IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin.
Biochem Biophys Res Commun
; 381(4): 572-6, 2009 Apr 17.
Article
em En
| MEDLINE
| ID: mdl-19236847
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 ((9-10)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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Fibronectinas
/
Proteína 5 de Ligação a Fator de Crescimento Semelhante à Insulina
/
Proteína 3 de Ligação a Fator de Crescimento Semelhante à Insulina
Tipo de estudo:
Risk_factors_studies
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Reino Unido