TI  - cDNA cloning and expression of a human  FGF receptor  which binds acidic and
      basic  FGF .
PG  - 197-208
AB  - We have isolated and characterized a cDNA clone, <prot>phFGFR</prot>, encoding a human
      fibroblast growth factor (FGF) receptor. <prot>phFGFR</prot> contains an open reading
      frame which encodes an 820 amino acid polypeptide with three
      immunoglobulin-like domains in the extracellular part and an intracellular
      split tyrosine kinase domain. Transient expression in COS-1 cells and
      immunoprecipitation using an antiserum raised against a C-terminal
      peptide, gave rise to two components, representing mature (130 kDa) and
      precursor (115 kDa) forms of the <prot>phFGFR</prot> encoded polypeptide, which was
      denoted <prot>hFGFR-1</prot>. Crosslinking of iodinated <prot>acidic FGF</prot> (<prot>aFGF</prot>) and <prot>basic FGF</prot>
      (<prot>bFGF</prot>) to transiently expressing COS-1 cells revealed a major band of 95
      kDa, which was competed for by both <prot>aFGF</prot> and <prot>bFGF</prot> . From Scatchard
      analyses, the Kd:s for binding of  <prot>aFGF</prot>  and  <prot>bFGF</prot>  to   <prot>hFGFR-1</prot>   were estimated to 25 pM and 41 pM, respectively. Thus, <prot>phFGFR</prot> encodes a human   FGF
      receptor   with high affinity for both  <prot>aFGF</prot>  and  <prot>bFGF</prot> .
AD  - Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
