IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin

James Beattie, M. Kreiner, G.J. Allan, D.J. Flint, Diana Domingues, Christopher F. van der Walle

Research output: Contribution to journalArticle

12 Citations (Scopus)


We have used Surface Plasmon Resonance (SPR) - based biosensor technology to investigate the interaction of the six high affinity insulin-like growth factor binding proteins (IGFBP 1-6) with the cell binding domain (CBD) of fibronectin. Using a biotinylated derivative of the ninth and tenth TypeIII domains of FN (9-10FNIII), we show that IGFBP-3 and -5 bind to FN-CBD. We show that this binding is inhibited by IGF-I and that, for IGFBP-5, binding occurs through the C-terminal heparin binding domain of the protein. Using site-directed mutagenesis of 9-10FNIII, we show both the 'synergy' and RGD sites within these FN domains are required for maximum binding of both IGFBPs. We discuss the possible biological consequences of our results.
Original languageEnglish
Pages (from-to)572-576
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - Feb 2009


  • fibronectin
  • insulin-like growth factor binding protein
  • surface plasmon resonance
  • pharmacology

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