Ligand-binding specificity of human fibroblast growth factor receptor-3 IIIc

Autor:	Michael Jaye, J. M. Kaplow, Hsien-Yi Lin, Michael J. Hayman
Rok vydání:	1997
Předmět:	musculoskeletal diseases animal structures Fibroblast Growth Factor 6 Blotting Western Fibroblast growth factor Biophysics Fibroblast Growth Factor 4 Gene Expression Ligands Biochemistry Binding Competitive Cell Line Structural Biology Proto-Oncogene Proteins Genetics Animals Humans Receptor Fibroblast Growth Factor Type 3 Receptor Fibroblast Growth Factor Type 1 Molecular Biology Ligand binding Chemistry Fibroblast growth factor receptor 2 Fibroblast growth factor receptor 1 Receptor Protein-Tyrosine Kinases Cell Biology Fibroblast growth factor receptor 4 Fibroblast growth factor receptor 3 Protein-Tyrosine Kinases Ligand (biochemistry) Molecular biology Receptors Fibroblast Growth Factor Fibroblast growth factor receptor Rats Fibroblast Growth Factors embryonic structures Fibroblast Growth Factor 1 Fibroblast Growth Factor 2 biological phenomena cell phenomena and immunity Protein Binding
Zdroj:	FEBS letters. 411(2-3)
ISSN:	0014-5793
Popis:	Earlier studies indicated that human fibroblast growth factor receptor (FGFR)-3IIIc was activated equally well by both FGF-1 and FGF-2. In contrast, murine FGFR-3IIIc was preferentially activated by FGF-1. To address this issue, we determined the ligand-binding specificity of human FGFR-3IIIc in comparison with human FGFR-1IIIc. By equilibrium binding human FGFR-3IIIc preferentially bound FGF-1 with high affinity, whereas FGFR-1IIIc 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-3III, FGF-1 is a preferred ligand for human FGFR-3IIIc.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e80f5e45af8ab8aabfe1b3a775f89b52 https://pubmed.ncbi.nlm.nih.gov/9271242 Zobrazit plný text záznamu Plný text