Evidence map›Paper›PMID 26893379›Full record

ArticleThe Journal of biological chemistry2016

Fibromodulin Interacts with Collagen Cross-linking Sites and Activates Lysyl Oxidase.

Sebastian Kalamajski, Dominique Bihan, Arkadiusz Bonna, Kristofer Rubin, Richard W Farndale

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Bone matrix proteins: regulators of skeletal remodeling and repair.Journal of bone and mineral metabolism · 2026
    Review
  3. Article
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  5. Article
  6. Article
  7. Article
  8. Review
  9. Recombinant lysyl oxidase effects on embryonic tendon cell phenotype and behavior.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
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  18. Article
  19. Review
  20. Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022
    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

5 authors at 2 institutions in 2 countries.

Sebastian KalamajskiFrom the Department of Laboratory Medical Sciences, Lund University, Medicon Village 406-3, 22363 Lund, Sweden and sebastian.kalamajski@med.lu.se.ORCID http://orcid.org/0000-0002-6600-9302
Dominique Bihanthe Department of Biochemistry, Downing Site, University of Cambridge, Cambridge CB2 1QW, United Kingdom.
Arkadiusz Bonnathe Department of Biochemistry, Downing Site, University of Cambridge, Cambridge CB2 1QW, United Kingdom.
Kristofer RubinFrom the Department of Laboratory Medical Sciences, Lund University, Medicon Village 406-3, 22363 Lund, Sweden and.
Richard W Farndalethe Department of Biochemistry, Downing Site, University of Cambridge, Cambridge CB2 1QW, United Kingdom rwf10@cam.ac.uk.
University of Cambridge · GBLund University · SE

Funding

British Heart Foundation RG/09/003/27122British Heart Foundation RG/15/4/31268Medical Research Council G0400701Wellcome Trust 094470/Z/10/Z
6 · The paper itself

Abstract

The hallmark of fibrotic disorders is a highly cross-linked and dense collagen matrix, a property driven by the oxidative action of lysyl oxidase. Other fibrosis-associated proteins also contribute to the final collagen matrix properties, one of which is fibromodulin. Its interactions with collagen affect collagen cross-linking, packing, and fibril diameter. We investigated the possibility that a specific relationship exists between fibromodulin and lysyl oxidase, potentially imparting a specific collagen matrix phenotype. We mapped the fibromodulin-collagen interaction sites using the collagen II and III Toolkit peptide libraries. Fibromodulin interacted with the peptides containing the known collagen cross-linking sites and the MMP-1 cleavage site in collagens I and II. Interestingly, the interaction sites are closely aligned within the quarter-staggered collagen fibril, suggesting a multivalent interaction between fibromodulin and several collagen helices. Furthermore, we detected an interaction between fibromodulin and lysyl oxidase (a major collagen cross-linking enzyme) and mapped the interaction site to 12 N-terminal amino acids on fibromodulin. This interaction also increases the activity of lysyl oxidase. Together, the data suggest a fibromodulin-modulated collagen cross-linking mechanism where fibromodulin binds to a specific part of the collagen domain and also forms a complex with lysyl oxidase, targeting the enzyme toward specific cross-linking sites.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCell LineCollagenEnzyme ActivationExtracellular Matrix ProteinsFibromodulinGene DeletionHumansMiceMice, KnockoutMolecular Sequence DataProtein Interaction MapsProtein-Lysine 6-OxidaseProteoglycansCollagenExtracellular Matrix ProteinsFibromodulinFMOD protein, humanFmod protein, mouseProtein-Lysine 6-OxidaseProteoglycanscollagencross-linkingextracellular matrixfibromodulinlysyl oxidasesmall leucine-rich proteoglycan (SLRP)

Identifiers

PMID26893379
PMCPMC4825002
OpenAlexW2285460751

What OpenQuestion holds

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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 OpenQuestion graph.