Fibronectin fibril pattern displays the force balance of cell-matrix adhesion.
Formation of fibrillar patterns of fibronectin on polymer substrates with gradated physicochemical surface properties was analysed during early stages of endothelial cell adhesion. Fibronectin was pre-adsorbed onto three maleic anhydride copolymer thin films with distinct differences in the protein adsorption strength as verified by heteroexchange experiments. The evolved micrometer scale fibrillar patterns of fibronectin on the compared polymer surfaces were characterized after 50 min of cellular reorganization by an auto-correlation analysis using fluorescence microscopy data. Statistical analysis revealed a decrease of the typical spacings of the fibronectin fibrils from 2.6 to 1.8 mum with decreasing fibronectin adsorption strength to the substrate. Size and density of focal adhesions correlated with this dependence of the fibronectin fibril pattern. From these data a model was developed relating the fibronectin fibril pattern to the fibronectin-substrate adsorption strength through the cytoskeletal force regulation mechanism of the cell.
Pompe
Tilo
T
Leibniz Institute of Polymer Research Dresden, Max Bergmann Center of Biomaterials Dresden, Hohe Strasse 6, 01069 Dresden, Germany. pompe-tilo@ipfdd.de
Keller
Kristin
K
Mitdank
Claudia
C
Werner
Carsten
C
D000268:Adhesiveness; D001665:Binding Sites; D002448:Cell Adhesion / Q000502:physiology*; D002478:Cells, Cultured; D003198:Computer Simulation; D042783:Endothelial Cells / Q000502:physiology* / Q000648:ultrastructure*; D005109:Extracellular Matrix / Q000502:physiology* / Q000648:ultrastructure*; D005353:Fibronectins / Q000378:metabolism* / Q000648:ultrastructure*; D006801:Humans; D007090:Image Interpretation, Computer-Assisted; D008954:Models, Biological; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical
D005353:Fibronectins