Browse > Article
http://dx.doi.org/10.3839/jabc.2011.028

The Promotion of Cell Attachment and Proliferation on Silk Fibroin  

Jo, You-Young (Sericultural & Apicultural Materials Division, National Academy of Agricultural Science, RDA)
Kweon, Hae-Yong (Sericultural & Apicultural Materials Division, National Academy of Agricultural Science, RDA)
Lee, Kwang-Gill (Sericultural & Apicultural Materials Division, National Academy of Agricultural Science, RDA)
Nam, Sung-Hee (Sericultural & Apicultural Materials Division, National Academy of Agricultural Science, RDA)
Lee, Heui-Sam (Sericultural & Apicultural Materials Division, National Academy of Agricultural Science, RDA)
Yeo, Joo-Hong (Sericultural & Apicultural Materials Division, National Academy of Agricultural Science, RDA)
Publication Information
Journal of Applied Biological Chemistry / v.54, no.3, 2011 , pp. 166-170 More about this Journal
Abstract
Silk fibroin, a natural protein produced by silkworm, is a good biomaterial which has biodegradability and biocompatibility. To ascertain the effects of silk fibroin on cell growth, silk fibroin films were prepared using silk fibroin aqueous solutions of various concentrations. We investigated the attachment, proliferation, morphology of the cells and the expression levels of genes related to cell attachment and growth on the silk fibroin films. When the cells were cultured on the 0.1 and 1% silk fibroin film, the cell adhesion ability was very excellent. Particularly, overall cell growth on the 1% silk fibroin film was definitely superior to the others. Also, expression levels of genes related cell growth were increased on the 0.1 and 1% silk fibroin film. These results suggest silk as a material for medical applications.
Keywords
cell attachment; cell proliferation; gene expression; silk fibroin;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Sofia S, McCarthy MB, Gronowicz G, and Kaplan DL (2001) Functionalized silk-based biomaterials for bone formation. J Biomed Mater Res 54, 139-148.   DOI   ScienceOn
2 Sun M, Zhou P, Pan LF, Liu S, and Yang HX (2009) Enhanced cell affinity of the silk fibroin-modified PHBHHx material. J Mater Sci Mater Med 20, 1743-1751.   DOI   ScienceOn
3 Yeo JH, Lee KG, Kim HC, Oh HYL, Kim AJ, and Kim SY (2000) The effects of Pva/chitosan/fibroin (PCF)-blended spongy sheets on wound healing in rats. Biol Pharm Bull 10, 1220-1223.
4 Zhou CZ, Confalonieri F, Medina N, Zivanovic Y, Esnault C, and Yang T (2000) Fine organization of Bombyx mori fibroin heavy chain gene. Nucleic Acids Res 28, 2413-2419.   DOI
5 Minoura N, Tsukada M, and Nagura M (1990) Fine structure and oxygen permeability of silk fibroin membrane treated with methanol. Polymer 31, 265-269.   DOI   ScienceOn
6 Mosmann T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65, 55-63.   DOI   ScienceOn
7 Moy RL, Lee A, and Zalka A (1991) Commonly used suture materials in skin surgery. Am Fam Physician 44, 2123-2128.
8 Pankov R and Yamada KM (2002) Fibronectin at a glance. J Cell Sci 115, 3861-3863.   DOI   ScienceOn
9 Santin M, Motta A, Freddi G, and Cannas M (1999) In vitro evaluation of the inflammatory potential of the silk fibroin. J Biomed Mater Res 46, 382-389.   DOI   ScienceOn
10 Fraser RD, MacRae TP, and Stewart FH (1966) Poly-l-alanylglycyl-lanalylglycyl- l-serylglycine: a model for the crystalline regions of silk fibroin. J Mol Biol 19, 580-582.   DOI
11 Horan RL, Antle K, Collette AL, Wang YZ, Huang J, Moreau JE, Volloch V, Kaplan DL, and Altman GH (2005) In vitro degradation of silk fibroin. Biomaterials 26, 3385-3393.   DOI   ScienceOn
12 Hynes RO (1990) In Fibronectins. Springer-Verlag, New York, NY
13 Jensen LT and Host NB (1997) Collagen: Scaffold for repair or execution. Cardiovascular Research 33, 535-539.   DOI   ScienceOn
14 Kenyon NJ, Ward RW, McGrew G, and Last JA (2003) TGF-b1 causes airway fibrosis and increased collagen I and III mRNA in mice. Thrax 58, 772-777.   DOI   ScienceOn
15 Kim UJ, Park J, Kim HJ, Wada M, and Kaplan DL (2005) Threedemensional aqueous-derived biomaterial scaffolds from silk fibroin. Biomaterials 26, 2775-2785.   DOI   ScienceOn
16 Lv Q, Cao C, Zhang Y, Man X, and Zhu H (2004) The preparation of insoluble fibroin films induced by degummed fibroin or fibroin microspheres. J Mater Sci Mater Med 15, 1193-1197.   DOI
17 Kweon HY, Ha HC, Um IC, and Park YH (2001) Physical properties of silk fibroin/chitosan blend films. J Appl Plym Sci 80, 928-934.   DOI   ScienceOn
18 Lammli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.   DOI   ScienceOn
19 Lucas F, Shaw JTB, and Smith SG (1957) The amino acid sequence in a fraction of the fibroin of Bombyx mori. Biochem J 66, 468-479.
20 Lyon M, Rushton G, Askari JA, Humphries MJ, and Gallagher JT (2000) Elucidation of the Structural Features of Heparan Sulfate, Important for Interaction with the Hep-2 Domain of Fibronectin. J Biol Chem 275, 4599-4606.   DOI   ScienceOn