A 15-amino acid C-terminal peptide of beta-defensin-3 inhibits bone resorption by inhibiting the osteoclast differentiation and disrupting podosome belt formation

摘要: Human beta-defensin-3 (HBD3), which is secreted from cells in the skin, salivary gland, and bone marrow, exhibits antimicrobial immunomodulatory activities. Its C-terminal end contains a 15-amino acid polypeptide (HBD3-C15) that known to effectively elicit activity. Recently, certain peptides are inhibit osteoclast differentiation and, thus, we investigated whether HBD3-C15 hinders destruction assess its potential use as an anti-bone resorption agent. inhibited receptor activator of nuclear factor κB ligand (RANKL)-induced formation pits. In addition, disrupted RANKL-induced podosome belt feature typically found mature osteoclasts with bone-resorbing capacity. downregulated cortactin, cofilin, vinculin, involved formation. Furthermore, loss induced by RANKL was significantly reduced mouse calvarial implantation model treated HBD3-C15. Similar inhibitory effects were observed on Aggregatibacter actinomycetemcomitans lipopolysaccharide (AaLPS). Concordantly, attenuated AaLPS-implanted mouse. Collectively, these results suggest has effect developing this occurs via disruption could be therapeutic agent for inhibition destruction.