Ligand binding properties of binary complexes of heparin and immunoglobulin-like modules of FGF receptor 2

Fumiyuki Uematsu, Mikio Kan, Fen Wang, Jun Hyeog Jang, Yongde Luo, Wallace L. McKeehan

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Epithelial cells, which express FGFR2IIIb, bind and respond to FGF-1, FGF-7 and FGF-10, but not FGF-2. Stromal cells, which bind and respond to FGF-1 and FGF-2, but not FGF-7 and FGF-10, express FGFR2IIIc or FGFR1IIIc. Here we show that when both isolated FGFR2βIIIb and FGFR2βIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity. In addition, FGF-2 and FGF-7 bound to both heparin-Ig module IIIb and IIIc complexes, but FGF-1 bound to neither Ig module III. The results show that in isolation both Ig modules II and III of FGFR2 can interact with heparin and that each exhibits a binding site for FGF. We suggest that the specificity of FGFR2IIIb and FGFR2IIIc is dependent on the cell membrane environment and heparin/heparan sulfate. Ig modules II and III cooperate both within monomers and across dimers with cellular heparan sulfates to confer cell type-dependent specificity of the FGFR complex for FGF. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)830-836
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume272
Issue number3
DOIs
StatePublished - Jun 16 2000

Keywords

  • Cell communication
  • Extracellular matrix
  • Heparan sulfate proteoglycans
  • Prostate cancer
  • Stromal-epithelial interactions
  • Tyrosine kinases

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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