Selective regulation of osteoclast adhesion and spreading by PLCγ/PKCα-PKCδ/RhoA-Rac1 signaling

• Published in: BMB reports Vol. 51; no. 5; pp. 230 - 235
• Main Authors: Kim, Jin-Man, Lee, Kyunghee, Jeong, Daewon
• Format: Journal Article
• Language: English
• Published: Korea (South) Korean Society for Biochemistry and Molecular Biology 01.05.2018; 생화학분자생물학회
• Subjects: Animals; Cell Adhesion - drug effects; Cell Movement - drug effects; Integrin alphaVbeta3 - metabolism; Macrophage Colony-Stimulating Factor - pharmacology; Male; Mice, Inbred C57BL; Osteoclasts - cytology; Osteoclasts - drug effects; Osteoclasts - metabolism; Osteopontin - pharmacology; Phospholipase C gamma - metabolism; Protein Kinase C-alpha - metabolism; Protein Kinase C-delta - metabolism; rac1 GTP-Binding Protein - metabolism; rhoA GTP-Binding Protein - metabolism; Signal Transduction - drug effects; 화학
• ISSN: 1976-6696; 1976-670X
• DOI: 10.5483/BMBRep.2018.51.5.198

Bone resorption by multinucleated osteoclasts is a multistep process involving adhesion to the bone matrix, migration to resorption sites, and formation of sealing zones and ruffled borders. Macrophage colony-stimulating factor (M-CSF) and osteopontin (OPN) have been shown to be involved in the bone resorption process by respective activation of integrin αvβ3 via "inside-out" and "outside-in" signaling. In this study, we investigated the link between signal modulators known to M-CSF- and OPN-induced osteoclast adhesion and spreading. M-CSF- and OPN-induced osteoclast adhesion was achieved via activation of stepwise signals, including integrin αvβ3, PLCγ, PKCδ, and Rac1. Osteoclast spreading induced by M-CSF and OPN was shown to be controlled via sequential activation, consistent with the osteoclast adhesion processes. In contrast to osteoclast adhesion, osteoclast spreading induced by M-CSF and OPN was blocked via activation of PLCγ/PKCα/RhoA signaling. The combined results indicate that osteoclast adhesion and spreading are selectively regulated via PLCγ/PKCα-PKCδ/RhoA-Rac1 signaling. [BMB Reports 2018; 51(5): 230-235].