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


Journal

Acta biomaterialia
ISSN: 1878-7568
Titre abrégé: Acta Biomater
Pays: England
ID NLM: 101233144

Informations de publication

Date de publication:
15 09 2020
Historique:
received: 17 03 2020
revised: 06 07 2020
accepted: 08 07 2020
pubmed: 17 7 2020
medline: 15 5 2021
entrez: 17 7 2020
Statut: ppublish

Résumé

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 β

Identifiants

pubmed: 32673751
pii: S1742-7061(20)30400-1
doi: 10.1016/j.actbio.2020.07.015
pii:
doi:

Substances chimiques

Bone Morphogenetic Protein 2 0
Ligands 0
Peptides, Cyclic 0
cyclic arginine-glycine-aspartic acid peptide 0
Heparitin Sulfate 9050-30-0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

90-103

Informations de copyright

Copyright © 2020. Published by Elsevier Ltd.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Julius Sefkow-Werner (J)

Grenoble Institute of Technology, Université Grenoble Alpes, LMGP UMR 5628, Grenoble, France; CEA, CNRS, UGA, BRM ERL 5000, Grenoble, France.

Paul Machillot (P)

Grenoble Institute of Technology, Université Grenoble Alpes, LMGP UMR 5628, Grenoble, France; CEA, CNRS, UGA, BRM ERL 5000, Grenoble, France.

Adria Sales (A)

Grenoble Institute of Technology, Université Grenoble Alpes, LMGP UMR 5628, Grenoble, France; CEA, CNRS, UGA, BRM ERL 5000, Grenoble, France.

Elaine Castro-Ramirez (E)

Grenoble Institute of Technology, Université Grenoble Alpes, LMGP UMR 5628, Grenoble, France; CEA, CNRS, UGA, BRM ERL 5000, Grenoble, France.

Melissa Degardin (M)

Université Grenoble Alpes, CNRS, DCM, Grenoble, France.

Didier Boturyn (D)

Université Grenoble Alpes, CNRS, DCM, Grenoble, France.

Elisabetta Ada Cavalcanti-Adam (EA)

University of Heidelberg, Department of Biophysical Chemistry, Heidelberg, Germany.

Corinne Albiges-Rizo (C)

Institut Albert Bonniot, Université Grenoble Alpes, INSERM U1209, CNRS UMR5309, Grenoble, France.

Catherine Picart (C)

Grenoble Institute of Technology, Université Grenoble Alpes, LMGP UMR 5628, Grenoble, France; CEA, CNRS, UGA, BRM ERL 5000, Grenoble, France; CEA, direction of fundamental research, interdisciplinary research institute of Grenoble (IRIG), FRE CNRS, Grenoble, France. Electronic address: catherine.picart@cea.fr.

Elisa Migliorini (E)

Grenoble Institute of Technology, Université Grenoble Alpes, LMGP UMR 5628, Grenoble, France; CEA, CNRS, UGA, BRM ERL 5000, Grenoble, France. Electronic address: elisa.migliorini@grenoble-inp.fr.

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