International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Toll-like receptor and silk sericin for tissue engineering

  • Kim, Seong-Gon (Dept. of Oral and Maxillofacial Surgery, College of Dentistry, Gangneung-Wonju National University) ;
  • Kweon, HaeYong (Sericultural and Apicultural Division, National Institute of Agricultural Science, RDA) ;
  • Jo, You-Young (Sericultural and Apicultural Division, National Institute of Agricultural Science, RDA)
  • Received : 2021.02.22
  • Accepted : 2021.03.22
  • Published : 2021.03.31
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Abstract

Toll-like receptor (TLR) is responsible for the recognition of foreign protein. Accordingly, TLR is mainly expressed in the immune associated cells. When foreign protein such as silk sericin is considered for the graft, the response of TLR should be considered. TLR is not all or none responsive receptor. TLR can be activated differently by the intensity of the input. Silk sericin is easily fragmented. The protein conformation of silk sericin is different to the degumming method. TLR response to silk sericin may be different to the degumming method. Consequently, objective tailored extraction method should be investigated and developed.

Keywords

References

  1. Achek A, Kwon HK, Patra MC, Shah M, Hong R, Lee WH, et al. (2020) A peptide derived from the core β-sheet region of TIRAP decoys TLR4 and reduces inflammatory and autoimmune symptoms in murine models. EBioMedicine 52 ,102645. https://doi.org/10.1016/j.ebiom.2020.102645
  2. Ajibade AA, Wang Q, Cui J, Zou J, Xia X, Wang M, et al. (2012) TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1+CD11b+ neutrophils. Immunity 36, 43-54. https://doi.org/10.1016/j.immuni.2011.12.010
  3. Al-Halifa S, Zottig X, Babych M, Cote-Cyr M, Bourgault S, Archambault D (2020) Harnessing the activation of Toll-like receptor 2/6 by self-assembled cross-β fibrils to design adjuvanted nanovaccines. Nanomaterials (Basel) 10(10), 1981. https://doi.org/10.3390/nano10101981
  4. Aramwit P, Sangcakul A (2007) The effects of sericin cream on wound healing in rats. Biosci Biotechnol Biochem 71(10), 2473-2477. https://doi.org/10.1271/bbb.70243
  5. Belvin MP, Anderson KV (1996) A conserved signaling pathway: the Drosophila toll-dorsal pathway. Annu Rev Cell Dev Biol 12, 393-416. https://doi.org/10.1146/annurev.cellbio.12.1.393
  6. Celhar T, Magalhaes R, Fairhurst AM (2012) TLR7 and TLR9 in SLE: when sensing self goes wrong. Immunol Res 53, 58-77. https://doi.org/10.1007/s12026-012-8270-1
  7. Chen ZJ (2012) Ubiquitination in signaling to and activation of IKK. Immunol Rev 246, 95-106. https://doi.org/10.1111/j.1600-065X.2012.01108.x
  8. Chirila TV, Suzuki S, McKirdy NC (2016) Further development of silk sericin as a biomaterial: comparative investigation of the procedures for its isolation from Bombyx mori silk cocoons. Prog Biomater 5, 135-145. https://doi.org/10.1007/s40204-016-0052-8
  9. Chlapanidas T, Farago S, Lucconi G, Perteghella S, Galuzzi M, Mantelli M, et al. (2013) Sericins exhibit ROS-scavenging, anti-tyrosinase, anti-elastase and in vitro immunomodulatory activities, Int J Biol Macromol 58, 47-56. https://doi.org/10.1016/j.ijbiomac.2013.03.054
  10. Dembic Z (2005) The function of toll-like receptors; in Toll and toll-like receptors: an immunologic perspective. Rich T (ed), p18-55, Kluwer Academics, New York, NY, USA.
  11. 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. https://doi.org/10.1016/S0965-1748(97)00022-2
  12. Hashimoto C, Hudson KL, Anderson KV (1988) The Toll gene of drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein. Cell 52, 269-279. https://doi.org/10.1016/0092-8674(88)90516-8
  13. 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
  14. Jo YY, Kweon HY, Oh JH (2020) Sericin for tissue engineering. Appl Sci 10(23), 8457. https://doi.org/10.3390/app10238457
  15. Kang DW, Yun PY, Choi YH, Kim YK (2019) Sinus bone graft and simultaneous vertical ridge augmentation: case series study. Maxillofac Plast Reconstr Surg 41, 36. https://doi.org/10.1186/s40902-019-0221-5
  16. Kaur J, Rajkhowa R, Tsuzuki T, Millington K, Zhang J, Wang X (2013) Photoprotection by silk cocoons. Biomacromolecules 14, 3660-3667. https://doi.org/10.1021/bm401023h
  17. Kawai T, Akira S (2010) The role of pattern-recognition receptors in innate immunity: update on toll-like receptors. Nat Immunol 11, 373-384. https://doi.org/10.1038/ni.1863
  18. Kawasaki T, Kawai T (2014) Toll-like receptor signaling pathways, Front Immunol 5, 461.
  19. Kim SG (2020) Immunomodulation for maxillofacial reconstructive surgery. Maxillofac Plast Reconstr Surg 42(1), 5. https://doi.org/10.1186/s40902-020-00249-4
