IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin |
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Authors: | James Beattie Michaela Kreiner Gordon J Allan David J Flint Diana Domingues Christopher F van der Walle |
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Institution: | Strathclyde Institute of Pharmacy and Biomedical Sciences (SIBPS), University of Strathclyde, 27 Taylor St., Glasgow G4 0NR, United Kingdom |
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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. |
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Keywords: | Fibronectin Insulin-like growth factor binding protein Surface plasmon resonance |
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