title: Improving cell-adhesive properties of recombinant Bombyx mori silk by incorporation of collagen or fibronectin derived peptides produced by transgenic silkworms.
abstract: Silk of Bombyx mori can be used as various biomaterials. Especially, it is useful as a protein for coating the surface of cell culture plates since the silk possesses a biocompatibility to the cultured cells. However, the cell-adhesive ability is weaker than collagen or fibronectin, which are used for coating the plate more frequently (Yao et al. J. Biochem., 2004, 136, 643-649). To increase the biocompatibility of the silk, we constructed transgenic silkworms, inserting the modified fibroin light-chain genes for making recombinant silks that possessed partial collagen or fibronectin sequences, that is, [GERGDLGPQGIAGQRGVV(GER)3GAS]8GPPGPCCGGG or [TGRGDSPAS]8, respectively. Films were made from the recombinant silks, and the cell-adhesive activity for cultured mammalian cells was observed. The results showed that the two types of recombinant silk films possessed a much higher cell-adhesive activity as compared to the original unmodified silk. Especially, the recombinant silk with the sequence [TGRGDSPAS]8, produced by a transgenic Nd-sD mutant, gave a 6 times higher activity than the original unmodified silk.
authors.affiliation: Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo, Japan.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Yanagisawa
authors.forename: Zhenghua
authors.initials: Z
authors.lastname: Zhu
authors.forename: Isao
authors.initials: I
authors.lastname: Kobayashi
authors.forename: Keiro
authors.initials: K
authors.lastname: Uchino
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Tamada
authors.forename: Toshiki
authors.initials: T
authors.lastname: Tamura
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Asakura
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D030801:Animals, Genetically Modified; D012831:Bombyx / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002448:Cell Adhesion / Q000187:drug effects; D002460:Cell Line; D003094:Collagen / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009842:Oligopeptides / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D047011:Silk / Q000235:genetics / Q000378:metabolism*
chemical_list: D005353:Fibronectins; D009842:Oligopeptides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D047011:Silk; C047981:arginyl-glycyl-aspartic acid; D003094:Collagen