Characterization of Recombinant Human Fibroblast Growth Factor (FGF)-10 Reveals Functional Similarities with Keratinocyte Growth Factor (FGF-7)
| Autor: | Makoto Igarashi, Stuart A. Aaronson, Paul W. Finch |
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| Rok vydání: | 1998 |
| Předmět: |
DNA
Complementary Fibroblast Growth Factor 7 Molecular Sequence Data Filaggrin Proteins Biology Fibroblast growth factor Biochemistry 3T3 cells Cell Line Mice chemistry.chemical_compound Escherichia coli medicine Animals Humans Receptors Growth Factor Amino Acid Sequence Cloning Molecular Receptor Fibroblast Growth Factor Type 2 Growth Substances Molecular Biology Mice Inbred BALB C FGF10 Base Sequence Heparin Fibroblast growth factor receptor 2 3T3 Cells Cell Biology Fibroblast growth factor receptor 4 Fibroblast growth factor receptor 3 Receptors Fibroblast Growth Factor Molecular biology Recombinant Proteins Fibroblast Growth Factors medicine.anatomical_structure chemistry Keratinocyte growth factor Mitogens Fibroblast Growth Factor 10 |
| Zdroj: | Journal of Biological Chemistry. 273:13230-13235 |
| ISSN: | 0021-9258 |
| Popis: | A newly identified member of the fibroblast growth factor (FGF) family, designated FGF-10, is expressed during development and preferentially in adult lung. The predicted FGF-10 protein is most related to keratinocyte growth factor (KGF, or FGF-7). The latter is unique among FGFs in that it binds and signals only through the FGF receptor (FGFR2b) isoform KGF receptor (KGFR) expressed specifically by epithelial cells. In order to examine the biological and biochemical properties of human FGF-10, we isolated the cDNA and expressed its encoded protein in bacteria. The recombinant protein (rFGF-10) was a potent mitogen for Balb/MK mouse epidermal keratinocytes with activity detectable at 0.1 nM and maximal at around 5 nM. Within this concentration range, FGF-10 did not stimulate DNA synthesis in NIH/3T3 mouse fibroblasts. rFGF-10 bound the KGFR with high affinity comparable to that of KGF, and did not bind detectably to either the FGFR1c (Flg) or FGFR2c (Bek) receptor isoforms. The mitogenic activity of FGF-10 could be distinguished from that of KGF by its different sensitivity to heparin and lack of neutralization by a KGF monoclonal antibody. These results indicate that FGF-10 and KGF have similar receptor binding properties and target cell specificities, but are differentially regulated by components of the extracellular matrix. |
| Databáze: | OpenAIRE |
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