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  Heparan sulfate co-immobilized with cRGD ligands and BMP2 on biomimetic platforms promotes BMP2-mediated osteogenic differentiation

Sefkow-Werner, J., Machillot, P., Sales, A., Castro-Ramirez, E., Degardin, M., Boturyn, D., et al. (2020). Heparan sulfate co-immobilized with cRGD ligands and BMP2 on biomimetic platforms promotes BMP2-mediated osteogenic differentiation. Acta Biomaterialia, 1-12. doi:10.1016/j.actbio.2020.07.015.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-CF84-C Version Permalink: http://hdl.handle.net/21.11116/0000-0006-CF85-B
Genre: Journal Article

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 Creators:
Sefkow-Werner, Julius, Author
Machillot, Paul, Author
Sales, Adria, Author
Castro-Ramirez, Elaine, Author
Degardin, Melissa, Author
Boturyn, Didier, Author
Cavalcanti-Adam, Elisabetta Ada1, 2, Author              
Albiges-Rizo, Corinne, Author
Picart, Catherine, Author
Migliorini, Elisa, Author
Affiliations:
1Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              
2Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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Free keywords: Biomimetic approach ; BMP2 ; Heparan sulfate ; Integrins ; Osteogenic differentiation ; Cell adhesion
 Abstract: The chemical and physical properties of the extracellular matrix (ECM) are known to be fundamental for regulating growth factor bioactivity. The role of heparan sulfate (HS), a glycosaminoglycan, and of cell adhesion proteins (containing the cyclic RGD (cRGD) ligands) on bone morphogenetic protein 2 (BMP2)-mediated osteogenic differentiation has not been fully explored. In particular, it is not known whether and how their effects can be potentiated when they are presented in controlled close proximity, as in the ECM. Here, we developed streptavidin platforms to mimic selective aspects of the in vivo presentation of cRGD, HS and BMP2, with a nanoscale-control of their surface density and orientation to study cell adhesion and osteogenic differentiation. We showed that whereas a controlled increase in cRGD surface concentration upregulated BMP2 signaling due to β3 integrin recruitment, silencing either β1 or β3 integrins negatively affected BMP2-mediated phosphorylation of SMAD1/5/9 and alkaline phosphatase expression. Furthermore, the presence of adsorbed BMP2 promoted cellular adhesion at very low cRGD concentrations. Finally, we proved that HS co-immobilized with cRGD both sustained BMP2 signaling and enhanced osteogenic differentiation compared to BMP2 directly immobilized on streptavidin, even with a low cRGD surface concentration. Altogether, our results show that HS facilitated and sustained the synergy between BMP2 and integrin pathways and that the co-immobilization of HS and cRGD peptides optimised BMP2-mediated osteogenic differentiation.

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Language(s): eng - English
 Dates: 2020-07-062020-03-172020-07-082020-07-13
 Publication Status: Published online
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.actbio.2020.07.015
 Degree: -

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Title: Acta Biomaterialia
  Other : Acta Biomater.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 1 - 12 Identifier: ISSN: 1742-7061
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017060