Abstract
The fibroblast growth factor receptor (FGFR) can be activated through direct interactions with various fibroblast growth factors or through a number of cell adhesion molecules, including the neural cell adhesion molecule (NCAM). We produced recombinant proteins comprising the ligand-binding immunoglobulin-like modules 2 and 3 of FGFR1b, FGFR1c, FGFR2b, FGFR2c, FGFR3b, FGFR3c, and FGFR4, and found that all FGFR isoforms, except for FGFR4, interacted with NCAM. The binding affinity of NCAM-FGFR interactions was considerably higher for splice variant 'b' than for splice variant 'c'. We suggest that the expression pattern of various FGFR isoforms determines the cell context-specific effects of NCAM signaling through FGFR.
Original language | English |
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Journal | NeuroReport |
Volume | 22 |
Issue number | 15 |
Pages (from-to) | 727-732 |
Number of pages | 6 |
ISSN | 0959-4965 |
DOIs | |
Publication status | Published - 26 Oct 2011 |
Keywords
- Animals
- Male
- Neural Cell Adhesion Molecules
- Protein Isoforms
- Rats
- Rats, Wistar
- Receptors, Fibroblast Growth Factor
- Recombinant Proteins
- Signal Transduction
- Surface Plasmon Resonance