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Enhanced osteogenesis by collagen‐binding peptide from bone sialoprotein in vitro and in vivo
Author(s) -
Choi Yoon Jung,
Lee Jue Yeon,
Chung ChongPyoung,
Park Yoon Jeong
Publication year - 2013
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.34356
Subject(s) - bone sialoprotein , peptide , microbiology and biotechnology , materials science , in vivo , protein kinase b , fusion protein , in vitro , chemistry , biochemistry , biology , signal transduction , osteocalcin , alkaline phosphatase , enzyme , recombinant dna , gene
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.