| First Author | Lin HY | Year | 1997 |
| Journal | FEBS Lett | Volume | 411 |
| Issue | 2-3 | Pages | 389-92 |
| PubMed ID | 9271242 | Mgi Jnum | J:42128 |
| Mgi Id | MGI:1095214 | Doi | 10.1016/s0014-5793(97)00739-4 |
| Citation | Lin HY, et al. (1997) Ligand-binding specificity of human fibroblast growth factor receptor-3 IIIc. FEBS Lett 411(2-3):389-92 |
| abstractText | 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. |
