prikaz prve stranice dokumenta Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling
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Scientific paper - Original scientific paper
Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling
Cells, 8 (2019), 12; https://doi.org/10.3390/cells8121646
Posa, Francesca; Grab, Anna Luise; Martin, Volker; Hose, Dirk; Seckinger, Anja; Mori, Giorgio; Vukičević, Slobodan; Cavalcanti-Adam, Elisabetta Ada

Institutional repository: Dr Med - University of Zagreb School of Medicine Digital Repository

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Posa, F., Grab, A. L., Martin, V., Hose, D., Seckinger, A., Mori, G. ... Cavalcanti Adam, E. A. (2019). Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling. Cells, 8. (12). doi: 10.3390/cells8121646

Posa, Francesca, et al. "Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling." Cells, vol. 8, no. 12, 2019. https://doi.org/10.3390/cells8121646

Posa, Francesca, Anna Luise Grab, Volker Martin, Dirk Hose, Anja Seckinger, Giorgio Mori, Slobodan Vukičević and Elisabetta Ada Cavalcanti Adam. "Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling." Cells 8, no. 12 (2019). https://doi.org/10.3390/cells8121646

Posa, F., et al. (2019) 'Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling', Cells, 8(12). doi: 10.3390/cells8121646

Posa F, Grab AL, Martin V, Hose D, Seckinger A, Mori G, and sur.. Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling. Cells [Internet]. 2019 December 15 [cited 2024 May 10];8(12). doi: 10.3390/cells8121646

F. Posa, et al., "Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling", Cells, vol. 8, no. 12, December 2019. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:105:139774. [Accessed: 10 May 2024]

Metadata
Title (english)Copresentation of BMP-6 and RGD ligands enhances cell adhesion and BMP-mediated signaling
AuthorFrancesca Posa
AuthorAnna Luise Grab
AuthorVolker Martin
AuthorDirk Hose
AuthorAnja Seckinger
AuthorGiorgio Mori
AuthorSlobodan Vukičević
AuthorElisabetta Ada Cavalcanti-Adam
Author's institutionUniversity of Zagreb
School of Medicine
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract (english)
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.
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review
Publication versionPublished version
Journal titleCells
Numberingvol. 8, no. 12
p-ISSN2073-4409
DOIhttps://doi.org/10.3390/cells8121646
URN:NBNurn:nbn:hr:105:139774
Publication2019-12-15
Document URLhttp://doi.org/10.3390/cells8121646
Type of resourceText
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2024-03-28 10:36:24