Identification and characterization of a novel, intracellular isoform of fibroblast growth factor receptor-1(FGFR-1).

A novel, low molecular weight, intracellular isoform of FGF receptor-1 (FGFR-1) was identified in embryonic chicken tissues using several antibodies specific for different domains of FGF receptors. This low molecular weight isoform differs from the previously characterized isoforms of FGFR-1 in that it contains little or no carbohydrate. Furthermore, in contrast to the other isoforms of FGFR-1, this novel isoform is located exclusively intracellularly. However, it is capable of binding 125I-FGF-2 and it possesses intrinsic kinase activity. Pulse-chase experiments indicate that this isoform of FGFR-1 is not simply a precursor to glycosylated FGFR-1 since it can be detected long after the appearance of glycosylated FGFR-1 in the cells. These results suggest that the novel FGFR-1 isoform plays a role in regulating FGF activity distinct from cell surface, glycosylated FGFR-1. The possible roles of this FGFR-1 variant in FGF signaling are discussed.