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Fibroblast growth factors (FGFs) play a central role in limb development and postnatal skeletogenesis through binding to their cognate receptor tyrosine kinases (RTKs). Since RTKs can signal through multiple downstream pathways to regulate both cellular proliferation and cell-type-specific matrix degradation, a selective inhibition of the FGF-RTK pathway may have the potential to influence matrix turnover. PD166866 is a potent inhibitor of the fibroblast growth factor receptor-4 (FGFR4)-PDGFRbeta-c-kit RTK signal transduction pathway. In this study, we examined the ability of PD166866 to affect both cellular proliferation and matrix-degrading activity in mouse embryonic and fetal fibroblasts. We also addressed the impact of PD166866 on cartilage formation in the organ culture and repair model. PD166866 inhibited FGF-stimulated proliferation of both embryonic and fetal chondroprogenitor cells in a dose-dependent manner. PD166866 reduced [3H]proline release from NIH 3T3 cells (IC50 0.9 microM), but had no effect on the release of [3H]proline from rat fetal cartilage. PD166866 decreased [3H]proline release from embryonic cartilage explants in a dose-dependent manner (IC50 1.9 microM). However, explants treated with PD166866 for 24 h in organ culture responded to FGF2 with a significant increase in [3H]proline release. These data demonstrate that PD166866 decreases the turnover of cartilage extracellular matrix, but paradoxically appears to enhance FGF2-stimulated matrix turnover. Since the FGF-FGFR signaling pathway controls multiple activities including matrix turnover in chondrocytes, the current data suggest that the use of an FGF-RTK inhibitor to treat cartilage-related disorders is not a viable therapeutic approach.[A combined high