FGF-10 Protein, Human

Fibroblast Growth Factor 10 (FGF-10), also known as Keratinocyte Growth Factor 2 (KGF-2), is a member of the fibroblast growth factor (FGF) family, specifically belonging to the FGF7 subfamily. Human FGF-10 is a 19 kDa protein composed of 208 amino acids, encoded by the FGF10 gene located on chromosome 5p13-p12. It was first isolated from human lung cDNA libraries by Emoto et al. in 1997 and subsequently characterized as a paracrine signaling molecule with structural homology to FGF-7 (KGF).

Unlike endocrine FGFs, FGF-10 functions as a paracrine signaling factor that requires heparan sulfate proteoglycans as essential co-factors for high-affinity binding to its cognate receptor. FGF-10 exhibits high specificity for the FGFR2-IIIb splice variant (also known as FGFR2b or K-sam), which is predominantly expressed in epithelial cells. This ligand-receptor interaction is critical for mediating mesenchymal-epithelial communication during development and tissue homeostasis.

Structurally, FGF-10 contains a conserved β-trefoil core domain characteristic of the FGF family, along with unique N-terminal and C-terminal extensions that influence its receptor binding specificity and biological activity. The protein is secreted through the classical endoplasmic reticulum-Golgi pathway and undergoes proteolytic processing to generate the mature, biologically active form.