Abstract
Receptor activator of nuclear factor-kB ligand (RANKL), a well-known membrane-bound molecule expressed on osteoblasts and bone marrow stromal cells, is believed to induce osteoclast differentiation and activation by binding to the receptor activator of nuclear factor-kB (RANK), which is expressed on the surface of osteoclast lineage cells. This induction is inhibited by osteoprotegerin (OPG) that is secreted by osteoblast lineage and acts as a decoy receptor of RANKL. Currently the essential role of the OPG/RANKL/RANK system in the process of osteoclast maturation, as well as activation, has been well established, and the majority of bone resorption regulators control osteoclast formation and activation through their effects on this system and especially on the relative expression levels of RANKL and OPG [1].
References
Marx J. 2004. Coming to grips with bone loss. Science. 305, 1420–1422.
Zhou H., Kartsogiannis V., Hu Y.S., Elliott J., Quinn J.M., McKinstry W.J., Gillespie M.T., Ng K.W. 2001. A novel osteoblast-derived C-type lectin that inhibits osteoclast formation. J. Biol. Chem. 276, 14916–14923.
Zhou H., Kartsogiannis V., Quinn J.M., Ly C., Gange C., Elliott J., Ng K.W., Gillespie M.T. 2002. Osteoclast inhibitory lectin, a family of new osteoclast inhibitors. J. Biol. Chem. 277, 48808–48815.
Kartsogiannis V., Sims N.A., Quinn J.M., Ly C., Cipetic M., Poulton I.J., Walker E.C., Saleh H., McGregor N.E., Wallace M.E., Smyth M.J., Martin T.J., Zhou H., Ng K.W., Gillespie M.T. 2008. Osteoclast inhibitory lectin, an immune cell product that is required for normal bone physiology in vivo. J. Biol. Chem. 283, 30850–30860.
Hu Y.S., Zhou H., Myers D., Quinn J.M., Atkins G.J., Ly C., Gange C., Kartsogiannis V., Elliott J., Kostakis P., Zannettino A.C., Cromer B., McKinstry W.J., Findlay D.M., Gillespie M.T., Ng K.W. 2004. Isolation of a human homolog of osteoclast inhibitory lectin that inhibits the formation and function of osteoclasts. J. Bone. Miner. Res. 19, 89–99.
Nakamura A., Ly C., Cipetic M., Sims N.A., Vieusseux J., Kartsogiannis V., Bouralexis S., Saleh H., Zhou H., Price J.T., Martin T.J., Ng K.W., Gillespie M.T., Quinn J.M. 2007. Osteoclast inhibitory lectin (OCIL) inhibits osteoblast differentiation and function in vitro. Bone. 40, 305–315.
Palmiter R.D., Sandgren E.P., Avarbock M.R., Allen D.D., Brinster R.L. 1991. Heterologous introns can enhance expression of transgenes in mice. Proc. Natl. Acad. Sci. U. S. A. 88, 478–482.
Kaufman R.J. 1990. Selection and coamplification of heterologous genes in mammalian cells. Methods Enzymol. 185, 537–566.
Lee H.B., Alam M.R., Seol J.W., Kim N.S. 2008. Tartrate-resistant acid phosphatase, matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in early stages of canine osteoarthritis. Vet. Med. 53, 214–220.
Rangaswami H., Bulbule A., Kundu G.C. 2004. Nuclear factor-inducing kinase plays a crucial role in osteopontin-induced MAPK/lkappaB alpha kinase-dependent nuclear factor kappaB-mediated promatrix metalloproteinase-9 activation. J. Biol. Chem. 279, 38921–38935.
Sundaram K., Nishimura R., Senn J., Youssef R.F., London S.D., Reddy S.V. 2007. RANK ligand signaling modulates the matrix metalloproteinase-9 gene expression during osteoclast differentiation. Exp. Cell Res. 313, 168–178.
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Cui, Z., Mi, M., Wang, J. et al. High level secretory expression of murine OCIL by CHO cells and action of OCIL on osteoclast differentiation. Mol Biol 45, 686–690 (2011). https://doi.org/10.1134/S0026893311040169
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DOI: https://doi.org/10.1134/S0026893311040169