Evidence map›Paper›PMID 27512953›Full record

ArticleCell death & disease2016

Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps.

Krisztián Csomós, Endre Kristóf, Bernadett Jakob, István Csomós, György Kovács, Omri Rotem, Judit Hodrea, Zsuzsa Bagoly, Laszlo Muszbek, Zoltán Balajthy and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 25% 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, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  6. Review
  7. Review
  8. Transglutaminase 1: Emerging Functions beyond Skin.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Neutrophil extracellular traps in chronic lung disease: implications for pathogenesis and therapy.European respiratory review : an official journal of the European Respiratory Society · 2022
    Review
  16. Review
  17. Fungal-Induced Programmed Cell Death.Journal of fungi (Basel, Switzerland) · 2021
    Review
  18. Article
  19. Review
  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

12 authors at 2 institutions in 1 country.

Krisztián CsomósDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Endre KristófDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Bernadett JakobDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
István CsomósDepartment of Biophysics and Cell Biology, University of Debrecen, Debrecen, Hungary.
György KovácsDepartment of Computer Graphics and Image Processing, University of Debrecen, Debrecen, Hungary.
Omri RotemDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Judit HodreaDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Zsuzsa BagolyDivision of Clinical Laboratory Science, University of Debrecen, Debrecen, Hungary.
Laszlo MuszbekDivision of Clinical Laboratory Science, University of Debrecen, Debrecen, Hungary.
Zoltán BalajthyDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Éva CsőszDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
László FésüsDepartment of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
University of Debrecen · HUHungarian Academy of Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neutrophil extracellular trap (NET) ejected from activated dying neutrophils is a highly ordered structure of DNA and selected proteins capable to eliminate pathogenic microorganisms. Biochemical determinants of the non-randomly formed stable NETs have not been revealed so far. Studying the formation of human NETs we have observed that polyamines were incorporated into the NET. Inhibition of myeloperoxidase, which is essential for NET formation and can generate reactive chlorinated polyamines through hypochlorous acid, decreased polyamine incorporation. Addition of exogenous primary amines that similarly to polyamines inhibit reactions catalyzed by the protein cross-linker transglutaminases (TGases) has similar effect. Proteomic analysis of the highly reproducible pattern of NET components revealed cross-linking of NET proteins through chlorinated polyamines and ɛ(γ-glutamyl)lysine as well as bis-γ-glutamyl polyamine bonds catalyzed by the TGases detected in neutrophils. Competitive inhibition of protein cross-linking by monoamines disturbed the cross-linking pattern of NET proteins, which resulted in the loss of the ordered structure of the NET and significantly reduced capacity to trap bacteria. Our findings provide explanation of how NETs are formed in a reproducible and ordered manner to efficiently neutralize microorganisms at the first defense line of the innate immune system.

Indexed as

HalogenationCross-Linking ReagentsExtracellular TrapsHumansNeutrophilsPolyaminesProteinsProteomicsStaphylococcus aureusTransglutaminasesCross-Linking ReagentsPolyaminesProteinsTransglutaminases

Identifiers

PMID27512953
PMCPMC5108309
OpenAlexW2515426563

What OpenQuestion holds

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LicenceCC BY
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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.