Evidence map›Paper›PMID 39384749›Full record

ArticleNature communications2024

Strain-dependent glutathionylation of fibronectin fibers impacts mechano-chemical behavior and primes an integrin switch.

Wei Li, Leandro Moretti, Xinya Su, Chiuan-Ren Yeh, Matthew P Torres, Thomas H Barker

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. 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

6 authors.

Wei LiSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, USA.
Leandro MorettiDepartment of Biomedical Engineering, Schools of Engineering and Medicine, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0002-7374-8074
Xinya SuSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, USA.
Chiuan-Ren YehDepartment of Biomedical Engineering, Schools of Engineering and Medicine, University of Virginia, Charlottesville, VA, USA.
Matthew P TorresSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, USA.
Thomas H BarkerDepartment of Biomedical Engineering, Schools of Engineering and Medicine, University of Virginia, Charlottesville, VA, USA. thomas.barker@virginia.edu.ORCID 0000-0002-3218-8111

Funding

Mechanosensors that detect and treat Lung FibrosisR01HL132585 · NHLBI · UNIVERSITY OF VIRGINIA · PI BARKER, THOMAS HARRISON · 2015 to 2019
$3.3M
Targeting the alpha v integrin mechanotransduction axis in IPFR01HL127283 · NHLBI · UNIVERSITY OF VIRGINIA · PI BARKER, THOMAS HARRISON · 2015 to 2018
$1.6M
NHLBI NIH HHS R01 HL127283NHLBI NIH HHS R01 HL132585NSF | Directorate for Mathematical & Physical Sciences | Division of Mathematical Sciences (DMS) DMS1764406Simons Foundation SFARI-594594U.S. Department of Health & Human Services | NIH | NIH Office of the Director (OD) R01HL132585
6 · The paper itself

Abstract

The extracellular matrix (ECM) is a protein polymer network that physically supports cells within a tissue. It acts as an important physical and biochemical stimulus directing cell behaviors. For fibronectin (Fn), a predominant component of the ECM, these physical and biochemical activities are inextricably linked as physical forces trigger conformational changes that impact its biochemical activity. Here, we analyze whether oxidative post-translational modifications, specifically glutathionylation, alter Fn's mechano-chemical characteristics through stretch-dependent protein modification. ECM post-translational modifications represent a potential for time- or stimulus-dependent changes in ECM structure-function relationships that could persist over time with potentially significant impacts on cell and tissue behaviors. In this study, we show evidence that glutathionylation of Fn ECM fibers is stretch-dependent and alters Fn fiber mechanical properties with implications on the selectivity of engaging integrin receptors. These data demonstrate the existence of multimodal post-translational modification mechanisms within the ECM with high relevance to the microenvironmental regulation of downstream cell behaviors.

Indexed as

Extracellular MatrixFibronectinsGlutathioneIntegrinsProtein Processing, Post-TranslationalAnimalsHumansFibronectinsGlutathioneIntegrins

Identifiers

PMID39384749
PMCPMC11479631

What Socratic 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 Socratic graph.