Special Issue "Advanced Biointerface for Controlled Cell-Material Interactions"

Guest Editor
Prof. Dr. Maryam Tabrizian
Department of Biomedical Engineering, Faculty of Dentistry; Affiliations: Centre for Biorecognition and Biosensors (Director) and McGill Institute for Advanced Materials, Duff Medical Science Building, Room 313, 3775 University Street, Montreal (Qc), Canada
Website: http://www.bmed.mcgill.ca/tabrizian
E-Mail:
Interests: cell-biomaterial interactions; LbL self-assembly systems; nanostructured platforms for gene/protein therapy and tissue engineering; nanostructured interface and microfluidic systems by surface molecular engineering; nanolithography and nanopatterning for biorecognition systems; real-time monitoring of cellular activities; characterization of biomaterials debris in biological tissues; polymer synthesis and characterization; advanced surface technologies

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Title: Influence of the Material-Driven Fibronectin fibrillogenesis on Osteoblast Behavior
Authors: Patricia Rico, Cristina González-García, José Ballester-Beltran, Virginia Llopis and Manuel Salmerón Sánchez
Affiliation: Center for Biomaterials and Tissue Engineering, Universidad Politécnica de Valencia, Spain; E-Mail: masalsan@fis.upv.es (M.S.S.)
Abstract: Cells assemble fibronectin (FN) into fibrillar networks through an integrin-mediated process that leads to the unfolding of the globular FN molecule, exposing domains not previously available that activate intracellular signalling complexes. We have recently shown that simple FN adsorption onto poly(ethyl acrylate) surfaces triggered FN organization into a fibrillar network via interactions in the amino-terminal 70 kDa fragment, which is involved in the formation of cell-mediated FN fibrils. Here, we demonstrate that the substrate-assembled FN network exhibits significantly enhanced biological activities compared to control FN molecules adsorbed onto substrates (e.g. control glass) that do not promote FN fibrillogenesis. FN adsorption on PEA from solutions of increasing concentration provide a set of protein topologies on the material surface: from isolated molecules to assembled fibrils, on which we followed focal adhesion formation and F-actin cytoskeleton development during osteoblast adhesion. The availability of cell adhesion domains after adsorption was quantified making use of monoclonal antibodies directed to the 9-10^th domains of the FN molecule, and was better on the material-assembled FN. To gain insights into the mechanisms controlling the cellular responses to material-driven FN networks, we examined binding of α₅β₁ integrin to the adsorbed FN by Immunofluorescence following crosslinking of bound integrins to FN and extraction of cellular components. Also, FAK phosphorylation a critical signal related to cell signalling was enhanced on the material-assembled FN.