Cilengitide inhibits osteoclast adhesion through blocking the α_vβ₃-mediated FAK/Src signaling pathway.

ABSTRACT: The remodeling of actin cytoskeleton of osteoclasts on the bone matrix is essential for osteoclastic resorption activity. A specific regulator of the osteoclast cytoskeleton, integrin α_vβ₃, is known to provide a key role in the degradation of mineralized bone matrixes. Cilengitide is a potent inhibitor of integrins and is capable of affecting α_vβ₃ receptors, and has anti-tumor and anti-angiogenic and apoptosis-inducing effects. However, its function on osteoclasts is not fully understood. Here, the cilengitide role on nuclear factor κB ligand-receptor activator (RANKL)-induced osteoclasts was explored. Cells were cultured with varying concentrations of cilengitide (0,0.002,0.2 and 20 μM) for 7 days, followed by detected via Cell Counting K

SUBMITTER: Guo DY 

PROVIDER: S-EPMC10395300 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature