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

Jue Yeon Lee, Jung Eun Choo, Young Sook Choi, Kuen Yong Lee, Do Sik Min, Sung Hee Pi, Yang Jo Seol, Seung Jin Lee, In Ho Jo, Chong Pyoung Chung, Yoon Jeong Park

Research output: Contribution to journalArticle

38 Citations (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.

Original languageEnglish
Pages (from-to)970-979
Number of pages10
JournalJournal of Biomedical Materials Research - Part A
Volume83
Issue number4
DOIs
Publication statusPublished - 2007 Dec 15

Fingerprint

Osteoblasts
Fibroblast Growth Factor 2
Fibroblasts
Heparin
Peptides
Binding sites
Binding Sites
Heparin Lyase
Fibroblast Growth Factor Receptors
Heparan Sulfate Proteoglycans
Tissue regeneration
Tissue culture
Cell adhesion
Biological Factors
Intercellular Signaling Peptides and Proteins
Surface treatment
Assays
Bone

All Science Journal Classification (ASJC) codes

  • Ceramics and Composites
  • Biomaterials
  • Biomedical Engineering
  • Metals and Alloys

Cite this

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. / Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblast differentiation. In: Journal of Biomedical Materials Research - Part A. 2007 ; Vol. 83, No. 4. pp. 970-979.
@article{4177600b5e2841f6bc8c636dae052886,
title = "Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblast differentiation",
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.",
author = "Lee, {Jue Yeon} and Choo, {Jung Eun} and Choi, {Young Sook} and Lee, {Kuen Yong} and Min, {Do Sik} and Pi, {Sung Hee} and Seol, {Yang Jo} and Lee, {Seung Jin} and Jo, {In Ho} and Chung, {Chong Pyoung} and Park, {Yoon Jeong}",
year = "2007",
month = "12",
day = "15",
doi = "10.1002/jbm.a.31351",
language = "English",
volume = "83",
pages = "970--979",
journal = "Journal of Biomedical Materials Research",
issn = "1549-3296",
publisher = "John Wiley and Sons Inc.",
number = "4",

}

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

In: Journal of Biomedical Materials Research - Part A, Vol. 83, No. 4, 15.12.2007, p. 970-979.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblast differentiation

AU - Lee, Jue Yeon

AU - Choo, Jung Eun

AU - Choi, Young Sook

AU - Lee, Kuen Yong

AU - Min, Do Sik

AU - Pi, Sung Hee

AU - Seol, Yang Jo

AU - Lee, Seung Jin

AU - Jo, In Ho

AU - Chung, Chong Pyoung

AU - Park, Yoon Jeong

PY - 2007/12/15

Y1 - 2007/12/15

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=36849031316&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36849031316&partnerID=8YFLogxK

U2 - 10.1002/jbm.a.31351

DO - 10.1002/jbm.a.31351

M3 - Article

C2 - 17580326

AN - SCOPUS:36849031316

VL - 83

SP - 970

EP - 979

JO - Journal of Biomedical Materials Research

JF - Journal of Biomedical Materials Research

SN - 1549-3296

IS - 4

ER -