Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5.
We have purified biologically active recombinant human fibroblast growth factor 5 (FGF-5) from Escherichia coli. In the presence of heparin, recombinant FGF-5 is as active as native growth factor, demonstrating that glycosylation does not significantly potentiate FGF-5 activity. FGF-5 can bind and induce autophosphorylation of human FGF receptors (FGFR) 1 and 2. Competition binding studies show that the KD for FGF-5-FGFR-1 and FGF-5-FGFR-2 interactions are both between 0.5 and 1.5 x 10(-9) M.
Clements, DA; Wang, JK; Dionne, CA; Goldfarb, M
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