Fibroblast growth factor (FGF) receptor 1-IIIb is a naturally occurring functional receptor for FGFs that is preferentially expressed in the skin and the brain.
Journal of Biological Chemistry. 2000-05-01; 275(21): 16091-16097
DOI: 10.1074/jbc.275.21.16091
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Beer HD(1), Vindevoghel L, Gait MJ, Revest JM, Duan DR, Mason I, Dickson C, Werner S.
Author information:
(1)Institute of Cell Biology, Swiss Federal Institute of Technology, CH-8093 Zürich, Switzerland.
Fibroblast growth factors (FGFs) transmit their signals through four
transmembrane receptors that are designated FGFR1-4. Alternative splicing in the
extracellular region of FGFR1-3 generates receptor variants with different
ligand binding affinities. Thus two types of transmembrane receptors (IIIb and
IIIc isoforms) have been identified for FGFR2 and FGFR3, and the existence of
analogous variants has been postulated for FGFR1 based on its genomic structure.
However, only a single full-length transmembrane FGFR1 variant (FGFR1-IIIc) has
been identified so far. Here we describe the cloning of a full-length cDNA
encoding FGFR1-IIIb from a mouse skin wound cDNA library. This receptor isoform
was expressed at the highest levels in a subset of sebaceous glands of the skin
and in neurons of the hippocampus and the cerebellum. FGFR1-IIIb was expressed
in L6 rat skeletal muscle myoblasts and used in cross-linking and receptor
binding studies. FGF-1 was found to bind the receptor with high affinity,
whereas FGF-2, -10, and -7 bound with significantly lower affinities. Despite
their apparently similar but low affinities, FGF-10 but not FGF-7 induced the
activation of p44/42 mitogen-activated protein kinase in FGFR1-IIIb-expressing
L6 myoblasts and stimulated mitogenesis in these cells, demonstrating that this
new receptor variant is a functional transmembrane receptor for FGF-10.
DOI: 10.1074/jbc.275.21.16091
PMID: 10821861 [Indexed for MEDLINE]