Angiogenesis

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Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3, and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).

FGFR-3 participates in a diverse array of biological processes, including cell growth, differentiation, and migration. Activating mutations in FGFR-3 are associated with multiple myeloma, cervical carcinoma, and bladder cancer and it represents a potential target for therapy (6).

1. Powers, C.J. et al. (2000) Endocr Relat Cancer 7, 165-97.
2. Reilly, J.F. et al. (2000) J Biol Chem 275, 7771-8.
3. Mohammadi, M. et al. (1996) Mol Cell Biol 16, 977-89.
4. Mohammadi, M. et al. (1991) Mol Cell Biol 11, 5068-78.
5. Larsson, H. et al. (1999) J Biol Chem 274, 25726-34.
6. Knowles, M.A. (2008) Future Oncol 4, 71-83.

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FGF Receptor 3 Antibody

©1999-2012 Cell Signaling Technology, Inc.

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