Cilengitide inhibits osteoclast adhesion through blocking the αvβ3-mediated FAK/Src signaling pathway

The remodeling of actin cytoskeleton osteoclasts on the bone matrix is essential for osteoclastic resorption activity. A specific regulator osteoclast cytoskeleton, integrin αvβ3, known to provide a key role in degradation mineralized matrixes. Cilengitide potent inhibitor integrins and capable affecting αvβ3 receptors, has anti-tumor anti-angiogenic apoptosis-inducing effects. However, its function not fully understood. Here, cilengitide nuclear factor κB ligand-receptor activator (RANKL)-induced was explored. Cells were cultured with varying concentrations (0,0.002,0.2 20 μM) 7 days, followed by detected via Cell Counting Kit-8, staining tartrate resistant acid phosphatase (TRAP), F-actin ring formation, assays, adhesion immunoblotting real-time fluorescent quantitative PCR. Results demonstrated that effectively restrained functionality formation concentration-dependent manner, without causing any cytotoxic Mechanistically, inhibited osteoclast-relevant genes expression; meanwhile, downregulated expression signaling molecules associated including focal kinase (FAK), c-Src. Therefore, this results have confirmed regulates activity blocking signal pathway resulting diminished osteoclasts.