Evidence map›Paper›PMID 28382370›Full record

ArticleThrombosis and haemostasis2017

Impact of fibrinogen carbamylation on fibrin clot formation and stability.

Veronika Binder, Brith Bergum, Stéphane Jaisson, Philippe Gillery, Carsten Scavenius, Endy Spriet, Anne Karin Nyhaug, Helen M Roberts, Iain L C Chapple, Annelie Hellvard and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Thrombosis and haemostasis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Toward improved thrombolysis in ischemic stroke: targeting nonfibrin components.Research and practice in thrombosis and haemostasis · 2026
    Review
  4. Review
  5. Article
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  9. Review
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  13. Article
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  15. Thrombus composition and thrombolysis resistance in stroke.Research and practice in thrombosis and haemostasis · 2023
    Article
  16. Article
  17. Article
  18. Review
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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 6 institutions in 6 countries.

Veronika BinderVeronika Binder, Broegelmann Research Laboratory, Department of Clinical Science, University of Bergen, The Laboratory Building, 5th floor, Bergen, Norway, Tel.: +47 55 97 46 48, Fax: +47 55 97 58 17, E-mail: veronika.binder@k2.uib.no.
Brith Bergum
Stéphane Jaisson
Philippe Gillery
Carsten Scavenius
Endy Spriet
Anne Karin Nyhaug
Helen M Roberts
Iain L C Chapple
Annelie Hellvard
Nicolas Delaleu
Piotr Mydel
University of Bergen · NOCentre National de la Recherche Scientifique · FRImmune Regulation (United Kingdom) · GBJagiellonian University · PLAarhus University · DKSIB Swiss Institute of Bioinformatics · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbamylation is a non-enzymatic post-translational modification induced upon exposure of free amino groups to urea-derived cyanate leading to irreversible changes of protein charge, structure and function. Levels of carbamylated proteins increase significantly in chronic kidney disease and carbamylated albumin is considered as an important biomarker indicating mortality risk. High plasma concentrations and long half-life make fibrinogen a prime target for carbamylation. As aggregation and cross-linking of fibrin monomers rely on lysine residues, it is likely that carbamylation impacts fibrinogen processing. In this study we investigated carbamylation levels of fibrinogen from kidney disease patients as well as the impact of carbamylation on fibrinogen cleavage by thrombin, fibrin polymerisation and cross-linking in vitro. In conjunction, all these factors determine clot structure and stability and thus control biochemical and mechanical properties. LC-MS/MS analyses revealed significantly higher homocitrulline levels in patient fibrinogen than in fibrinogen isolated from control plasma. In our in vitro studies we found that although carbamylation does not affect thrombin cleavage per se, it alters fibrin polymerisation kinetics and impairs cross-linking and clot degradation. In addition, carbamylated fibrin clots had reduced fiber size and porosity associated with decreased mechanical stability. Using mass spectroscopy, we discovered that N-terminally carbamylated fibrinopeptide A was generated in this process and acted as a strong neutrophil chemoattractant potentially mediating recruitment of inflammatory cells to sites of fibrin(ogen) turnover. Taken together, carbamylation of fibrinogen seems to play a role in aberrant fibrin clot formation and might be involved in haemostatic disorders associated with chronic inflammatory diseases.

Indexed as

Blood CoagulationProtein Processing, Post-TranslationalChemotaxis, LeukocyteCitrullineCyanatesFactor XIIIaFibrinFibrinogenFibrinolysisFibrinopeptide AHumansKineticsNeutrophilsPolymerizationProtein ConformationProtein StabilityCitrullineCyanatesFactor XIIIaFibrinFibrinogenFibrinopeptide AhomocitrullineThrombinUreacarbamylationFibrinogenfibrin structure

Identifiers

PMID28382370
PMCPMC5442607
OpenAlexW2604369119

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Registered trials

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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.