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Background  Fibronectin-null cells assemble soluble fibronectin shortly after adherence to a substrate coated with intact fibronectin but not when adherent to the cell-binding domain of fibronectin (modules  7 F3- 10 F3). Interactions of adherent cells with regions of adsorbed fibronectin other than modules  7 F3- 10 F3, therefore, are required for early display of the cell surface sites that initiate and direct fibronectin assembly.    Methodology/Principal Findings  To identify these regions, coatings of proteolytically derived or recombinant pieces of fibronectin containing modules in addition to  7 F3- 10 F3 were tested for effects on fibronectin assembly by adherent fibronectin-null fibroblasts. Pieces as large as one comprising modules  2 F3- 14 F3, which include the heparin-binding and cell adhesion domains, were not effective in supporting fibronectin assembly. Addition of module  1 F3 or the C-terminal modules to modules  2 F3- 14 F3 resulted in some activity, and addition of both  1 F3 and the C-terminal modules resulted in a construct,  1 F3-C, that best mimicked the activity of a coating of intact fibronectin. Constructs  1 F3-C V0,  1 F3-C V64, and  1 F3-C Δ(V 15 F3 10 F1) were all able to support fibronectin assembly, suggesting that  1 F3 through  11 F1 and/or  12 F1 were important for activity. Coatings in which the active parts of  1 F3-C were present in different proteins were much less active than intact  1 F3-C.    Conclusions  These results suggest that  1 F3 acts together with C-terminal modules to induce display of fibronectin assembly sites on adherent cells.

Display of Cell Surface Sites for Fibronectin Assembly Is Modulated by Cell Adherence to 1F3 and C-Terminal Modules of Fibronectin