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Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblat differentiation

Cited 37 time in Web of Science Cited 38 time in Scopus
Authors
Lee, Jue-Yeon; Choo, Jung-Eun; Choi, Young-Sook; Lee, Kuen-Yong; Min, Do-Sik; Pi, Sung-Hee; Seol, Yang-Jo; Lee, Seung-Jin; Jo, In-Ho; Chung, Chong-Pyoung; Park, Yoon-Jeong
Issue Date
2007-12
Publisher
Wiley-Blackwell
Citation
J Biomed Mater Res 83A: 970–979, 2007
Keywords
synthetic peptidefibroblast growth factorheparin binding domainsurface immobilizationosteoblast differentiationbone regeneration
Abstract
Fibroblast growth factor (FGF)-2 regulates a variety of cellular functions, such as proliferation and differentiation, by binding to cell surface FGF receptors (FGFRs) in the presence of heparin proteoglycans. FGF-2 is known as a heparin-binding growth factor, but the localization of the heparin binding site has not been fully investigated until now. We used two potential heparin binding domains of FGF-2, the residues 105-111 (F105, YKRSRYT) and 119-135 (F119, KRTGQYKLGSKTGPGQK). Peptides could be stably immobilized onto the surface of tissue culture plates. Using solid phase binding assays, we demonstrated that both peptides had higher binding affinity toward heparin compared with nonbinding control sequence. The biological significance of these sites was tested by cell attachment and osteoblast differentiation studies. Cell attachment to the peptides F105 and F119 increased in a dose-dependent manner. Heparin and heparinase treatments decreased cell adhesion to both F105 and F119. This demonstrates that both F105 and F119 interact with cell-surface heparan sulfate proteoglycans, suggesting that FGF-2 has two heparin binding sites. In addition, osteoblast differentiation, confirmed by ALPase activity and mineralization, was increased by surface immobilized peptide F105 and F119. Taken together, these heparin binding peptides could be applied as biological agents enhancing osteoblast differentiation as well as surface modification tools in the tissue regeneration area, especially for bone regeneration.
ISSN
1549-3296
Language
English
URI
http://hdl.handle.net/10371/62703
DOI
https://doi.org/10.1002/jbm.a.31351
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College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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