Ligand binding properties of binary complexes of heparin and immunoglobulin-like modules of FGF receptor 2. Academic Article uri icon


  • Epithelial cells, which express FGFR2IIIb, bind and respond to FGF-1, FGF-7 and FGF-10, but not FGF-2. Stromal cells, which bind and respond to FGF-1 and FGF-2, but not FGF-7 and FGF-10, express FGFR2IIIc or FGFR1IIIc. Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity. In addition, FGF-2 and FGF-7 bound to both heparin-Ig module IIIb and IIIc complexes, but FGF-1 bound to neither Ig module III. The results show that in isolation both Ig modules II and III of FGFR2 can interact with heparin and that each exhibits a binding site for FGF. We suggest that the specificity of FGFR2IIIb and FGFR2IIIc is dependent on the cell membrane environment and heparin/heparan sulfate. Ig modules II and III cooperate both within monomers and across dimers with cellular heparan sulfates to confer cell type-dependent specificity of the FGFR complex for FGF.

published proceedings

  • Biochem Biophys Res Commun

altmetric score

  • 3

author list (cited authors)

  • Uematsu, F., Kan, M., Wang, F., Jang, J. H., Luo, Y., & McKeehan, W. L.

citation count

  • 27

complete list of authors

  • Uematsu, F||Kan, M||Wang, F||Jang, JH||Luo, Y||McKeehan, WL

publication date

  • January 2000