ABSTRACT
BACKGROUND: Fibroblast growth factor receptor 1 (FGFR1) mRNA can be alternatively spliced to generate isoforms containing (FGFR1alpha) or lacking (FGFR1beta) the first immunoglobulin-like domain. We examined which isoforms are expressed by cultured prostate cells, their affinities for FGF-2, and the effect of heparin on FGF-2 binding. METHODS: FGFR1 isoform expression was examined by RT-PCR. FGFR1alpha and FGFR1beta were expressed in CHO cells mutant in heparan sulfate synthesis, and their affinities for FGF-2, FGF-1, FGF-4, and FGF-6 were determined in the presence and absence of heparin. RESULTS: FGFR1alpha was expressed in luminal epithelial cells, whereas FGFR1beta was expressed in basal epithelial and smooth muscle cells. FGFR1beta bound FGF-2 with three-fourfold higher affinity than FGFR1alpha both in the presence and absence of heparin. Heparin increased affinity of both receptor isoforms for FGF-2 approximately four-fivefold. CONCLUSIONS: Prostate smooth muscle and basal epithelial cells are likely to be more sensitive than luminal epithelial cells to the low concentrations of FGFs present in vivo.