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J Biol Chem, Vol. 273, Issue 21, 13230-13235, May 22, 1998
From the Derald H. Ruttenberg Cancer Center, Mount Sinai School of
Medicine, New York, New York 10029
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.
Characterization of Recombinant Human Fibroblast Growth Factor
(FGF)-10 Reveals Functional Similarities with Keratinocyte Growth
Factor (FGF-7)
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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