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The identification of a heparin binding domain peptide from bone morphogenetic protein-4 and its role on osteogenesis

Title
The identification of a heparin binding domain peptide from bone morphogenetic protein-4 and its role on osteogenesis
Authors
Choi Y.J.Lee J.Y.Park J.H.Park J.B.Suh J.S.Choi Y.S.Lee S.J.Chung C.-P.Park Y.J.
Ewha Authors
이승진
SCOPUS Author ID
이승진scopus
Issue Date
2010
Journal Title
Biomaterials
ISSN
0142-9612JCR Link
Citation
vol. 31, no. 28, pp. 7226 - 7238
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The presence of heparin binding has been become crucial in exerting growth factor related tissue formation. Receptor-mediated osteoblastic differentiation by bone morphogenetic protein (BMP)-4 and supportive function of its heparin binding has been proposed, direct role of the heparin binding site of BMP-4 on osteogenesis has not yet been fully investigated. If the binding site itself plays role on osteogenesis, the site domain can be useful in bone formation in combination with biomaterial. Herein, we synthesized a peptide sequence corresponding to residues 15-24 of BMP-4 (HBD, RKKNPNCRRH), as potential heparin binding sequence. The HBD peptide-induced ostoegenic differentiation by activating extracellular signal-regulated kinase (ERK1/2), one of the key regulators in hMSC. Also, treatment of cultured hMSCs with heparinase blocked both HBD peptide-induced osteogenic differentiation and GAG chain detection while abolishing the increased phospho-ERK level. These results suggest that the identified heparin binding domain peptide (HBD) stimulated osteoblastic differentiation via interaction with heparin and the ERK signaling. In vivo results further demonstrated that HBD, as a form of complex with alginate gel, was able to induce bone formation in the bone defect. © 2010 Elsevier Ltd.
DOI
10.1016/j.biomaterials.2010.05.022
Appears in Collections:
약학대학 > 약학과 > Journal papers
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