Autor: |
Akon Higuchi, Yasunari Takanashi, Nobuya Tsuzuki, Tetsuo Asakura, Chong-Su Cho, Toshihiro Akaike, Mariko Hara |
Předmět: |
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Zdroj: |
Journal of Biomedical Materials Research, Part A; 6/1/2003, Vol. 65 Issue 3, p369, 10p |
Abstrakt: |
The production of interferon-β by NB1-RGB fibroblast cells cultured on protein and peptide membranes prepared from silk fibroin, motif peptides of silk fibroin [(AG)n] containing arginineglycineaspartic acid (RGD) peptide, and Pronectin was investigated. The cell density on various protein and peptide membranes was approximately the same, although the production of interferon-β depended significantly on the membranes where the cells were cultured. The highest production of interferon-β was observed when the cells were cultured on (AG)6RGD(AG)7 membranes prepared with hexafluoroacetone (HFA) as the casting solvent. On RGD-containing peptide membranes more centrally located in the peptides, the cells produced more interferon-β when the peptide membranes were prepared with HFA as the casting solvent. However, there was no enhanced production of interferon-β by cells on (AG)6RGD(AG)7 membranes prepared with 9 mol/L LiBr or 4.5 mol/L LiClO4 solution as the casting solvent. Therefore, both the chemical composition and the secondary and higher order structure of the peptide membranes are important for enhanced production of interferon-β. The blocking of integrin β1 on the cells by anti-integrin β1 antibody prevented the enhanced production of interferon-β on (AG)6RGD(AG)7 membranes prepared with HFA. We suggest that the cells must bind to the RGD sequence having the appropriate conformation through their integrin β1 for enhanced production of interferon-β. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 65A: 369378, 2003 [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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