期刊
BONE
卷 48, 期 6, 页码 1336-1345出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.bone.2011.02.018
关键词
Osteoclast; Caspase; MAP kinase; NF-kappa B; Ribosome-inactivating protein
资金
- National Science Council, Taiwan [NSC 98-2320-B-039-012-MY3]
- National Taiwan University, Taiwan [100F008-406]
- China Medical University Hospital, Taiwan [DMR-95-035]
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-kappa B, 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. (C) 2011 Elsevier Inc. All rights reserved.
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