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Title: Ligand-binding specificity of human fibroblast growth factor receptor-3 IIIc. Author: Lin HY, Kaplow J, Jaye M, Hayman MJ. Journal: FEBS Lett; 1997 Jul 14; 411(2-3):389-92. PubMed ID: 9271242. Abstract: Earlier studies indicated that human fibroblast growth factor receptor (FGFR)-3 IIIc was activated equally well by both FGF-1 and FGF-2. In contrast, murine FGFR-3 IIIc was preferentially activated by FGF-1. To address this issue, we determined the ligand-binding specificity of human FGFR-3 IIIc in comparison with human FGFR-1 IIIc. By equilibrium binding human FGFR-3 IIIc preferentially bound FGF-1 with high affinity, whereas FGFR-1 IIIc bound both FGF-1 and -2 with high affinity. By competition binding using FGF-1, -2, -4, or -6, FGF-1 competed more efficiently than the other FGFs. These results suggest that like the murine FGFR-3 III, FGF-1 is a preferred ligand for human FGFR-3 IIIc.[Abstract] [Full Text] [Related] [New Search]