Evidence map›Paper›PMID 34500696›Full record

ReviewMolecules (Basel, Switzerland)2021

Mass Spectrometry for the Monitoring of Lipoprotein Oxidations by Myeloperoxidase in Cardiovascular Diseases.

Catherine Coremans, Cédric Delporte, Frédéric Cotton, Phillipe Van De Borne, Karim Zouaoui Boudjeltia, Pierre Van Antwerpen

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022
    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

6 authors at 1 institution in 1 country.

Catherine CoremansRD3-Pharmacognosy, Bioanalysis and Drug Discovery, Faculty of Pharmacy, Université Libre de Bruxelles, 1050 Brussels, Belgium.ORCID 0000-0002-9555-1272
Cédric DelporteRD3-Pharmacognosy, Bioanalysis and Drug Discovery, Faculty of Pharmacy, Université Libre de Bruxelles, 1050 Brussels, Belgium.ORCID 0000-0001-7453-7028
Frédéric CottonLaboratoire Hospitalier Universitaire de Bruxelles (LHUB-ULB), Department of Clinical Chemistry, Université Libre de Bruxelles (ULB), 1000 Brussels, Belgium.
Phillipe Van De BorneDepartment of Cardiology Erasme Hospital, Université Libre de Bruxelles, 1070 Brussels, Belgium.
Karim Zouaoui BoudjeltiaLaboratory of Experimental Medicine (ULB 222 Unit), CHU-Charleroi, ISPPC Hôpital Vésale, Université Libre de Bruxelles, 6110 Montigny-Le-Tilleul, Belgium.
Pierre Van AntwerpenRD3-Pharmacognosy, Bioanalysis and Drug Discovery, Faculty of Pharmacy, Université Libre de Bruxelles, 1050 Brussels, Belgium.ORCID 0000-0002-4934-8863
Université Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative modifications of HDLs and LDLs by myeloperoxidase (MPO) are regularly mentioned in the context of atherosclerosis. The enzyme adsorbs on protein moieties and locally produces oxidizing agents to modify specific residues on apolipoproteins A-1 and B-100. Oxidation of lipoproteins by MPO (Mox) leads to dysfunctional Mox-HDLs associated with cholesterol-efflux deficiency, and Mox-LDLs that are no more recognized by the LDL receptor and become proinflammatory. Several modification sites on apoA-1 and B-100 that are specific to MPO activity are described in the literature, which seem relevant in patients with cardiovascular risk. The most appropriate analytical method to assess these modifications is based on liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS). It enables the oxidized forms of apoA-1and apoB-100 to be quantified in serum, in parallel to a quantification of these apolipoproteins. Current standard methods to quantify apolipoproteins are based on immunoassays that are well standardized with good analytical performances despite the cost and the heterogeneity of the commercialized kits. Mass spectrometry can provide simultaneous measurements of quantity and quality of apolipoproteins, while being antibody-independent and directly detecting peptides carrying modifications for Mox-HDLs and Mox-LDLs. Therefore, mass spectrometry is a potential and reliable alternative for apolipoprotein quantitation.

Indexed as

ApolipoproteinsCardiovascular DiseasesChromatography, LiquidOxidation-ReductionTandem Mass SpectrometryApolipoproteinsapolipoproteinsLC-MS/MSlipoprotein qualityoxidationpeptide quantification

Identifiers

PMID34500696
PMCPMC8434463
OpenAlexW3196884381

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.