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Fibronectin activity on substrates with controlled OH density
Author(s) -
Gugutkov Dencho,
Altankov George,
Rodríguez Hernández José Carlos,
Monleón Pradas Manuel,
Salmerón Sánchez Manuel
Publication year - 2010
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.32374
Subject(s) - fibronectin , adhesion , materials science , substrate (aquarium) , cell adhesion , adsorption , morphology (biology) , protein adsorption , polymer chemistry , biophysics , chemical engineering , extracellular matrix , polymer , chemistry , biochemistry , organic chemistry , composite material , oceanography , biology , engineering , genetics , geology
Adhesion of human fibroblast to a family of fibronectin (FN) coated model substrates consisting of copolymers of ethyl acrylate and hydroxyl ethylacrylate in different ratios to obtain a controlled surface density of OH groups was investigated. Cell adhesion and spreading surprisingly decreased as the fraction of OH groups on the surface increased. AFM studies of FN conformation revealed formation of a protein network on the more hydrophobic surfaces. The density of this network diminished as the fraction of OH groups in the sample increased, up to a maximal OH concentration at which, instead of the network, only FN aggregates were observed. The kinetics of network development was followed at different adsorption times. Immunofluorescence for vinculin revealed the formation of well‐developed focal adhesion complexes on the more hydrophobic surface (similar to the control glass), which became less defined as the fraction of OH groups increased. Thus, the efficiency of cell adhesion is enhanced by the formation of FN networks on the substrate, directly revealing the importance of the adsorbed protein conformation for cell adhesion. However, cell‐dependent reorganization of substrate‐associated FN, which usually takes place on more hydrophilic substrates (as do at the control glass slides), was not observed in this system, suggesting the increased strength of protein‐to‐substrate interaction. Instead, the late FN matrix formation—after 3 days of culture—was again better pronounced on the more hydrophobic substrates and decreased as the fraction of OH groups increase, which is in a good agreement with the results for overall cell morphology and focal adhesion formation. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res, 2010