Evidence map›Paper›PMID 27808176›Full record

ArticleScientific reports2016

Sulfated hyaluronan alters fibronectin matrix assembly and promotes osteogenic differentiation of human bone marrow stromal cells.

Sarah Vogel, Simon Arnoldini, Stephanie Möller, Matthias Schnabelrauch, Ute Hempel

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

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  12. Heparin-fibronectin interactions in the development of extracellular matrix insolubility.Matrix biology : journal of the International Society for Matrix Biology · 2018
    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

5 authors at 3 institutions in 2 countries.

Sarah VogelInstitute of Physiological Chemistry, Carl Gustav Carus Faculty of Medicine, Technische Universität Dresden, Fiedlerstrasse 42, 01307 Dresden, Germany.
Simon ArnoldiniLaboratory of Applied Mechanobiology, Department of Health Science and Technology, ETH Zurich, Vladimir-Prelog-Weg 4, 8093 Zurich, Switzerland.
Stephanie MöllerBiomaterials Department, INNOVENT e. V., Pruessingstrasse 27B, 07745 Jena, Germany.
Matthias SchnabelrauchBiomaterials Department, INNOVENT e. V., Pruessingstrasse 27B, 07745 Jena, Germany.
Ute HempelInstitute of Physiological Chemistry, Carl Gustav Carus Faculty of Medicine, Technische Universität Dresden, Fiedlerstrasse 42, 01307 Dresden, Germany.
Innovent · DETU Dresden · DEETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular matrix (ECM) composition and structural integrity is one of many factors that influence cellular differentiation. Fibronectin (FN) which is in many tissues the most abundant ECM protein forms a unique fibrillary network. FN homes several binding sites for sulfated glycosaminoglycans (sGAG), such as heparin (Hep), which was previously shown to influence FN conformation and protein binding. Synthetically sulfated hyaluronan derivatives (sHA) can serve as model molecules with a well characterized sulfation pattern to study sGAG-FN interaction. Here is shown that the low-sulfated sHA (sHA1) interacts with FN and influences fibril assembly. The interaction of FN fibrils with sHA1 and Hep, but not with non-sulfated HA was visualized by immunofluorescent co-staining. FRET analysis of FN confirmed the presence of more extended fibrils in human bone marrow stromal cells (hBMSC)-derived ECM in response to sHA1 and Hep. Although both sHA1 and Hep affected FN conformation, exclusively sHA1 increased FN protein level and led to thinner fibrils. Further, only sHA1 had a pro-osteogenic effect and enhanced the activity of tissue non-specific alkaline phosphatase. We hypothesize that the sHA1-triggered change in FN assembly influences the entire ECM network and could be the underlying mechanism for the pro-osteogenic effect of sHA1 on hBMSC.

Indexed as

Alkaline PhosphataseBone Marrow CellsCell DifferentiationCells, CulturedExtracellular MatrixFibronectinsFluorescence Resonance Energy TransferGlycosaminoglycansHeparinHumansHyaluronic AcidMesenchymal Stem CellsMicroscopy, FluorescenceOsteogenesisProtein BindingProtein ConformationAlkaline PhosphataseFibronectinsGlycosaminoglycansHeparinHyaluronic AcidSulfates

Identifiers

PMID27808176
PMCPMC5093463
OpenAlexW2547934565

What OpenQuestion holds

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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.