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Ligand‐binding specificity of human fibroblast growth factor receptor‐3 IIIc
Author(s) -
Lin Hsien-Yi,
Kaplow June,
Jaye Michael,
Hayman Michael J.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00739-4
Subject(s) - fibroblast growth factor receptor , fibroblast growth factor , receptor , ligand (biochemistry) , fibroblast growth factor receptor 1 , fibroblast growth factor receptor 4 , chemistry , biology , biochemistry
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.