Picture of a black hole

Strathclyde Open Access research that creates ripples...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of research papers by University of Strathclyde researchers, including by Strathclyde physicists involved in observing gravitational waves and black hole mergers as part of the Laser Interferometer Gravitational-Wave Observatory (LIGO) - but also other internationally significant research from the Department of Physics. Discover why Strathclyde's physics research is making ripples...

Strathprints also exposes world leading research from the Faculties of Science, Engineering, Humanities & Social Sciences, and from the Strathclyde Business School.

Discover more...

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.