Evidence map›Paper›PMID 25697357›Full record

ArticleThe Journal of biological chemistry2015

Myeloperoxidase-dependent lipid peroxidation promotes the oxidative modification of cytosolic proteins in phagocytic neutrophils.

Rachel P Wilkie-Grantham, Nicholas J Magon, D Tim Harwood, Anthony J Kettle, Margreet C Vissers, Christine C Winterbourn, Mark B Hampton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Post-translational modifications on the metal-sequestering protein calprotectin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Transcription Factor ArcA ModulatesFrontiers in microbiology · 2019
    Article
  8. Article
  9. Article
  10. Expression, Purification, and Antimicrobial Activity of S100A12.Journal of visualized experiments : JoVE · 2017
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. 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

7 authors at 1 institution in 1 country.

Rachel P Wilkie-GranthamFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand.
Nicholas J MagonFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand.
D Tim HarwoodFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand.
Anthony J KettleFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand.
Margreet C VissersFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand.
Christine C WinterbournFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand.
Mark B HamptonFrom the Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch 8140, New Zealand mark.hampton@otago.ac.nz.
University of Otago · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phagocytic neutrophils generate reactive oxygen species to kill microbes. Oxidant generation occurs within an intracellular phagosome, but diffusible species can react with the neutrophil and surrounding tissue. To investigate the extent of oxidative modification, we assessed the carbonylation of cytosolic proteins in phagocytic neutrophils. A 4-fold increase in protein carbonylation was measured within 15 min of initiating phagocytosis. Carbonylation was dependent on NADPH oxidase and myeloperoxidase activity and was inhibited by butylated hydroxytoluene and Trolox, indicating a role for myeloperoxidase-dependent lipid peroxidation. Proteomic analysis of target proteins revealed significant carbonylation of the S100A9 subunit of calprotectin, a truncated form of Hsp70, actin, and hemoglobin from contaminating erythrocytes. The addition of the reactive aldehyde 4-hydroxynonenal (HNE) caused carbonylation, and HNE-glutathione adducts were detected in the cytosol of phagocytic neutrophils. The post-translational modification of neutrophil proteins will influence the functioning and fate of these immune cells in the period following phagocytic activation, and provides a marker of neutrophil activation during infection and inflammation.

Indexed as

Lipid PeroxidationAldehydesButylated HydroxytolueneCalgranulin BChromansCytosolElectrophoresis, Gel, Two-DimensionalHumansImmunoblottingLeukocyte L1 Antigen ComplexNADPH OxidasesNeutrophilsOxidation-ReductionPeroxidasePhagocytosisProtein Carbonylation4-hydroxy-2-nonenal6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acidAldehydesButylated HydroxytolueneCalgranulin BChromansLeukocyte L1 Antigen ComplexNADPH OxidasesPeroxidaseProteome4-HydroxynonenalcalprotectinLipid PeroxidationMyeloperoxidaseNeutrophilNOX2Oxidative BurstOxidative StressOxygen RadicalsPhagocytosisProtein CarbonylationS100 Proteins

Identifiers

PMID25697357
PMCPMC4392286
OpenAlexW2076041072

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.