Evidence map›Paper›PMID 16567085›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2006

The N-terminal 70-kDa fragment of fibronectin binds to cell surface fibronectin assembly sites in the absence of intact fibronectin.

Bianca R Tomasini-Johansson, Douglas S Annis, Deane F Mosher

Open access · greenAbstract read
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

40 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  7. The interactions between integrin αInternational journal of biological sciences · 2022
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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 1 country.

Bianca R Tomasini-JohanssonDepartment of Medicine and Biomolecular Chemistry, University of Wisconsin, Madison, 4285 Medical Sciences Center, 1300 University Ave., Madison, WI 53706, USA. brtomasini@wisc.edu
Douglas S Annis
Deane F Mosher
University of Wisconsin–Madison · US

Funding

STUDIES OF FIBRONECTIN AND RELATED GLYCOPROTEINSR01HL021644 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MOSHER, DEANE FREMONT · 1985 to 2010
$3.2M
NHLBI NIH HHS HL21644NHLBI NIH HHS R01 HL021644
6 · The paper itself

Abstract

Binding of the N-terminal 70-kDa (70K) fragment of fibronectin to fibroblasts blocks assembly of intact fibronectin and is an accurate indicator of the ability of various agents to enhance or inhibit fibronectin assembly. Such binding is widely thought to be to already assembled fibronectin. We evaluated this hypothesis with fibronectin-null mouse fibroblasts plated on laminin-1 in the absence of intact fibronectin. As a proteolytic fragment or recombinant protein, 70K bound fibronectin-null cells specifically in linear arrays that extended outwards from the periphery of spread cells. At early time points, these arrays were similar to those formed by intact fibronectin. 70K arrays formed within 5 min following ligand addition at concentrations as low as 5 nM, indicating rapid and high affinity binding. Bound 70K was extractable with Triton X-100 or deoxycholate but became insoluble when cross-linked with a membrane-impermeable agent into large SDS-stable complexes. Intact fibronectin, in contrast, became progressively non-extractable in the absence of cross-linking. The detergent-resistant arrays of cross-linked 70K localized to tips of cellular extensions and partially overlapped with alpha6 and beta1 integrin subunits at the base of the extensions. alpha5 did not localize with 70K arrays, but became progressively co-localized with assemblies of intact fibronectin over time. These results support a model in which the 70-kDa region of fibronectin binds to linearly arrayed cell surface molecules of adherent cells to initiate assembly, display of the arrays is controlled by the integrin that mediates adhesion, and fibronectin-binding integrins promote fibronectin-fibronectin interactions during progression of assembly.

Indexed as

AnimalsBinding SitesCell MembraneCells, CulturedCross-Linking ReagentsDetergentsFibronectinsFluorescein-5-isothiocyanateFluorescent DyesIntegrinsMiceMice, KnockoutMicroscopy, FluorescenceModels, BiologicalMolecular WeightPeptide FragmentsCross-Linking ReagentsDetergentsFibronectinsFluorescein-5-isothiocyanateFluorescent DyesIntegrinsPeptide Fragments

Identifiers

PMID16567085
PMCPMC1482735
OpenAlexW1964568800

What OpenQuestion holds

Textmetadata
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.