Browse > Article
http://dx.doi.org/10.5352/JLS.2010.20.8.1249

Sericin Enhances Secretion of Thyroglobulin in the Thyrocytes  

Jin, Cho-Yi (Department of Anatomy, School of Medicine, Chungnam National University)
Song, Seong-Hee (Department of Anatomy, School of Medicine, Chungnam National University)
Go, Young-Hwa (Department of Anatomy, School of Medicine, Chungnam National University)
Kwon, Ki-Sang (Department of Anatomy, School of Medicine, Chungnam National University)
Yun, Eun-Young (National Academy of Agricultural Science, R.D.A.)
Goo, Tae-Won (National Academy of Agricultural Science, R.D.A.)
Yeo, Joo-Hong (National Academy of Agricultural Science, R.D.A.)
Kim, Seung-Whan (Department of Emergency Medicine, Chungnam National University Hospital)
Choi, Jong-Soon (Division of Life Science, Korea Basic Science Institute)
Yu, Kweon (Korea Research Institute of Bioscience and Biotechnology)
Kwon, O-Yu (Department of Anatomy, School of Medicine, Chungnam National University)
Publication Information
Journal of Life Science / v.20, no.8, 2010 , pp. 1249-1253 More about this Journal
Abstract
Sericin is a type of high molecular weight water-soluble glycoprotein surrounding fibroin (silk protein) that has been used as a cell culture supplement and accelerates cell proliferation in various serum-free media. The purpose of this study was to investigate the enhancing effect of thyroglobulin (Tg) secretion by sericin in thyrocytes, FRTL-5 cells. While Tg-mRNA expression was not enhanced, a secreted form of Tg was obviously increased by sericin. In this status, expression of both endoplasmic reticulum (ER) molecular chaperones (Bip & calreticulin) and ER membrane proteins (IRE1, PERK & ATF6) was enhanced. The proximal step of IRE1, XBP1 mRNA splicing was slightly detected however, the proximal step of PERK, phosphorylation of $eIF2{\alpha}$, was changeless. In addition, sericin enhanced cell viability by the MTT assay. The above results showing the ability of sericin to promote protein production demonstrated its potential usefulness as a new biomaterial.
Keywords
Sericin; thyroglobulin; ER molecular chaperone;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Tsujimoto, K., H. Takagi, M. Takahashi, H. Yamada, and S. Nakamori. 2001. Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. J. Biochem. 129, 979-986.   DOI   ScienceOn
2 Yoshida, H., T. Matsui, A. Yamamoto, T. Okada, and K. Mori. 2001. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107, 881-891.   DOI
3 Zhang, Y. Q. 2002. Applications of natural silk protein sericin in biomaterials. Biotechnol. Adv. 20, 91-100.   DOI
4 Zhaorigetu, S., N. Yanaka, M. Sasaki, H. Watanabe, and N. Kato. 2003. Inhibitory effects of silk protein, sericin on UVB-induced acute damage and tumor promotion by reducing oxidative stress in the skin of hairless mouse. J. Photochem. Photobiol. B. 71, 11-17.   DOI
5 Benjamin, I. J. 2006. Viewing a stressful episode of ER: is ATF6 the triage nurse? Circ. Res. 98, 1120-1122.   DOI
6 De Gracia, D. J., R. Kumar, C. R. Owe, G. S. Krause, and B. C. White. 2002. Molecular pathways of protein synthesis inhibition during brain reperfusion: implications for neuronal survival or death. J. Cereb. Blood Flow Metab. 22, 127-141.
7 Harding, H. P., M. Calfon, F. Urano, I.Novoa, and Ron D. 2002. Transcriptional and translational control in the Mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18, 575-599.   DOI
8 Kawaoi, A. 1987. Early stages of synthesis of thyroglobulin (Tg), thyroxine (T4), and triiodothyronine (T3) in fetal rat thyroid. An immunoelectron microscopic study. J. Histochem. Cytochem. 35, 1137-1142.   DOI   ScienceOn
9 Kim, P. S., O. Y. Kwon, and P. Arvan. 1996. An Endoplasmic reticulum storage disease causing congenital goiter with hypothyroidism. J. Cell Biol. 133, 517-527.   DOI
10 Kwon, K., T. W. Goo, and O. Y. Kwon. 2005. Development of rapid detection method for unfolded protein response in the mammalian Cells. J. Exp. Biomed. Sci. 11, 249-252.
11 Terada, S., T. Nishimura, M. Sasaki, H. Yamada, and M. Miki. 2002. Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma. Cytotechnology 40, 3-12.   DOI   ScienceOn
12 Ogawa A., S. Terada, T. Kanayama, M. Miki, M. Morikawa, T. Kimura, and S. Terada. 2005. Development of a novel serum-free freezing medium for mammalian cells using the silk protein sericin. Biotechnol. Appl. Biochem. 42, 183-188.   DOI
13 Park, S., K. H. You, M. Shong, T. W. Goo, E. Y. Yun, S. W. Kang, and O. Y. Kwon. 2005. Overexpression of ERp29 in the thyrocytes of FRTL-5 cells. Mol. Biol. Rep. 32, 7-13.   DOI