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

Title
Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblast differentiation
Authors
Lee J.-Y.Choo J.-E.Choi Y.-S.Lee K.-Y.Min D.-S.Pi S.-H.Seol Y.-J.Lee S.-J.Jo I.-H.Chung C.-P.Park Y.-J.
Ewha Authors
이승진조인호
SCOPUS Author ID
이승진scopus; 조인호scopus
Issue Date
2007
Journal Title
Journal of Biomedical Materials Research - Part A
ISSN
1549-3296JCR Link
Citation
vol. 83, no. 4, pp. 970 - 979
Indexed
SCI; SCIE; SCOPUS WOS scopus
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. © 2007 Wiley Periodicals, Inc.
DOI
10.1002/jbm.a.31351
Appears in Collections:
약학대학 > 약학과 > Journal papers
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