Abstract
Sericin is the silk protein that covers fibroin fibers and functions as a `glue' in the cocoons of silkworms, and its most abundant component, Ser1, contains repeats of Ser- and Thr-rich 38 amino acid residues. The viability of Sf9 insect cells was 20, 57 and 49% on the fifth day and 41, 91 and 70% on the ninth day after serum deprivation in the presence of no additives, 3000 μg sericin hydrolysate and 350 μg SerD (the peptide containing the two repetitive units) ml−1, respectively. Thus, the sericin samples were useful in preventing cell death and promoting cellular growth after acute serum deprivation.
Similar content being viewed by others
References
Akiyama D, Okazaki M, Hirabayashi K (1993) Method for the preparation of a polymer with a high water absorption capacity containing sericin. J. Seric. Sci. Jpn. 62: 392–396.
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.
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.
Minoura N, Aiba S, Gotoh Y, Tsukada M, Imai Y (1995) Attachment and growth of cultured fibroblast cells on silk protein matrices. J. Biomed. Mater. Res. 29: 1215–1221.
Nilausen K (1978) Role of fatty acids in growth-promoting effect of serum albumin on hamster cells in vitro. J. Cell Physiol. 96: 1–14.
Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368–379.
Takasu Y, Yamada H, Tsubouchi K (2002) Isolation of three main sericin components from the cocoon of the silkworm, Bombyx mori. Biosci. Biotechnol. Biochem. 66: 2715–2718.
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. Cytotechnology 40: 3–12.
Tsujimoto K, Takagi H, Takahashi M, Yamada H, Nakamori S (2001) Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. J. Biochem. 129: 979–986.
Voegeli R, Meier J, Blust R (1993) Sericin silk protein: unique structure and properties. Cosmet. Toiletries 108: 101–108.
Weiss SA, Godwin GP, Gorfien SF, Whitford WG (1995) Insect cell culture in serum-free media. Meth. Mol. Biol. 39: 79–95.
Zhang YQ (2002) Applications of natural silk protein sericin in biomaterials. Biotechnol. Adv. 20: 91–100.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Takahashi, M., Tsujimoto, K., Yamada, H. et al. The silk protein, sericin, protects against cell death caused by acute serum deprivation in insect cell culture. Biotechnology Letters 25, 1805–1809 (2003). https://doi.org/10.1023/A:1026284620236
Issue Date:
DOI: https://doi.org/10.1023/A:1026284620236