Evidence map›Paper›PMID 8567726›Full record

ArticleThe Journal of cell biology1996

Beta 1 integrin-dependent and -independent polymerization of fibronectin.

K Wennerberg, L Lohikangas, D Gullberg, M Pfaff, S Johansson, R Fässler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

113 citing papers in PubMed, 289 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Fibronectin matrix assembly at a glance.Journal of cell science · 2025
    Review
  5. Article
  6. Fibroblast integrin α11β1 is a collagen assembly receptor in mechanoregulated fibrillar adhesions.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

53 more citing papers are in PubMed but not listed here.

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.

K WennerbergDepartment of Medical and Physiological Chemistry, Biomedical Center, Uppsala, Sweden.
L Lohikangas
D Gullberg
M Pfaff
S Johansson
R Fässler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mouse cell line GD25, which lacks expression of the beta 1 family of integrin heterodimers due to disruption of the beta 1 integrin subunit gene, was used for expression of full-length cDNA coding for splice variant A of the mouse beta 1 integrin subunit. In a stably transformed clone (GD25-beta 1A), the expressed protein was found to form functional heterodimeric receptors together with the subunits alpha 3, alpha 5, and alpha 6. Both GD25 and GD25-beta 1A attached to fibronectin and formed focal contacts which contained alpha v beta 3, but no detectable alpha 5 beta 1A. The presence of GRGDS peptide allowed alpha 5 beta 1A to locate to focal contacts of GD25-beta 1A cultured on fibronectin, while the beta 1-null GD25 cells were unable to attach under these conditions. Affinity chromatography revealed that alpha 5 beta 1A and alpha v beta 3 could bind to a large cell-binding fragment of fibronectin. alpha 5 beta 1A strongly promoted polymerization of fibronectin into a fibrillar network on top of the cells. Whereas little alpha v beta 3 was colocalized with the fibronectin fibrils in GD25-beta 1A cells, this integrin was able to support fibronectin fibril polymerization in GD25 cells. However, the alpha v beta 3-induced polymerization was less efficient and occurred mainly in dense cultures of the GD25 cells. Thus, while both alpha 5 beta 1A and alpha v beta 3 are able to support adhesion to fibronectin, alpha v beta 3 dominates in the formation of focal contacts, and alpha 5 beta 1A has a prime function in fibronectin matrix assembly. This is the first report on fibronectin matrix assembly in the absence of beta 1 integrins.

Indexed as

AnimalsAntigens, CDBlotting, NorthernCell AdhesionCell LineDNA, ComplementaryFibronectinsFlow CytometryFluorescent Antibody TechniqueGenetic VariationHumansIntegrin alpha5Integrin beta1IntegrinsMicePolymersAntigens, CDDNA, ComplementaryFibronectinsIntegrin alpha5Integrin beta1IntegrinsPolymersRecombinant Proteins

Identifiers

PMID8567726
PMCPMC2120698
OpenAlexW2066665315

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.