Evidence map›Paper›PMID 30237127›Full record

ArticleRedox biology2018

Chlorination and oxidation of human plasma fibronectin by myeloperoxidase-derived oxidants, and its consequences for smooth muscle cell function.

Tina Nybo, Huan Cai, Christine Y Chuang, Luke F Gamon, Adelina Rogowska-Wrzesinska, Michael J Davies

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022
    Review
  14. Heme Peroxidases at Unperturbed and Inflamed Mucous Surfaces.Antioxidants (Basel, Switzerland) · 2021
    Review
  15. Myeloperoxidase Inhibitory and Antioxidant Activities of (Pharmaceuticals (Basel, Switzerland) · 2021
    Article
  16. Review
  17. Review
  18. The Dual Role of Myeloperoxidase in Immune Response.International journal of molecular sciences · 2020
    Review
  19. Review
  20. 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

6 authors at 2 institutions in 1 country.

Tina NyboDepartment of Biomedical Sciences, Panum Institute, University of Copenhagen, Copenhagen, Denmark.
Huan CaiDepartment of Biomedical Sciences, Panum Institute, University of Copenhagen, Copenhagen, Denmark.
Christine Y ChuangDepartment of Biomedical Sciences, Panum Institute, University of Copenhagen, Copenhagen, Denmark.
Luke F GamonDepartment of Biomedical Sciences, Panum Institute, University of Copenhagen, Copenhagen, Denmark.
Adelina Rogowska-WrzesinskaDepartment of Biochemistry and Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, Odense, Denmark.
Michael J DaviesDepartment of Biomedical Sciences, Panum Institute, University of Copenhagen, Copenhagen, Denmark. Electronic address: davies@sund.ku.dk.
University of Copenhagen · DKUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibronectin (FN) occurs as both a soluble form, in plasma and at sites of tissue injury, and a cellular form in tissue extracellular matrices (ECM). FN is critical to wound repair, ECM structure and assembly, cell adhesion and proliferation. FN is reported to play a critical role in the development, progression and stability of cardiovascular atherosclerotic lesions, with high FN levels associated with a thick fibrotic cap, stable disease and a low risk of rupture. Evidence has been presented for FN modification by inflammatory oxidants, and particularly myeloperoxidase (MPO)-derived species including hypochlorous acid (HOCl). The targets and consequences of FN modification are poorly understood. Here we show, using a newly-developed MS protocol, that HOCl and an enzymatic MPO system, generate site-specific dose-dependent Tyr chlorination and dichlorination (up to 16 of 100 residues modified), and oxidation of Trp (7 of 39 residues), Met (3 of 26) and His (1 of 55) within selected FN domains, and particularly the heparin- and cell-binding regions. These alterations increase FN binding to heparin-containing columns. Studies using primary human coronary artery smooth muscle cells (HCASMC) show that exposure to HOCl-modified FN, results in decreased adherence, increased proliferation and altered expression of genes involved in ECM synthesis and remodelling. These findings indicate that the presence of modified fibronectin may play a major role in the formation, development and stabilisation of fibrous caps in atherosclerotic lesions and may play a key role in the switching of quiescent contractile smooth muscle cells to a migratory, synthetic and proliferative phenotype.

Indexed as

Amino Acid SequenceCell AdhesionCell ProliferationCells, CulturedFibronectinsHalogenationHumansHypochlorous AcidMyocytes, Smooth MuscleOxidation-ReductionPeroxidaseFibronectinsHypochlorous AcidPeroxidase3-chlorotyrosineChlorinationExtracellular matrixFibronectinHypochlorous acidMyeloperoxidaseOxidationVascular smooth muscle cells

Identifiers

PMID30237127
PMCPMC6142189
OpenAlexW2889820585

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.