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A vitronectin-derived dimeric peptide suppresses osteoclastogenesis by binding to c-Fms and inhibiting M-CSF signaling
Cited 5 time in
Web of Science
Cited 4 time in Scopus
- Authors
- Issue Date
- 2022-09
- Publisher
- Academic Press
- Citation
- Experimental Cell Research, Vol.418 No.1, p. 113252
- Abstract
- © 2022 Elsevier Inc.Vitronectin is an abundant multifunctional glycoprotein found in serum, the extracellular matrix, and bone, and is involved in diverse physiological processes. Here, we developed a new bioactive dimeric peptide (VnP-8-DN1 dimer) from a human vitronectin-derived motif (IDAAFTRINCQG; residues 206–217; VnP-8) via removal of an isoleucine residue at the N-terminus of VnP-8 and spontaneous air oxidation. The VnP-8-DN1 dimer potently enhanced cell attachment activity, and this activity was mediated by binding to cellular heparan sulfate proteoglycan receptors. Moreover, the VnP-8-DN1 dimer suppressed osteoclast differentiation by blocking the early stage of osteoclastogenesis induced by macrophage colony-stimulating factor (M-CSF) and receptor activator of nuclear factor-κB ligand (RANKL). Furthermore, the VnP-8-DN1 dimer decreased the bone-resorbing activity of osteoclasts and increased the survival of osteoclast precursor cells by decreasing the cellular level of c-Fms and reducing RANK expression. Taken together, these results demonstrate that the VnP-8-DN1 dimer inhibits the early stages of M–CSF– and RANK-induced osteoclast differentiation by binding to c-Fms and inhibiting M-CSF signaling.
- ISSN
- 0014-4827
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