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Nanoscale Features of Fibronectin Fibrillogenesis Depend on Protein-Substrate Interaction and Cytoskeleton Structure

Institute of Polymer Research Dresden and Max Bergmann Center of Biomaterials Dresden, 01069 Dresden, Germany

Correspondence: Address reprint requests to Tilo Pompe, Insitute of Polymer Research Dresden and Max Bergmann Center of Biomaterials Dresden, Hohe Str. 6, 01069 Dresden, Germany. Tel.: 49-351-4658274; Fax: 49-351-4658533; E-mail: pompe-tilo{at}ipfdd.de.

Cell-reorganized fibronectin layers on polymer films providing a gradation of the binding strength between protein and substrate were analyzed by combined fluorescence and scanning force microscopy. The nanoscale fibronectin patterns exhibited paired parallel fibrils with characteristic spacings of 156, 233, 304, and 373 nm. These spacings depend on the interaction of fibronectin with the substrate: at enhanced fibronectin-substrate anchorage the cells form larger stress fibers, which are assembled by -actinin cross-linked pairs of actin filaments subunits at the focal adhesions. A ubiquitous repeating unit of 71 nm was found within these characteristic distances. We conclude that the dimensions of the actin stress fibers reflect the binding strength of fibronectin to the polymer substrate and act—in turn—as a template for the reorganization of fibronectin into surface-bound nanofibrils with characteristic spacings. This explanation was confirmed by data showing the -actinin/fibronectin colocalization.