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Acta Biochimica et Biophysica Sinica Advance Access originally published online on September 6, 2009
Acta Biochimica et Biophysica Sinica 2009 41(10):852-857; doi:10.1093/abbs/gmp076
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© The Author 2009. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

Protein engineering of a fibroblast growth factor-1 fusion protein with cell adhesive activity

Eunyi Jeon1, Hae-Won Kim2,3 and Jun-Hyeog Jang1,*

1 Department of Biochemistry, Inha University School of Medicine, Incheon, Korea
2 Deparment of Biomaterials Science, School of Dentistry and Institute of Tissue Regeneration Engineering (ITREN), Dankook University, Cheonan, Korea
3 Biomaterials and Tissue Engineering Lab, Department of Nanobiomedical Science & WCU Research Center, Dankook University, Cheonan, Korea

* Correspondence address. Tel: +82-32-890-0933; Fax: +82-32-882-1877; E-mail: juhjang{at}inha.ac.kr


  Abstract

Fibroblast growth factor-1 (FGF1) is one of the most potent angiogenic growth factors, and also plays an important role in regulating cellular functions including cell proliferation, motility, differentiation, survival, and tissue regeneration processes. Here we described a novel fusion protein that was designed by combining the cell adhesion sequence from fibronectin with FGF1. The F1–Fn fusion protein functions as a minimized protein that directs integrin-dependent cell adhesion and stimulates cellular responses including cell proliferation and differentiation. Moreover, our results indicate that Fn-mediated signaling synergizes with signals from FGF1 in promoting cellular adhesion, proliferation, and differentiation in MG63 cells.

Keywords    bone; fibroblast growth factor-1; fusion protein; fibronectin; extracellular matrix

Received: May 13, 2009; Accepted: June 22, 2009
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