Evidence map›Paper›PMID 31847477›Full record

ArticleCells2019

Copresentation of BMP-6 and RGD Ligands Enhances Cell Adhesion and BMP-Mediated Signaling.

Francesca Posa, Anna Luise Grab, Volker Martin, Dirk Hose, Anja Seckinger, Giorgio Mori, Slobodan Vukicevic, Elisabetta Ada Cavalcanti-Adam

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

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

8 authors at 4 institutions in 3 countries.

Francesca PosaDepartment of Cellular Biophysics, Max Planck Institute for Medical Research, Jahnstr. 29, 69120 Heidelberg, Germany.ORCID 0000-0001-8099-3505
Anna Luise GrabDepartment of Cellular Biophysics, Max Planck Institute for Medical Research, Jahnstr. 29, 69120 Heidelberg, Germany.
Volker MartinDepartment of Cellular Biophysics, Max Planck Institute for Medical Research, Jahnstr. 29, 69120 Heidelberg, Germany.
Dirk HoseLaboratory for Myeloma Research and Medical Clinic V, University Hospital Heidelberg, Im Neuenheimer Feld 410, 69120 Heidelberg, Germany.
Anja SeckingerLaboratory for Myeloma Research and Medical Clinic V, University Hospital Heidelberg, Im Neuenheimer Feld 410, 69120 Heidelberg, Germany.
Giorgio MoriDepartment of Clinical and Experimental Medicine, University of Foggia, via L. Pinto, 71122 Foggia, Italy.ORCID 0000-0001-6731-0247
Slobodan VukicevicLaboratory for Mineralized Tissues, Center for Translational and Clinical Research, School of Medicine, University of Zagreb, Šalata 11, 10000 Zagreb, Croatia.ORCID 0000-0003-4076-0285
Elisabetta Ada Cavalcanti-AdamDepartment of Cellular Biophysics, Max Planck Institute for Medical Research, Jahnstr. 29, 69120 Heidelberg, Germany.ORCID 0000-0003-0243-1552
Heidelberg University · DEUniversity of Foggia · ITEuropean Molecular Biology Organization · DEUniversity of Zagreb · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report on the covalent immobilization of bone morphogenetic protein 6 (BMP-6) and its co-presentation with integrin ligands on a nanopatterned platform to study cell adhesion and signaling responses which regulate the transdifferentiation of myoblasts into osteogenic cells. To immobilize BMP-6, the heterobifunctional linker MU-NHS is coupled to amine residues of the growth factor; this prevents its internalization while ensuring that its biological activity is maintained. Additionally, to allow cells to adhere to such platform and study signaling events arising from the contact to the surface, we used click-chemistry to immobilize cyclic-RGD carrying an azido group reacting with PEG-alkyne spacers via copper-catalyzed 1,3-dipolar cycloaddition. We show that the copresentation of BMP-6 and RGD favors focal adhesion formation and promotes Smad 1/5/8 phosphorylation. When presented in low amounts, BMP-6 added to culture media of cells adhering to the RGD ligands is less effective than BMP-6 immobilized on the surfaces in inducing Smad complex activation and in inhibiting myotube formation. Our results suggest that a local control of ligand density and cell signaling is crucial for modulating cell response.

Indexed as

AnimalsBone Morphogenetic Protein 6Cell AdhesionCell DifferentiationCell LineGoldImmobilized ProteinsIntegrinsLigandsMetal NanoparticlesMiceMyoblastsOligopeptidesOsteogenesisPhosphorylationProtein Bindingarginyl-glycyl-aspartic acidBone Morphogenetic Protein 6GoldImmobilized ProteinsIntegrinsLigandsOligopeptidesSmad ProteinsTransforming Growth Factor betaBMP/Smad signalingbone morphogenetic protein 6integrin ligandsmyotube formationsurface copresentation

Identifiers

PMID31847477
PMCPMC6953040
OpenAlexW2996315077

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.