Evidence map›Paper›PMID 31436263›Full record

ArticleBiomaterials science2019

Fibrillar fibronectin plays a key role as nucleator of collagen I polymerization during macromolecular crowding-enhanced matrix assembly.

Jenna Graham, Michael Raghunath, Viola Vogel

Open access · hybridAbstract read
In one paragraph

Article in Biomaterials science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

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  11. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
    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

3 authors at 1 institution in 2 countries.

Jenna GrahamDepartment of Health Sciences and Technology, ETH Zürich, CH-8093 Zürich, Switzerland. viola.vogel@hest.ethz.ch.ORCID http://orcid.org/0000-0003-4491-9425
Michael RaghunathZHAW School of Life Sciences and Facility Management, Institute for Chemistry and Biotechnology, Center for Cell Biology and Tissue Engineering, CH-8820 Wädenswil, Switzerland.ORCID http://orcid.org/0000-0002-2138-6614
Viola VogelDepartment of Health Sciences and Technology, ETH Zürich, CH-8093 Zürich, Switzerland. viola.vogel@hest.ethz.ch.ORCID http://orcid.org/0000-0003-2898-7671
ETH Zurich · CH

Funding

The Role of Physical Cues in Collective Cell InvasionU54CA210173 · NCI · JOHNS HOPKINS UNIVERSITY · PI WIRTZ, DENIS · 2016 to 2020
$9.9M
T32: Predoctoral and Postdoctoral Training Program in Nanotechnology for Cancer ResearchT32CA153952 · NCI · JOHNS HOPKINS UNIVERSITY · PI Denis Wirtz · 2015 to 2026
$3.5M
T-32 NIH Postdoctoral Training Program in Nanotechnology for Cancer Medicine NTCMT32CA130840 · NCI · JOHNS HOPKINS UNIVERSITY · PI WIRTZ, DENIS · 2008 to 2012
$1.2M
NCI NIH HHS T32 CA130840NCI NIH HHS T32 CA153952NCI NIH HHS U54 CA210173
6 · The paper itself

Abstract

Macromolecular crowding is used by tissue engineers to accelerate extracellular matrix assembly in vitro, however, most mechanistic studies focus on the impact of crowding on collagen fiber assembly and largely ignore the highly abundant provisional matrix protein fibronectin. We show that the accelerated collagen I assembly as induced by the neutral crowding molecule Ficoll is regulated by cell access to fibronectin. Ficoll treatment leads to significant increases in the amount of surface adherent fibronectin, which can readily be harvested by cells to speed up fibrillogenesis. FRET studies reveal that Ficoll crowding also upregulates the total amount of fibronectin fibers in a low-tension state through upregulating fibronectin assembly. Since un-stretched fibronectin fibers have more collagen binding sites to nucleate the onset of collagen fibrillogenesis, our data suggest that the Ficoll-induced upregulation of low-tension fibronectin fibers contributes to enhanced collagen assembly in crowded conditions. In contrast, chemical cross-linking of fibronectin to the glass substrate prior to cell seeding prevents early force mediated fibronectin harvesting from the substrate and suppresses upregulation of collagen I assembly in the presence of Ficoll, even though the crowded environment is known to drive enzymatic cleavage of procollagen and collagen fiber formation. To show that our findings can be exploited for tissue engineering applications, we demonstrate that the addition of supplemental fibronectin in the form of an adsorbed coating markedly improves the speed of tissue formation under crowding conditions.

Indexed as

Collagen Type IExtracellular MatrixFibronectinsHumansMacromolecular SubstancesPolymerizationTissue EngineeringCollagen Type IFibronectinsMacromolecular Substances

Identifiers

PMID31436263
PMCPMC6810780
OpenAlexW2967374206

What OpenQuestion holds

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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.