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Structure and expression of human fibroblast growth factor-10.

The Journal of biological chemistry (1997-09-12)
H Emoto, S Tagashira, M G Mattei, M Yamasaki, G Hashimoto, T Katsumata, T Negoro, M Nakatsuka, D Birnbaum, F Coulier, N Itoh
ZUSAMMENFASSUNG

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.

MATERIALIEN
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Produktbeschreibung

Sigma-Aldrich
Fibroblast Growth Factor-10 human, >97% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture