Motogenic sites in human fibronectin are masked by long range interactions.

Journal article

Fibronectin (FN) is a large extracellular matrix glycoprotein important for development and wound healing in vertebrates. Recent work has focused on the ability of FN fragments and embryonic or tumorigenic splicing variants to stimulate fibroblast migration into collagen gels. This activity has been localized to specific sites and is not exhibited by full-length FN. Here we show that an N-terminal FN fragment, spanning the migration stimulation sites and including the first three type III FN ...

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Authors: Vakonakis, I; Staunton, D; Ellis, I; Sarkies, P; Flanagan, A

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 284
• Issue: 23
• Pages: 15668-15675
• Publication date: 2009-06-01
• DOI: 10.1074/jbc.m109.003673
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Humans; Amino Acid Substitution; Kidney; Escherichia coli; Genetic Variation; Rats; Wound Healing; Protein Conformation; Pichia; Recombinant Proteins; Cell Line; Chromatography, Gel; Tendons; Collagen; Animals; Alternative Splicing; Cytokines; Models, Molecular; Magnetic Resonance Spectroscopy; Peptide Fragments; Tail; Fibronectins