Multifunctional role of osteopontin in directing intrafibrillar mineralization of collagen and activation of osteoclasts.

作者: Douglas E. Rodriguez , Taili Thula-Mata , Edgardo J. Toro , Ya-Wen Yeh , Carl Holt

DOI: 10.1016/J.ACTBIO.2013.10.010

关键词:

摘要: Mineralized collagen composites are of interest because they have the potential to provide a bone-like scaffold that stimulates natural processes resorption and remodeling. Working towards this goal, our group has previously shown nanostructure bone can be reproduced using polymer-induced liquid-precursor (PILP) process, which enables intrafibrillar mineralization with hydroxyapatite achieved. This prior work used polyaspartic acid (pASP), simple mimic for acidic non-collagenous proteins, generate nanodroplets/nanoparticles an amorphous mineral precursor infiltrate interstices type-I fibrils. In study we show osteopontin (OPN) similarly serve as process-directing agent collagen, even though OPN is generally considered inhibitor. We also found inclusion in process promotes interaction mouse marrow-derived osteoclasts PILP-remineralized was demineralized, measured by actin ring formation. While osteoclast activation occurred when pASP agent, resulted dramatic effect on activation, presumably inherent arginine–glycine–aspartate ligands OPN. By capitalizing multifunctionality OPN, these studies may lead way producing biomimetic substitutes capability tailorable bioresorption rates.

参考文章(92)
L. F. Lozano, M. A. Peña-Rico, A. Heredia, J. Ocotlán-Flores, A. Gómez-Cortés, R. Velázquez, I. A. Belío, L. Bucio, Thermal analysis study of human bone Journal of Materials Science. ,vol. 38, pp. 4777- 4782 ,(2003) , 10.1023/A:1027483220584
Sun Jie, Liu Ning, Effects of osteopontin from bovine milk on osteoblasts in rat. Acta Nutrimenta Sinica. ,vol. 31, pp. 356- 360 ,(2009)
Fairland F. Amos, Matthew J. Olszta, Saeed R. Khan, Laurie B. Gower, Relevance of a Polymer‐Induced Liquid‐Precursor (PILP) Mineralization Process to Normal and Pathological Biomineralization John Wiley & Sons, Ltd. pp. 125- 217 ,(2007) , 10.1002/0470092122.CH4
MARC D. McKEE, ANTONIO NANCI, Osteopontin and the Bone Remodeling Sequence Annals of the New York Academy of Sciences. ,vol. 760, pp. 177- 189 ,(1995) , 10.1111/J.1749-6632.1995.TB44629.X
Dafna Geblinger, Benjamin Geiger, Lia Addadi, Surface‐Induced Regulation of Podosome Organization and Dynamics in Cultured Osteoclasts ChemBioChem. ,vol. 10, pp. 158- 165 ,(2009) , 10.1002/CBIC.200800549
Carl Holt, Esben S. Sørensen, Roger A. Clegg, Role of calcium phosphate nanoclusters in the control of calcification. FEBS Journal. ,vol. 276, pp. 2308- 2323 ,(2009) , 10.1111/J.1742-4658.2009.06958.X
Nilana MT Barros, Betty Hoac, Raquel L Neves, William N Addison, Diego M Assis, Monzur Murshed, Adriana K Carmona, Marc D McKee, Proteolytic processing of osteopontin by PHEX and accumulation of osteopontin fragments in Hyp mouse bone, the murine model of X‐linked hypophosphatemia Journal of Bone and Mineral Research. ,vol. 28, pp. 688- 699 ,(2013) , 10.1002/JBMR.1766
Pierre D. Delmas, Russell P. Tracy, B. Lawrence Riggs, Kenneth G. Mann, Identification of the noncollagenous proteins of bovine bone by two-dimensional gel electrophoresis Calcified Tissue International. ,vol. 36, pp. 308- 316 ,(1984) , 10.1007/BF02405335
Fairland F. Amos, Lijun Dai, Rajendra Kumar, Saeed R. Khan, Laurie B. Gower, Mechanism of formation of concentrically laminated spherules: implication to Randall's plaque and stone formation. Urological Research. ,vol. 37, pp. 11- 17 ,(2009) , 10.1007/S00240-008-0169-X