Evidence map›Paper›PMID 27009190›Full record

ArticleOpen biology2016

Selectivity in glycosaminoglycan binding dictates the distribution and diffusion of fibroblast growth factors in the pericellular matrix.

Changye Sun, Marco Marcello, Yong Li, David Mason, Raphaël Lévy, David G Fernig

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  10. Achondroplasia: Development, pathogenesis, and therapy.Developmental dynamics : an official publication of the American Association of Anatomists · 2017
    Review
  11. Article
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 1 institution in 1 country.

Changye SunDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0001-8602-9629
Marco MarcelloCentre for Cell Imaging, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.
Yong LiDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0002-5594-4434
David MasonCentre for Cell Imaging, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0002-8773-5274
Raphaël LévyDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0001-5728-0531
David G FernigDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK dgfernig@liverpool.ac.uk.ORCID http://orcid.org/0000-0003-4875-4293
University of Liverpool · GB

Funding

Medical Research Council MR/K015931/1
6 · The paper itself

Abstract

The range of biological outcomes generated by many signalling proteins in development and homeostasis is increased by their interactions with glycosaminoglycans, particularly heparan sulfate (HS). This interaction controls the localization and movement of these signalling proteins, but whether such control depends on the specificity of the interactions is not known. We used five fibroblast growth factors with an N-terminal HaloTag (Halo-FGFs) for fluorescent labelling, with well-characterized and distinct HS-binding properties, and measured their binding and diffusion in pericellular matrix of fixed rat mammary 27 fibroblasts. Halo-FGF1, Halo-FGF2 and Halo-FGF6 bound to HS, whereas Halo-FGF10 also interacted with chondroitin sulfate/dermatan sulfate, and FGF20 did not bind detectably. The distribution of bound FGFs in the pericellular matrix was not homogeneous, and for FGF10 exhibited striking clusters. Fluorescence recovery after photobleaching showed that FGF2 and FGF6 diffused faster, whereas FGF1 diffused more slowly, and FGF10 was immobile. The results demonstrate that the specificity of the interactions of proteins with glycosaminoglycans controls their binding and diffusion. Moreover, cells regulate the spatial distribution of different protein-binding sites in glycosaminoglycans independently of each other, implying that the extracellular matrix has long-range structure.

Indexed as

AnimalsBinding SitesCell LineExtracellular MatrixFibroblast Growth FactorsFibroblastsHeparan SulfateMicroscopy, ConfocalOptical ImagingProtein TransportRatsFibroblast Growth FactorsHeparan Sulfateextracellular matrixfibroblast growth factorglycosaminoglycangrowth factor diffusionheparan sulfate

Identifiers

PMID27009190
PMCPMC4821244
OpenAlexW2307502073

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.