Evidence map›Paper›PMID 31242089›Full record

ArticleMolecular biology of the cell2019

Fibronectin matrix as a scaffold for procollagen proteinase binding and collagen processing.

Jared T Saunders, Jean E Schwarzbauer

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

49 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Interspecies interactions in dual, fibrous gels enable control of gel structure and rheology.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Fibroblast integrin α11β1 is a collagen assembly receptor in mechanoregulated fibrillar adhesions.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  18. Article
  19. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
    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

2 authors at 1 institution in 1 country.

Jared T SaundersDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014.
Jean E SchwarzbauerDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014.
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Fibronectin-dependent mechanisms governing the assembly of a definitive extracellular matrixR01AR073236 · NIAMS · PRINCETON UNIVERSITY · PI SCHWARZBAUER, JEAN E · 2018 to 2022
$1.7M
Molecular Analysis of Extracellular Matrix AssemblyR01CA160611 · NCI · PRINCETON UNIVERSITY · PI SCHWARZBAUER, JEAN E · 2012 to 2017
$1.6M
NCI NIH HHS R01 CA160611NIAMS NIH HHS R01 AR073236NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

The extracellular matrix (ECM) proteins fibronectin (FN) and type I collagen (collagen I) are codistributed in many tissues, and collagens have been shown to depend on an FN matrix for fibrillogenesis. Microscopic analysis of a fibroblast ECM showed colocalization of procollagen I with FN fibrils, and proteolytic cleavage of procollagen to initiate fibril formation was significantly reduced with inhibition of FN matrix assembly. We examined the role of FN matrix in procollagen processing by the C-propeptide proteinase bone morphogenetic protein 1 (BMP-1). We found that BMP-1 binds to a cell-assembled ECM in a dose-dependent manner and that, like procollagen, BMP-1 colocalizes with FN fibrils in the matrix microenvironment. Binding studies with FN fragments identified a binding site in FN's primary heparin-binding domain. In solution, BMP-1-FN interactions and BMP-1 cleavage of procollagen I were both enhanced by the presence of heparin, suggesting a role for heparin in complex formation during proteolysis. Indeed, addition of heparin enhanced the rate of procollagen cleavage by matrix-bound BMP-1. Our results show that matrix localization of this proteinase facilitates the initiation of collagen assembly and suggest a model in which FN matrix and associated heparan sulfate act as a scaffold to organize enzyme and substrate for procollagen processing.

Indexed as

Binding SitesBone Morphogenetic Protein 1CollagenExtracellular MatrixExtracellular Matrix ProteinsFibroblastsFibronectinsHumansPrimary Cell CultureProcollagenProtein BindingProteolysisBone Morphogenetic Protein 1CollagenExtracellular Matrix ProteinsFibronectinsFN1 protein, humanProcollagen

Identifiers

PMID31242089
PMCPMC6743462
OpenAlexW2953530466

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.