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  • Title: Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule.
    Author: Pierschbacher MD, Hayman EG, Ruoslahti E.
    Journal: Cell; 1981 Oct; 26(2 Pt 2):259-67. PubMed ID: 6174240.
    Abstract:
    Proteolytic fragments of human plasma fibronectin were used to identify monoclonal antibodies reacting with the various domains of fibronectin. One of these antibodies, which reacts with cell-attachment-promoting fragments of fibronectin, inhibits attachment of cells to fibronectin-coated surfaces. A cell-attachment-promoting, chymotryptic, 120 kilodalton fragment was cleaved further with pepsin into three main fragments. The smallest, 15 kilodalton fragment was purified by affinity chromatography on the cell-attachment-inhibiting antibody insolubilized on Sepharose. This fragment is active in promoting cell attachment but lacks the other known binding activities of fibronectin. It can be localized between the collagen-binding and heparin-binding domains, about 127 to 197 kilodaltons from the NH2 terminus of the polypeptide. These results show that the interaction of fibronectin with cells is restricted to a defined portion of the molecule and is independent of the direct involvement of the known affinities toward other macromolecules.
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