The role of the fibronectin IGD motif in stimulating fibroblast migration

Christopher J. Millard, Ian R. Ellis, Andrew R. Pickford, Ana M. Schor, Seth L. Schor, Iain D. Campbell

    Research output: Contribution to journalArticlepeer-review

    29 Citations (Scopus)

    Abstract

    The motogenic activity of migration-stimulating factor, a truncated isoform of fibronectin (FN), has been attributed to the IGD motifs present in its FN type 1 modules. The structure-function relationship of various recombinant IGD-containing FN fragments is now investigated. Their structure is assessed by solution state NMR and their motogenic ability tested on fibroblasts. Even conservative mutations in the IGD motif are inactive or have severely reduced potency, while the structure remains essentially the same. A fragment with two IGD motifs is 100 times more active than a fragment with one and up to 106 times more than synthetic tetrapeptides. The wide range of potency in different contexts is discussed in terms of cryptic FN sites and cooperativity. These results give new insight into the stimulation of fibroblast migration by IGD motifs in FN.
    Original languageEnglish
    Pages (from-to)35530-35535
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume282
    Issue number49
    DOIs
    Publication statusPublished - 7 Dec 2007

    Keywords

    • BINDING-SITE
    • MODULE PAIR
    • PLASMA FIBRONECTIN
    • GELATIN-BINDING
    • CELL-ADHESION
    • MATRIX
    • RGD
    • IDENTIFICATION
    • FIBRILLOGENESIS
    • SEQUENCE

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