Evidence map›Paper›PMID 24204965›Full record

ArticlePloS one2013

Fatty acids are key in 4-hydroxy-2-nonenal-mediated activation of uncoupling proteins 1 and 2.

Elena A Malingriaux, Anne Rupprecht, Lars Gille, Olga Jovanovic, Petr Jezek, Martin Jaburek, Elena E Pohl

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Molecular Dynamics Simulations of Mitochondrial Uncoupling Protein 2.International journal of molecular sciences · 2021
    Article
  7. Induced Ketosis as a Treatment for Neuroprogressive Disorders: Food for Thought?The international journal of neuropsychopharmacology · 2020
    Review
  8. Review
  9. Article
  10. Article
  11. Important Trends in UCP3 Investigation.Frontiers in physiology · 2019
    Review
  12. Review
  13. Article
  14. Review
  15. Oleate induces KNeuroscience · 2017
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 2 countries.

Elena A MalingriauxInstitute of Physiology, Pathophysiology and Biophysics, University of Veterinary Medicine, Vienna, Austria.
Anne Rupprecht
Lars Gille
Olga Jovanovic
Petr Jezek
Martin Jaburek
Elena E Pohl
University of Veterinary Medicine Vienna · ATCzech Academy of Sciences · CZ

Funding

Austrian Science Fund FWF P 25123
6 · The paper itself

Abstract

The production of reactive oxygen species (ROS) in mitochondria is very sensitive to the proton motive force and may be decreased by mild uncoupling, mediated e.g. by mitochondrial uncoupling proteins (UCPs). UCPs were conversely hypothesized to be activated by ROS. Conclusions from experiments studying the reactive product of lipid peroxidation 4-hydroxy-2-nonenal (HNE) in isolated mitochondria and UCP knock-out mice are highly controversial. Here we investigated the molecular mechanism of HNE action by evaluating the separate contributions of lipid and protein phases of the membrane and by comparing UCP1 and UCP2, which were reconstituted in planar lipid bilayers. We demonstrated that aldehyde does not directly activate either UCP1 or UCP2. However, HNE strongly potentiated the membrane conductance increase (Gm) mediated by different long-chain fatty acids in UCP-containing and in UCP-free membranes and this suggest the involvement of both lipid-mediated and protein-mediated mechanisms with FA playing the central role. Gm increase was concentration-dependent and exhibited a typical saturation kinetic with the binding constant 0.3 mM. By using Electron Paramagnetic Resonance, membrane fluidity change could be excluded as a cause for the HNE-mediated increase in the presence of FA. The impact of the HNE binding to definite positively charged UCP amino acid residues is discussed as a possible protein-mediated mechanism of the UCP activation.

Indexed as

AldehydesAnimalsBlotting, WesternElectron Spin Resonance SpectroscopyElectrophysiologyFatty AcidsHumansIon ChannelsLipid BilayersLiposomesMembrane FluidityMembrane Potential, MitochondrialMiceMitochondriaMitochondrial ProteinsReactive Oxygen Species4-hydroxy-2-nonenalAldehydesFatty AcidsIon ChannelsLipid BilayersLiposomesMitochondrial ProteinsReactive Oxygen SpeciesUCP1 protein, humanUcp1 protein, mouseUCP2 protein, humanUcp2 protein, mouseUncoupling Protein 1Uncoupling Protein 2

Identifiers

PMID24204965
PMCPMC3810126
OpenAlexW2035252221

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.