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Fibroblast growth factor 2 (FGF-2), also known as basic fibroblast growth factor (bFGF), is a potent mitogenic and angiogenic signaling protein that belongs to the heparin-binding growth factor family (UniProt P09038). It exerts its biological effects by binding to and activating cell-surface fibroblast growth factor receptors (FGFRs), which in turn trigger several intracellular signaling cascades, including the RAS-MAPK, PI3K-AKT, and PLCγ pathways (PubMed: 28210162). These pathways are critical for normal physiological processes such as embryonic development, tissue repair, and wound healing. In various pathological conditions, particularly oncology, the dysregulation or overexpression of FGF-2 and its related proliferative pathways promotes tumor growth, survival, and neovascularization (PubMed: 25614001). Therapeutic strategies targeting this axis include the use of small-molecule tyrosine kinase inhibitors that block FGFR activity, as well as ligand-trapping molecules designed to sequester FGF-2 and prevent receptor activation. Clinical management of these therapies often involves monitoring for specific toxicities, such as hyperphosphatemia, which arise from the systemic inhibition of physiological FGF signaling (PubMed: 31101534).
Inhibition of FGF-2 signaling through competitive binding to FGFRs, sequestration of the FGF-2 ligand, or inhibition of FGFR tyrosine kinase activity.
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