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J. Biol. Chem., Vol. 282, Issue 49, 35530-35535, December 7, 2007

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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, and Iain D. Campbell¹

From the Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom, Unit of Cell and Molecular Biology, University of Dundee, Dundee DD1 4HR, Scotland, United Kingdom, and ^¶School of Biological Sciences, University of Portsmouth, Portsmouth PO1 2DY, United Kingdom

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.

Received for publication, September 10, 2007 , and in revised form, October 3, 2007.

^* This work was supported by the Wellcome Trust, the Biotechnology and Biological Sciences Research Council, and the Engineering and Physical Sciences Research Council. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Backbone NH and H assignments have been deposited in the BioMagRes-Bank under accession number 15447.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ To whom correspondence should be addressed: Dept. of Biochemistry, University of Oxford, South Parks Rd., Oxford, Oxfordshire OX1 3QU, UK. Tel.: 44-1865-275346; Fax: 44-1865-275253; E-mail: iain.campbell{at}bioch.ox.ac.uk.

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