Evidence map›Paper›PMID 24824874›Full record

ArticleBritish journal of pharmacology2015

Interactions of hydrogen sulfide with myeloperoxidase.

Zoltán Pálinkás, Paul G Furtmüller, Attila Nagy, Christa Jakopitsch, Katharina F Pirker, Marcin Magierowski, Katarzyna Jasnos, John L Wallace, Christian Obinger, Péter Nagy

Open access · bronzeAbstract read
In one paragraph

Article in British journal of pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023
    Review
  3. Review
  4. Review
  5. Hydrogen Sulfide Biology and Its Role in Cancer.Molecules (Basel, Switzerland) · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Regulation of the redox metabolome and thiol proteome by hydrogen sulfide.Critical reviews in biochemistry and molecular biology · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. The Role of Host-Generated HFrontiers in cellular and infection microbiology · 2020
    Review
  16. Article
  17. Article
  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

10 authors at 4 institutions in 3 countries.

Zoltán PálinkásDepartment of Molecular Immunology and Toxicology, National Institute of Oncology, Budapest, Hungary.
Paul G Furtmüller
Attila Nagy
Christa Jakopitsch
Katharina F Pirker
Marcin Magierowski
Katarzyna Jasnos
John L Wallace
Christian Obinger
Péter Nagy
BOKU University · ATNational Institute of Oncology · HUMcMaster University · CAPopulation Health Research Institute · CA

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

background and purposeThe actions of hydrogen sulfide in human physiology have been extensively studied and, although it is an essential mediator of many biological functions, the underlying molecular mechanisms of its actions are ill-defined. To elucidate the roles of sulfide in inflammation, we have investigated its interactions with human myeloperoxidase (MPO), a major contributor to inflammatory oxidative stress. EXPERIMENTAL APPROACH: The interactions of sulfide and MPO were investigated using electron paramagnetic resonance, electronic circular dichroism, UV-vis and stopped-flow spectroscopies. KEY

resultsWe found favourable reactions between sulfide and the native-ferric enzyme as well as the MPO redox intermediates, ferrous MPO, compound I and compound II. Sulfide was a potent reversible inhibitor of MPO enzymic activity with an IC50 of 1 µM. In addition, the measured second-order rate constants for the reactions of sulfide with compound I [k = (1.1 ± 0.06) × 10(6)  M(-1)  s(-1)] and compound II [k = (2.0 ± 0.03) × 10(5)  M(-1)  s(-1)] suggest that sulfide is a potential substrate for MPO in vivo. CONCLUSION AND IMPLICATIONS: Endogenous levels of sulfide are likely to inhibit the activity of circulating and endothelium-bound MPO. The fully reversible inhibition suggests a mediatory role of sulfide on the oxidant-producing function of the enzyme. Furthermore, the efficient HOCl oxidation of sulfide to give polysulfides (recently recognized as important components of sulfide biology) together with MPO-catalysed sulfide oxidation and the lack of interaction between MPO and sulfide oxidation products, predict a modulatory role of MPO in sulfide signalling.

Indexed as

AnimalsCircular DichroismElectron Spin Resonance SpectroscopyHumansHydrogen SulfideInflammationInhibitory Concentration 50MaleOxidation-ReductionOxidative StressPeroxidaseRats, WistarSignal TransductionHydrogen SulfidePeroxidase

Identifiers

PMID24824874
PMCPMC4369261
OpenAlexW1543548209

What OpenQuestion holds

Textmetadata
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.