Evidence map›Paper›PMID 28811641›Full record

ArticleScientific reports2017

Joint inflammation related citrullination of functional arginines in extracellular proteins.

Kalle H Sipilä, Vipin Ranga, Pekka Rappu, Markku Mali, Laura Pirilä, Ilona Heino, Johanna Jokinen, Jarmo Käpylä, Mark S Johnson, Jyrki Heino

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Citrullination of matrisomal proteins in health and diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  5. Article
  6. BP180/Collagen XVII: A Molecular View.International journal of molecular sciences · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Citrullination of fibronectin alters integrin clustering and focal adhesion stability promoting stromal cell invasion.Matrix biology : journal of the International Society for Matrix Biology · 2019
    Article
  13. Article
  14. Review
  15. Dynamic Substrates for Cell Biology.Current opinion in colloid & interface science · 2018
    Article
  16. 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

10 authors at 2 institutions in 1 country.

Kalle H SipiläDepartment of Biochemistry, University of Turku, Turku, Finland.
Vipin RangaStructural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.
Pekka RappuDepartment of Biochemistry, University of Turku, Turku, Finland.ORCID 0000-0002-5068-2842
Markku MaliTurku University Hospital, Division of Medicine, Department of Rheumatology, and University of Turku, Turku, Finland.
Laura PiriläTurku University Hospital, Division of Medicine, Department of Rheumatology, and University of Turku, Turku, Finland.
Ilona HeinoDepartment of Biochemistry, University of Turku, Turku, Finland.
Johanna JokinenDepartment of Biochemistry, University of Turku, Turku, Finland.
Jarmo KäpyläDepartment of Biochemistry, University of Turku, Turku, Finland.
Mark S JohnsonStructural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.
Jyrki HeinoDepartment of Biochemistry, University of Turku, Turku, Finland. jyrki.heino@utu.fi.
University of Turku · FIÅbo Akademi University · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report the extent, specific sites and structural requirements of joint inflammation related citrullination in extracellular proteins. A total of 40 synovial fluid samples derived from chronically inflamed human joints were analysed by heparin-agarose fractionation and LC-MS/MS. Citrullination of 55 arginines in extracellular proteins was detected. Importantly, 20% of the sites have a characterized function related to the hallmarks of destructive joint inflammation. E.g. four arginine residues, shown here to be citrullinated, are also affected by mutations in inherited diseases causing haemolysis or blood clotting dysfunction. Citrullination of integrin ligands was selected for further studies since fibronectin R234 in isoDGR was among the most frequently citrullinated arginines in synovial fluid. Assays with synovial fibroblasts and integrin αVβ3 indicated decreased affinity to the enzymatically citrullinated integrin binding sites. To conclude, our data indicate that in inflamed joints extensive citrullination affects the functional arginine residues in extracellular proteins.

Indexed as

CitrullinationAmino Acid MotifsAmino Acid SequenceArginineArthritisChronic DiseaseCitrullineExtracellular Matrix ProteinsExtracellular SpaceHumansModels, MolecularProtein ConformationProtein Interaction Domains and MotifsStructure-Activity RelationshipSynovial FluidArginineCitrullineExtracellular Matrix Proteins

Identifiers

PMID28811641
PMCPMC5557964
OpenAlexW2745290353

What Socratic 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 Socratic graph.