Sericin Protein Derived from Silk Accelerates Proliferation of Mammalian Cells

Terada, Satoshi; Yanagihara, Kana; Saitoh, Yasukazu; Takemura, K.; Nishimura, Tetsujiro; Miki, Masao; Sasaki, Michihito; Yamada, Hideyuki

doi:10.1007/978-94-017-0726-8_74

Cited by 44 publications

(64 citation statements)

References 3 publications

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“…To the best of our knowledge, the current study is the first to report the effects of sericin supplementation during maturation culture on the meiotic competence of sheep oocytes. Sericin has been reported to stimulate the proliferation of mammalian cells (Terada et al, 2002). Moreover, sericin decreases the level of reactive oxygen species in cultures by preventing H 2 O 2 -induced oxidative stress , and the mechanism of this antioxidant action is the chelation of trace elements stemming from the remarkably high content of hydroxy amino acids in sericin (Kato et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Maturation and fertilisation of sheep oocytes cultured in serum-free medium containing silk protein sericin

Yasmin

Otoi

Setiadi

et al. 2015

Acta Veterinaria Hungarica

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Sericin is a water-soluble component of silk and has been used as a biomaterial due to its antibacterial and ultraviolet radiation-resistant properties. This study was designed to evaluate the effect of sericin supplementation in a maturation medium on the meiotic competence and fertilisability of sheep oocytes. Cumulus-oocyte complexes (COCs) were cultured in TCM199 supplemented with sericin at various concentrations of 0 (control), 0.1, 0.25 and 0.5%, either with or without bovine serum albumin (BSA). When the COCs were matured without BSA, the supplementation of 0.1% sericin significantly increased the rates of maturation to metaphase II and the total fertilisation of oocytes compared with the other concentrations of sericin. When the COCs were matured with BSA, the beneficial effects of 0.1% sericin supplementation on the maturation and fertilisation of oocytes were not observed. Our findings indicate that supplementation with 0.1% sericin during maturation culture may improve the nuclear maturation and fertilisability of sheep oocytes. Moreover, it may be possible to replace BSA with sericin in chemically defined media without the risk of disease transmission.

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Section: Discussionmentioning

confidence: 99%

Maturation and fertilisation of sheep oocytes cultured in serum-free medium containing silk protein sericin

Yasmin

Otoi

Setiadi

et al. 2015

Acta Veterinaria Hungarica

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“…일반적으로 세포는 증식하기 위해 알부노이드 단백질인 BSA 등을 주요 에 너지원으로 이용한다. 세리신에 존재하는 세린은 알부노 이드 단백질로서 세포의 생존 및 증식에 관여한다 (Terada et al 2002). 세리신의 경우 세린이 30%이상, 피브로인의 경우 세린으로 변환될 수 있는 글리신이 44%이상 함유되 어 있다 (Kim et al 2012 …”

Section: 세포 증식 촉진 효과unclassified

Manufacture and Characterization of Silkworm Gland Hydrolysate

Hwang¹,

Lee²,

Kim³

et al. 2012

Korean Journal of Sericultural Science

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Silk protein has been explored to be used for biomedical applications for several decades. However, it has not been used in this field cause to their irreversible crystallization after dissolving in water. The existing methods of silk protein hydrolysis using silkworm cocoon were used with harmful solvents and through a very complicated process. Therefore, we have developed novel methods for the production of water-soluble hydrolysate using silkworm gland. We manufactured two types of silkworm gland-derived hydrolysate (water-soluble SGH, SSGH; total SGH, TSGH) and compared the characteristics with commercial cocoon-derived sericin hydrolysate (CSH). The molecular weight of SGH ranged from 7 to 50 kDa (SSGH) and 5 to 15 kDa (TSGH) within glycine, alanine, and aspartic acid as a main amino acid composition. In contrast, CSH ranged from 15 to 50 kDa within serine and aspartic acid. The results of FTIR implied that SGH was more soluble form than CSH, as shown by the decrease in the β-sheet structure at 1630 cm -1 on amide I peak. In comparison with 10% fetal bovine serum, 0.1% (1 mg/ml) SSGH had equivalent effect on the proliferation of human dermal fibroblasts and mesenchymal stem cells. All results of the SSGH made by novel manufacturing process indicate the SSGH is more preferable as a culture medium supplement than cocoon-derived sericin.

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“…Sericin proteins from the five Thai native silk cocoons were extracted using basic hydrolysis (Terada et al, 2002) and autoclaving (Zhang et al, 2004). For the basic hydrolysis, 100 g of cocoon was cut into small pieces before the addition of 5 L of 0.2% (w/v) sodium carbonate solution (pH 11-12) and boiled at 95°C for 2 h. Then, the extracts were filtered to remove fibroin using a glass microfiber filter.…”

Section: Preparation Of Sericin From Thai Native Silk Cocoonsmentioning

confidence: 99%