Picture of a sphere with binary code

Making Strathclyde research discoverable to the world...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. It exposes Strathclyde's world leading Open Access research to many of the world's leading resource discovery tools, and from there onto the screens of researchers around the world.

Explore Strathclyde Open Access research content

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

Beattie, James and Kreiner, M. and Allan, G.J. and Flint, D.J. and Domingues, Diana and van der Walle, Christopher F. (2009) IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin. Biochemical and Biophysical Research Communications, 381 (4). pp. 572-576. ISSN 1090-2104

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

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.