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Migration Stimulating Factor (MSF) is a genetically truncated isoform of fibronectin (Fn). MSF is a potent stimulator of fibroblast migration, whereas full length Fn is devoid of motogenic activity. MSF and Fn contain four IGD motifs, located in the 3rd, 5th, 7th and 9th type I modules; these modules are referred to as (3)FnI, (5)FnI, (7)FnI and (9)FnI, respectively. We have previously reported that mutation of IGD motifs in modules (7)FnI and (9)FnI of MSF is sufficient to completely abolish the motogenic response of target adult skin fibroblasts. We now report that the IGD sequences in (3)FnI and (5)FnI are also capable of exhibiting motogenic activity when present within fragments of MSF. When present within (1-5)FnI, these sequences require the presence of serum or vitronectin for their motogenic activity to be manifest, whereas the IGD sequences in (7)FnI and (9)FnI are bioactive in the absence of serum factors. All MSF and IGD-containing peptides stimulated the phosphorylation of the integrin binding protein focal adhesion kinase (FAK) but did not necessarily affect migration. These results suggest that steric hindrance determines the motogenic activity of MSF and Fn, and that both molecules contain cryptic bioactive fragments.

Original publication

DOI

10.1016/j.yexcr.2010.04.003

Type

Journal article

Journal

Exp Cell Res

Publication Date

10/09/2010

Volume

316

Pages

2465 - 2476

Keywords

Adult, Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Movement, Cells, Cultured, Cytokines, Dose-Response Relationship, Drug, Drosophila melanogaster, Fibroblasts, Fibronectins, Humans, Male, Molecular Motor Proteins, Molecular Sequence Data, Peptide Fragments, Rats, Sequence Homology, Amino Acid