International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Cytocompatibility of silkworm cocoon layer extracts

  • Jo, You-Young (Sericultural and Apicultural Materials Division, National Institute of Agricultural Science, RDA) ;
  • Kim, Sung-Kuk (Chonbuk National University School of Dentistry) ;
  • Lee, Kwang-Gill (Sericultural and Apicultural Materials Division, National Institute of Agricultural Science, RDA) ;
  • Bae, Sung Min (Sericultural and Apicultural Materials Division, National Institute of Agricultural Science, RDA) ;
  • Kim, Jong-Ho (School of Textile Engineering and Fashion Design, Kyungpook National University) ;
  • Shin, Bong-Seob (School of Textile Engineering and Fashion Design, Kyungpook National University) ;
  • Jeon, Jong-Young (School of Textile Engineering and Fashion Design, Kyungpook National University) ;
  • Kweon, HaeYong (Sericultural and Apicultural Materials Division, National Institute of Agricultural Science, RDA)
  • Received : 2016.10.20
  • Accepted : 2016.11.04
  • Published : 2016.12.31
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Abstract

Recently silk polymer produced by Bombyx mori silkworm has been considered as biological macromolecules. Silk polymer was extracted in PBS solution at $37^{\circ}C$ for 72 h or $72^{\circ}C$ for 24 h. The effect of EtOH treatment on the cocoon extraction was also examined. The extraction yield of cocoon was less than 1 wt% regardless of extraction conditions. UV spectroscopy showed that the experimental extracts have absorption bands at 280 nm. There is no cytotoxicity effect on the mouse fibroblast L929 cell. The phenotype of L929 cell was not changed under the experimental conditions. The proliferation behavior of L929 cell was not affected by the addition of cocoon extract. Therefore, cocoon extract might be cytocompatible and can be used as promising biomaterials.

Keywords

References

  1. Aramwit P, Kanokpanont S, De-Eknamkul W, Kamei K, Srichana T (2009) The effect of sericin with variable amino-acd content from different silk strains on the production of collagen and nitric oxide, J Biomater Sci Polym Ed 20, 1295-1306. https://doi.org/10.1163/156856209X453006
  2. Aramwit P, Sangcakul A (2007) The effects of sericin cream on wound healing in rats, Biosci Biotechnol Biochem 71, 2473-2477. https://doi.org/10.1271/bbb.70243
  3. Fan JB, Wu LP, Chen LS, Mao XY, Ren FZ (2009) Antioxidant activities of silk sericin from silkworm Bombyx mori, J Food Biochem 33, 74-88. https://doi.org/10.1111/j.1745-4514.2008.00204.x
  4. Garel A, Deleage G, Prudhomme JC (1997) Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the Ser 1B cDNA, Insect Biochem Mol Biol 27, 469-477. https://doi.org/10.1016/S0965-1748(97)00022-2
  5. Ha Y, Park Y, Kweon HY, Jo YY, Kim SG (2014) Comparison of the physical properties and in vivo bioactivities of silkworm-cocoon-derived silk membrane, collagen membrane, and polytetrafluoroethylene membrane for guided bone regeneration, Macromol Res 22, 1018-1023. https://doi.org/10.1007/s13233-014-2138-2
  6. Horan RL, Antle K, Collette AL, Wang Y, Huang J, Moreau JE, Volloch V, Kaplan DL, Altman GH (2005) In vitro degradation of silk fibroin, Biomaterials 26, 3385-3393. https://doi.org/10.1016/j.biomaterials.2004.09.020
  7. Ju WT, Kim KY, Sung GB, Kim YS (2014) Quantitative analysis of 1-Deoxynojirimycin content using silkworm genetic resources. Int J Indust Entomol 29(2), 162-168. https://doi.org/10.7852/ijie.2014.29.2.162
  8. Kaewkorn W, Limpeanchob N, Tiyaboonchai W, Pongcharoen S, Sutheerawattananonda M (2012) Effects of silk sericin on the proliferation and apoptosis of colon cancer cells, Biol. Res., 45, 45-50. https://doi.org/10.4067/S0716-97602012000100006
  9. Kato N, Sato S, Yamanaka A, Yamada H, Fuwa N, Nomura M (1998) Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity, Biosci Biotechnol Biochem 62, 145-147. https://doi.org/10.1271/bbb.62.145
  10. Kim J, Kim CH, Park CH, Seo JN, Kweon HY, Kang SW, Lee KG (2000) Comparison of methods for the repair of acute tympanic membrane perforations: Silk patch vs. Paper patch. Wound Rep Regen 18, 132-138.
  11. Kundu B, Rajkhowa R, Kundu SC, Wang X. (2013) Silk fibroin biomaterials for tissue regenerations, Adv Drug Deliv Rev 65, 457-470. https://doi.org/10.1016/j.addr.2012.09.043
  12. Meinel L, Hofmann S, Karageorgiou V, Kirker-Head C, McCool J, Gronowicz G, Zichner L, Langer R, Vunjak-Novakovic G, Kaplan DL (2005) The inflammatory responses to silk films in vitro and in vivo, Biomaterials 26, 147-155. https://doi.org/10.1016/j.biomaterials.2004.02.047
  13. Mo C, Holland C, Porter D, Shao Z, Vollrath F (2009) Concentration state dependence of the rheological and structural properties of reconstituted silk, Biomacromol 10, 2724-2728. https://doi.org/10.1021/bm900452u
  14. Terada S, Nishimura T, Sasaki M, Yamada H, Miki M (2002) Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma, Cytotechnol 40, 3-12. https://doi.org/10.1023/A:1023993400608
  15. Teramoto H, Kameda T, Tamada Y (2008) Preparation of gel film from Bombyx mori silk sericin and its characterization as a wound dressing, Biosci Biotechnol Biochem 72, 3189-3196. https://doi.org/10.1271/bbb.80375
  16. Teramoto H, Miyazawa M (2005) Molecular orientation behavior of silk sericin film as revealed by ATR infrared spectroscopy. Biomacromol 6, 2049-2057. https://doi.org/10.1021/bm0500547
  17. Vepari C, Kaplan DL (2007) Silk as a biomaterial, Prog Polym Sci 32, 991-1007. https://doi.org/10.1016/j.progpolymsci.2007.05.013
  18. Zhaorigetu S, Yanaka N, Sasaki M, Watanabe H, Kato N (2003) Silk protein, sericin, suppresses DMBA-TPA-induced mouse skin tumorigenesis by reducing oxidative stress, inflammatory responses and endogenous tumor promoter TNF-alpha, Oncol Rep 10, 537-543.
  19. Zhou CZ, Confalonieri F, Jacquet M, Perasso R, Li ZG, Janin J. (2001) Silk fibroin: Structural implications of a remarkable amino acid sequence, Proteins 44, 119-122. https://doi.org/10.1002/prot.1078

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