NADH was found to be a good substrate for AO with apparent K(m) and V(max) values of 29 μM and 12 nmol min(-1) mg(-1), respectively. From O(2)(•−) generation measurements by cytochrome c reduction the apparent K(m) and V(max) values of NADH for AO were 11 μM and 15 nmol min(-1) mg(-1), respectively. With NADH oxidation by AO, ≥65% of the total electron flux led to O(2)(•−) generation. Diphenyleneiodonium completely inhibited AO-mediated O(2)(•−) production, confirming that this occurs at the FAD site. Inhibitors of this NADH-derived O(2)(•−) generation were studied with amidone the most potent exerting complete inhibition at 100 μM concentration, while 150 μM menadione, raloxifene, or β-estradiol led to 81%, 46%, or 26% inhibition, respectively. From the kinetic data, and the levels of AO and NADH, O(2)(•−) production was estimated to be ~89 and ~4 nM/s in liver and heart, respectively, much higher than that estimated for XOR under similar conditions. Owing to the ubiquitous distribution of NADH, aldehydes, and other endogenous AO substrates, AO is predicted to have an important role in cellular redox stress and related disease pathogenesis.

Indexed as

Aldehyde OxidaseElectron Spin Resonance SpectroscopyKineticsMultienzyme ComplexesNADH, NADPH OxidoreductasesOxidation-ReductionSuperoxidesAldehyde OxidaseMultienzyme ComplexesNADH, NADPH OxidoreductasesNADH oxidaseSuperoxides

Identifiers

PMID22404107
PMCPMC3954720
OpenAlexW2092178799

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.