display of cell surface sites for fibronectin assembly is modulated by cell adherence to 1f3 and c-terminal modules of fibronectin显示细胞表面网站纤连蛋白组装是由细胞调制坚持1 f3和纤连蛋白c端模块的.pdfVIP

Display of Cell Surface Sites for Fibronectin Assembly Is Modulated by Cell Adherence to 1F3 and C-Terminal Modules of Fibronectin 1,2,3. 1,2,3. 1,2,3¤ 1,2,3 4 Jielin Xu , Eunnyung Bae , Qinghong Zhang , Douglas S. Annis , Harold P. Erickson , Deane F. Mosher1,2,3* 1 Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin, United States of America, 2 Department of Pathology and Laboratory Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America, 3 Department of Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America, 4 Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, United States of America Abstract 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 7F3-10F3). Interactions of adherent cells with regions of adsorbed fibronectin other than modules 7F3-10F3, 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 7F3-10F3 were tested for effects on fibronectin assembly by adherent fibronectin-null fibroblasts. Pieces as large as one comprising modules 2F3-14F3, which include the heparin-binding and cell adhesion domains, were not effective in supporting fibronectin assembly. Addition of module 1F3 or the C-terminal modules to mod