International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
권호 표지
DOI QR코드

DOI QR Code

Different level of tumor necrosis factor-α expression after administration of silk sericin fraction in RAW264.7 cells

  • Kim, Dae-Won (Dept. of Oral Biochemistry, College of Dentistry, Gangneung-Wonju National University) ;
  • Jo, You-Young (Sericultural and Apicultural Division, National Institute of Agricultural Sciences, RDA) ;
  • Kweon, HaeYong (Sericultural and Apicultural Division, National Institute of Agricultural Sciences, RDA) ;
  • Kim, Seong-Gon (Dept. of Oral and Maxillofacial Surgery, College of Dentistry, Gangneung-Wonju National University)
  • Received : 2020.09.07
  • Accepted : 2020.09.18
  • Published : 2020.09.29
Download PDF
⟨ Previous Next ⟩

Abstract

Tumor necrosis factor-α (TNFα) is a representative marker for inflammation. Silk sericin is known as mild TNFα inducer. The purpose of this study was to compare the level of TNFα among different fractions of silk sericin. Silk sericin was extracted from cocoon and separated it by molecular weight. Each fraction was applied to RAW264.7 cells. The level of TNFα was evaluated by western blot and ELISA assay. In results, the level of TNFα was increased as time-dependent manner. Higher molecular weight fraction of sericin induced higher amount of TNFα than lower molecular weight fraction. In conclusion, different molecular weight fraction of sericin induced TNFα differently.

Keywords

References

  1. Ahsan F, Ansari TM, Usmani S, Bagga P (2018) An insight on silk protein sericin: From processing to biomedical application. Drug Res (Stuttg) 68(6), 317-327. https://doi.org/10.1055/s-0043-121464
  2. Andrade-Oliveira V, Foresto-Neto O, Watanabe IKM, Zatz R, Camara NOS (2019) Inflammation in renal diseases: New and old players. Front Pharmacol 10, 1192. https://doi.org/10.3389/fphar.2019.01192
  3. Bae YS, Kim CW, Bae DG, Um IC (2016) Effect of degumming on structure and mechanical properties of silk textile made with silk/polyurethane core-spun yarn. Int J Indust Entomol 33(2), 132-137. https://doi.org/10.7852/ijie.2016.33.2.132
  4. Dowling JK, Dellacasagrande J (2016) Toll-like receptors: Ligands, cell-based models, and readouts for receptor action. In: Toll-like receptors. McCoy CE (ed.), pp. 3-28, Humana Press. New York, NY, USA.
  5. Gholipourmalekabadi M, Sapru S, Samadikuchaksaraei A, Reis RL, Kaplan DL, Kundu SC (2020) Silk fibroin for skin injury repair: Where do things stand? Adv Drug Deliv Rev 153, 28-53. https://doi.org/10.1016/j.addr.2019.09.003
  6. Jiao Z, Song Y, Jin Y, Zhang C, Peng D, Chen Z, et al. (2017) In vivo characterizations of the immune properties of sericin: An ancient material with emerging value in biomedical applications. Macromol Biosci 17(12), 1700229. https://doi.org/10.1002/mabi.201700229
  7. Jo YY, Kim DW, Choi JY, Kim SG (2019) 4-Hexylresorcinol and silk sericin increase the expression of vascular endothelial growth factor via different pathways. Sci Rep 9, 3448. https://doi.org/10.1038/s41598-019-40027-5
  8. Jo YY, Kweon H, Kim DW, Baek K, Kim MK, Kim SG, et al. (2017) Bone regeneration is associated with the concentration of tumour necrosis factor-¥a induced by sericin released from a silk mat. Sci Rep 7, 15589. https://doi.org/10.1038/s41598-017-15687-w
  9. Kaur J, Rajkhowa R, Tsuzuki T, Millington K, Zhang J, Wang X (2013) Photoprotection by silk cocoons. Biomacromol 14(10), 3660-3667. https://doi.org/10.1021/bm401023h
  10. Kim DW, Jo YY, Garagiola U, Choi JY, Kang YJ, Oh JH, et al. (2020) Increased level of vascular endothelial growth factors by 4-hexylresorcinol is mediated by transforming growth factor-¥a1 and accelerates capillary regeneration in the burns in diabetic animals. Int J Mol Sci 21(10), 3473. https://doi.org/10.3390/ijms21103473
  11. Kim JW, Jo YY, Kweon HY, Kim DW, Kim SG (2018) The effects of proteins released from silk mat layers on macrophages. Maxillofac Plast Reconstr Surg 40, 10. https://doi.org/10.1186/s40902-018-0149-1
  12. Kim SG (2020) Immunomodulation for maxillofacial reconstructive surgery. Maxillofac Plast Reconstr Surg 42(1), 5. https://doi.org/10.1186/s40902-020-00249-4
  13. Mandal BB, Priya AS, Kundu S (2009) Novel silk sericin/gelatin 3-D scaffolds and 2-D films: fabrication and characterization for potential tissue engineering applications. Acta Biomater 5, 3007-3020. https://doi.org/10.1016/j.actbio.2009.03.026
  14. Nuchadomrong S, Senakoon W, Sirimungkarart S, Senawong T, Kitikoon P (2009) Antibacterial and antioxidant activities of sericin powder from Eri silkworm cocoons correlating to degumming processes. Int J Wild Silkmoth Silk 13, 69-78.
  15. Padron JG, Saito Reis CA, Kendal-Wright CE (2020) The role of danger associated molecular patterns in human fetal membrane weakening. Front Physiol 11, 602.
  16. Park CJ, Um IC (2016) Effect of centrifugation on the structure and properties of silk sericin. Int J Indust Entomol 33(2), 144-148. https://doi.org/10.7852/ijie.2016.33.2.144
  17. Park CJ, Um IC (2018) Effect of heat treatment on the structural characteristics and properties of silk sericin film. Int J Indust Entomol 37(2), 36-42. https://doi.org/10.7852/ijie.2018.37.2.36
  18. Thoma A, Lightfoot AP (2018) NF-kB and inflammatory cytokine signalling: Role in skeletal muscle atrophy. Adv Exp Med Biol 1088, 267-279. https://doi.org/10.1007/978-981-13-1435-3_12
  19. Zhang YQ, Ma Y, Xia YY, Shen WD, Mao JP, Xue RY (2006) Silk sericin-insulin bioconjugates: Synthesis, characterization and biological activity. J Control Release 115(3), 307-315. https://doi.org/10.1016/j.jconrel.2006.08.019
  20. Zhang Y, Zhao P, Dong Z, Wang D, Guo P, Guo X, et al. (2015) Comparative proteome analysis of multi-layer cocoon of the silkworm, Bombyx mori. PLoS ONE 10, e0123403. https://doi.org/10.1371/journal.pone.0123403

Cited by

  1. Toll-like receptor and silk sericin for tissue engineering vol.42, pp.1, 2021, https://doi.org/10.7852/ijie.2021.42.1.1