| First Author | Emoto H | Year | 1997 |
| Journal | J Biol Chem | Volume | 272 |
| Issue | 37 | Pages | 23191-4 |
| PubMed ID | 9287324 | Mgi Jnum | J:42892 |
| Mgi Id | MGI:1096714 | Doi | 10.1074/jbc.272.37.23191 |
| Citation | Emoto H, et al. (1997) Structure and expression of human fibroblast growth factor-10. J Biol Chem 272(37):23191-4 |
| abstractText | We isolated the cDNA encoding a novel member of the human fibroblast growth factor (FGF) family from the lung. The cDNA encodes a protein of 208 amino acids with high sequence homology (95.6%) to rat FGF-10, indicating that the protein is human FGF-10. Human FGF-10 as well as rat FGF-10 has a hydrophobic amino terminus ( approximately 40 amino acids), which may serve as a signal sequence. The apparent evolutionary relationships of human FGFs indicate that FGF-10 is closest to FGF-7. Chromosomal localization of the human FGF-10 gene was examined by in situ hybridization. The gene was found to map to the 5p12-p13 region. Human FGF-10 (amino acids 40 to 208 with a methionine residue at the amino terminus) was produced in Escherichia coli and purified from the cell lysate. Recombinant human FGF-10 (approximately 19 kDa) showed mitogenic activity for fetal rat keratinizing epidermal cells, but essentially no activity for NIH/3T3 cells, fibroblasts. The specificity of mitogenic activity of FGF-10 is similar to that of FGF-7 but distinct from that of bFGF. In structure and biological activity, FGF-10 is similar to FGF-7. |
