Enhanced osteogenesis by collagen-binding peptide from bone sialoprotein in vitro and in vivo

Authors

  • Yoon Jung Choi,

    1. Dental Regenerative Biotechnology Major, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Republic of Korea
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    • These authors equally contributed to this work.

  • Jue Yeon Lee,

    1. Research Institute, Nano Intelligent Biomedical Engineering Corporation (NIBEC), Seoul, Republic of Korea
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    • These authors equally contributed to this work.

  • Chong-Pyoung Chung,

    Corresponding author
    1. Research Institute, Nano Intelligent Biomedical Engineering Corporation (NIBEC), Seoul, Republic of Korea
    • Research Institute, Nano Intelligent Biomedical Engineering Corporation (NIBEC), Seoul, Republic of Korea
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  • Yoon Jeong Park

    Corresponding author
    1. Dental Regenerative Biotechnology Major, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Republic of Korea
    2. Research Institute, Nano Intelligent Biomedical Engineering Corporation (NIBEC), Seoul, Republic of Korea
    • Dental Regenerative Biotechnology Major, School of Dentistry and Dental Research Institute, Seoul National University, Seoul 110-749, Republic of Korea
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  • How to cite this article: Choi YJ, Lee JY, Chung C-P, Park YJ. 2013. Enhanced osteogenesis by collagen-binding peptide from bone sialoprotein in vitro and in vivo. J Biomed Mater Res Part A 2013:101A:547–554.

Abstract

Bone sialoprotein (BSP) is a mineralized, tissue-specific, and noncollagenous protein. The binding of BSP to collagen is thought to be important for the initiation of bone mineralization and formation. In this study, we elucidated the osteogenic efficiency of the collagen-binding (CB) peptide derived from BSP in vitro and in vivo. The CB peptide increased osteoblastic differentiation marker gene and protein expression without affecting cell proliferation. The osteoblastic differentiation by the CB peptide is performed by the activation of extracellular signal-regulated kinase (ERK1/2) and protein kinase B (Akt). Notably, the activation of CB peptide-induced osteogenic differentiation was completely blocked to the basal level by the specific inhibitors for ERK1/2 (U0126) and Akt (LY294002). In vivo results further demonstrated that the CB peptide-coated hydroxyapatite scaffold was able to induce bone formation in the bone defect. Taken together, the CB peptide can be developed as an osteoblastic differentiation agent as well as a fusion biomaterial for bone regeneration therapy. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A, 2013.

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