| First Author | Beattie J | Year | 2009 |
| Journal | Biochem Biophys Res Commun | Volume | 381 |
| Issue | 4 | Pages | 572-6 |
| PubMed ID | 19236847 | Mgi Jnum | J:147385 |
| Mgi Id | MGI:3840412 | Doi | 10.1016/j.bbrc.2009.02.088 |
| Citation | Beattie J, et al. (2009) IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin. Biochem Biophys Res Commun 381(4):572-6 |
| abstractText | 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 ((9-10)FNIII), 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 (9-10)FNIII, 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. |
