Evidence map›Paper›PMID 25433338›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2015

The α4β1 integrin and the EDA domain of fibronectin regulate a profibrotic phenotype in dermal fibroblasts.

Arti V Shinde, Rhiannon Kelsh, John H Peters, Kiyotoshi Sekiguchi, Livingston Van De Water, Paula J McKeown-Longo

Open access · greenAbstract read
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  7. Review
  8. Toll-like receptors and integrins crosstalk.Frontiers in immunology · 2024
    Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Poly(l-lactic acid) Scaffold Releasing an αACS applied bio materials · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Review
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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 2 countries.

Arti V ShindeCenter for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208, United States.
Rhiannon KelshCenter for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208, United States.
John H PetersVA Northern California Health Care System and Center for Musculoskeletal Health, Department of Internal Medicine, University of California - Davis School of Medicine, Sacramento, CA, United States.
Kiyotoshi SekiguchiDivision of Protein Chemistry, Institute for Protein Research, Osaka University, Osaka, Japan.
Livingston Van De WaterCenter for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208, United States.
Paula J McKeown-LongoCenter for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208, United States. Electronic address: mckeowp@mail.amc.edu.
Albany Medical Center Hospital · USProtein Research Foundation · JP

Funding

FIBRONECTIN POLYMERIZATION--EFFECTS ON CELL SIGNALINGR01CA069612 · NCI · ALBANY MEDICAL COLLEGE · PI MC KEOWN-LONGO, PAULA J · 1997 to 2009
$2.7M
MATRIX REGULATION OF CELL FUNCTION DURING WOUND HEALINGR01GM056442 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI VAN DE WATER, LIVINGSTON · 1997 to 2010
$2.7M
NCI NIH HHS CA 069612NCI NIH HHS R01 CA069612NIGMS NIH HHS GM056442NIGMS NIH HHS R01 GM056442
6 · The paper itself

Abstract

Prompt deposition of fibronectin-rich extracellular matrix is a critical feature of normal development and the host-response to injury. Fibronectin isoforms that include the EDA and EDB domains are prominent in these fibronectin matrices. We now report using human dermal fibroblast cultures that the EDA domain of fibronectin or EDA-derived peptides modeled after the C-C' loop promote stress fiber formation and myosin-light chain phosphorylation. These changes are accompanied by an increase in fibronectin synthesis and fibrillogenesis. These effects are blocked by pretreating cells with either siRNA or blocking antibody to the α4 integrin. Our data indicate that the interaction between the α4β1 integrin and the EDA domain of fibronectin helps to drive tissue fibrosis by promoting a contractile phenotype and an increase in fibronectin synthesis and deposition.

Indexed as

Binding SitesCell AdhesionCells, CulturedExtracellular Matrix ProteinsFibroblastsFibronectinsHumansIntegrin alpha4beta1LungMyosin Light ChainsPhenotypeProtein Structure, TertiarySkinStress FibersExtracellular Matrix ProteinsFibronectinsFN1 protein, humanIntegrin alpha4beta1Myosin Light ChainsContractilityFibronectinFibrosisRho kinaseStress fibersα4β1 integrin

Identifiers

PMID25433338
PMCPMC4657864
OpenAlexW2003709426

What OpenQuestion holds

Textmetadata
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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.