Evidence map›Paper›PMID 24534704›Full record

ArticleJournal of lipid research2014

Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100.

Cédric Delporte, Karim Zouaoui Boudjeltia, Caroline Noyon, Paul G Furtmüller, Vincent Nuyens, Marie-Christine Slomianny, Philippe Madhoun, Jean-Marc Desmet, Pierre Raynal, Damien Dufour and 11 more

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In one paragraph

Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

40 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  7. Neutrophils-biology and diversity.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2024
    Review
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  9. TheInnate immunity · 2024
    Article
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  11. Review
  12. Article
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  14. Review
  15. Review
  16. Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022
    Review
  17. Review
  18. Article
  19. Article
  20. Article
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

21 authors at 5 institutions in 3 countries.

Cédric DelporteLaboratory of Pharmaceutical Chemistry Faculty of Pharmacy, Université Libre de Bruxelles, Brussels, Belgium.
Karim Zouaoui Boudjeltia
Caroline Noyon
Paul G Furtmüller
Vincent Nuyens
Marie-Christine Slomianny
Philippe Madhoun
Jean-Marc Desmet
Pierre Raynal
Damien Dufour
Chintan N Koyani
Florence Reyé
Alexandre Rousseau
Michel Vanhaeverbeek
Jean Ducobu
Jean-Claude Michalski
Jean Nève
Luc Vanhamme
Christian Obinger
Ernst Malle
Pierre Van Antwerpen
Université Libre de Bruxelles · BEBOKU University · ATCentre National de la Recherche Scientifique · FRMedical University of Graz · ATGrand Charleroi Hospital · BE

Funding

Austrian Science Fund FWF F 3007Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

Oxidation of LDL by the myeloperoxidase (MPO)-H2O2-chloride system is a key event in the development of atherosclerosis. The present study aimed at investigating the interaction of MPO with native and modified LDL and at revealing posttranslational modifications on apoB-100 (the unique apolipoprotein of LDL) in vitro and in vivo. Using amperometry, we demonstrate that MPO activity increases up to 90% when it is adsorbed at the surface of LDL. This phenomenon is apparently reflected by local structural changes in MPO observed by circular dichroism. Using MS, we further analyzed in vitro modifications of apoB-100 by hypochlorous acid (HOCl) generated by the MPO-H2O2-chloride system or added as a reagent. A total of 97 peptides containing modified residues could be identified. Furthermore, differences were observed between LDL oxidized by reagent HOCl or HOCl generated by the MPO-H2O2-chloride system. Finally, LDL was isolated from patients with high cardiovascular risk to confirm that our in vitro findings are also relevant in vivo. We show that several HOCl-mediated modifications of apoB-100 identified in vitro were also present on LDL isolated from patients who have increased levels of plasma MPO and MPO-modified LDL. In conclusion, these data emphasize the specificity of MPO to oxidize LDL.

Indexed as

Amino Acid SequenceApolipoprotein B-100Case-Control StudiesHumansHydrogen PeroxideHydrolysisKidney DiseasesLipoproteins, LDLMolecular Sequence DataOxidation-ReductionPeptide FragmentsPeroxidaseProtein Processing, Post-TranslationalRenal DialysisAPOB protein, humanApolipoprotein B-100Hydrogen PeroxideLipoproteins, LDLPeptide FragmentsPeroxidase3-chlorotyrosineapolipoprotein B-100epitope mappinghypochlorous acidinflammationlow density lipoproteinmyeloperoxidase activity

Identifiers

PMID24534704
PMCPMC3966708
OpenAlexW2333736602

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.