Abstract：
:Human osteoclast formation from mononuclear phagocyte precursors involves interactions between lectins and their receptors. A type-2 ribosome inactivating protein consists of an A chain and a B chain. The glycosylated B chain binds specifically to galactose moieties of sugar molecules. In this study we showed that the recombinant ribosome inactivating protein B-chain (rRBC) could induce osteoclast formation from human monocytes and murine RAW264.7 macrophages. Tartrate-resistant acid phosphatase (TRAP) staining and bone resorption assays demonstrated that differentiation of osteoclast-like cells was induced in the presence of rRBC in a dose-dependent manner. The rRBC-induced osteoclast differentiation was independent of caspase activation and apoptosis induction activity; however, rRBC-induced osteoclastogenesis was dependent on activation of NF-κB, ERK1/2, and p38 MAP kinase. Thus, our data demonstrated that rRBC induced osteoclast differentiation through a non-apoptotic signaling pathway. In addition to triggering apoptosis, the rRBC also induced osteoclast differentiation. According to this study, a novel role is proposed for rRBC in regulating osteoclast differentiation and in osteoimmunology.
journal_name
Bonejournal_title
Boneauthors
Wang YM,Lu TL,Hsu PN,Tang CH,Chen JH,Liu KC,Kao JT,Tzen JT,Wu YYdoi
10.1016/j.bone.2011.02.018subject
Has Abstractpub_date
2011-06-01 00:00:00pages
1336-45issue
6eissn
8756-3282issn
1873-2763pii
S8756-3282(11)00070-6journal_volume
48pub_type
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