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  Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling

Posa, F., Grab, A.-L., Martin, V., Hose, D., Seckinger, A., Mori, G., et al. (2019). Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling. Cells, 8: 1646, pp. 1-16. doi:10.3390/cells8121646.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-6704-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-6705-2
Genre: Journal Article

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 Creators:
Posa, Francesca1, 2, Author              
Grab, Anna-Luise2, 3, Author              
Martin, Volker2, 3, Author              
Hose, Dirk, Author
Seckinger, Anja, Author
Mori, Giorgio, Author
Vukicevic, Slobodan, Author
Cavalcanti-Adam, Elisabetta Ada2, 3, Author              
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              
3Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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Free keywords: integrin ligands; bone morphogenetic protein 6; surface copresentation; myotube formation; BMP/Smad signaling
 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.

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Language(s): eng - English
 Dates: 2019-11-182019-12-132019-12-15
 Publication Status: Published online
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.3390/cells8121646
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Title: Cells
Source Genre: Journal
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Publ. Info: Basel : MDPI
Pages: - Volume / Issue: 8 Sequence Number: 1646 Start / End Page: 1 - 16 Identifier: ISSN: 2073-4409