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J. Biol. Chem., Vol. 265, Issue 22, 12767-12770, Aug, 1990
DP Bottaro, JS Rubin, D Ron, PW Finch, C Florio and SA Aaronson
Keratinocyte growth factor (KGF) is a member of the fibroblast growth
factor (FGF) family. KGF exhibits potent mitogenic activity for a variety
of epithelial cell types but is distinct from other known FGFs in that it
is not mitogenic for fibroblasts or endothelial cells. We report saturable
specific binding of 125I-KGF to surface receptors on intact Balb/MK mouse
epidermal keratinocytes. 125I-KGF binding was completed efficiently by
acidic FGF (aFGF) but with 20-fold lower efficiency by basic FGF (bFGF).
The pattern of 125I-acidic FGF binding and competition on Balb/MK
keratinocytes and NIH/3T3 fibroblasts suggests that these cell types
possess related but distinct FGF receptors. Scatchard analysis of 125I-KGF
binding suggested major and minor high affinity receptor components (KD =
400 and 25 pM, respectively) as well as a third high capacity/low affinity
heparin- like component. Covalent affinity cross-linking of 125I-KGF to its
receptor on Balb/MK cells revealed two species of 115 and 140 kDa. KGF also
stimulated the rapid tyrosine phosphorylation of a 90-kDa protein in
Balb/MK cells but not in NIH/3T3 fibroblasts. Together these results
indicate that Balb/MK keratinocytes possess high affinity KGF receptors to
which the FGFs may also bind. However, these receptors are distinct from
the receptor(s) for aFGF and bFGF on NIH/3T3 fibroblasts, which fail to
interact with KGF.
Characterization of the receptor for keratinocyte growth factor. Evidence for multiple fibroblast growth factor receptors
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
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