  20. 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
  21. Kim JW, Jo YY, Kim JY, Oh J, Yang BE, Kim SG (2019) Clinical study for silk mat application into extraction socket: a split-mouth, randomized clinical trial. Maxillofac Plast Reconstr Surg 41, 16. https://doi.org/10.1186/s40902-019-0199-z
  22. Kim SG, Jo YY, Kweon HY (2020a) Soluble fraction from silk mat induced bone morphogenic protein in RAW264.7 cells. Int J Indust Entomol 41, 51-55. https://doi.org/10.7852/IJIE.2020.41.2.51
  23. Kim DW, Jo YY, Kweon HY, Kim SG (2020b) Different level of tumor necrosis factor-a expression after administration of silk sericin fraction in RAW264.7 cells. Int J Indust Entomol 41, 1-5. https://doi.org/10.7852/IJIE.2020.40.3.1
  24. Kulkarni HS, Scozzi D, Gelman AE (2020) Recent advances into the role of pattern recognition receptors in transplantation. Cell Immunol 351, 104088. https://doi.org/10.1016/j.cellimm.2020.104088
  25. Kurioka A, Kurioka F, Yamazaki M (2004) Characterization of sericin powder prepared from citric acid-degraded sericin polypeptides of the silkworm, Bombyx mori. Biosci Biotechnol Biochem 68:774-780 https://doi.org/10.1271/bbb.68.774
  26. Kweon H, Yeo J, Kim K, Kim Y, Song H, Kim S, et al. (2009) Characteristics of silk sericin extracted from sericinjam. Int J Indust Entomol 18(2), 121-124.
  27. Medzhitov R, Preston-Hurlburt P, Janeway CAJ (1997) A human homologue of the Drosophila activation of adaptive immunity. Nature 388, 394-397. https://doi.org/10.1038/41131
  28. Meng X, Ao L, Song Y, Babu A, Yang X, Wang M, et al. (2008) Expression of functional Toll-like receptors 2 and 4 in human aortic valve interstitial cells: potential roles in aortic valve inflammation and stenosis. Am J Physiol Cell Physiol 294(1), C29-35. https://doi.org/10.1152/ajpcell.00137.2007
  29. Miehaille JJ, Garel A, Prudhomme JC (1990) Cloning and characterization of the highly polymorphic Ser2 gene of Bombyx mori. Gene 86, 177-184. https://doi.org/10.1016/0378-1119(90)90277-X
  30. Mok KH, Pettersson J, Orrenius S, Svanborg C (2007) HAMLET, protein folding, and tumor cell death. Biochem Biophys Res Commun 354, 1-7. https://doi.org/10.1016/j.bbrc.2006.12.167
  31. O'Neill LA, Golenbock D, Bowie AG (2013) The history of Toll-like receptors - redefining innate immunity. Nat Rev Immunol 13, 453-460. https://doi.org/10.1038/nri3446
  32. Oh H, Lee JY, Kim MK, Um IC, Lee KH (2011) Refining hot-water extracted silk sericin by ethanol-induced precipitation. Int J Biol Macromol 48(1), 32-37 https://doi.org/10.1016/j.ijbiomac.2010.09.008
  33. Okamoto H, Ishikawa E, Suzuki Y (1982) Structural analysis of sericin genes. Homologies with fibroin gene in the 5' flanking nucleotide sequences. J Biol Chem 257, 15192-15199. https://doi.org/10.1016/S0021-9258(18)33412-4
  34. Park BK, Nho SK, Um IC (2019) Crystallinity of yellow colored silkworm variety cocoons. Int J Indust Entomol 38, 51-55. https://doi.org/10.7852/IJIE.2019.38.2.51
  35. Rapsinski GJ, Wynosky-Dolfi MA, Oppong GO, Tursi SA, Wilson RP, Brodsky IE, et al. (2015) Toll-like receptor 2 and NLRP3 cooperate to recognize a functional bacterial amyloid, curli. Infect Immun 83(2) ,693-701. https://doi.org/10.1128/IAI.02370-14
  36. Su X, Ao L, Shi Y, Johnson TR, Fullerton DA, Meng X (2011) Oxidized low density lipoprotein induces bone morphogenetic protein-2 in coronary artery endothelial cells via Toll-like receptors 2 and 4. J Biol Chem 286(14), 12213-12220. https://doi.org/10.1074/jbc.M110.214619
  37. Takasu Y, Yamada H, Tsubouchi K (2002) Extraction and chromatographic analysis of cocoon sericin of the silkworm, Bombyx mori. J Insect Biotechnol Sericol 71, 151-156.
  38. Takeuchi A, Ohtsuki C, Miyazaki T, Kamitakahara M, Ogata S, Yamazaki M, et al. (2005) Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin. J R Soc Interface 2, 373-378. https://doi.org/10.1098/rsif.2005.0052
  39. Teramoto H, Kakazu A, Asakura T (2006) Native structure and degradation pattern of silk sericin studied by 13C NMR spectroscopy. Macromolecules 39, 6-8. https://doi.org/10.1021/ma0521147
  40. Tsukada M (1979) Structural properties of silk sericin extracted by Mosher's method. J Sericult Sci Japan 48, 301-306.
  41. Tu S, Zhong D, Xie W, Huang W, Jiang Y, Li Y (2016) Role of toll-like receptor signaling in the pathogenesis of graft-versus-host diseases. Int J Mol Sci 17, E1288.
  42. Tukel C, Wilson RP, Nishimori JH, Pezeshki M, Chromy BA, Baumler AJ (2009) Responses to amyloids of microbial and host origin are mediated through Toll-like receptor 2. Cell Host Microbe 6, 45-53. https://doi.org/10.1016/j.chom.2009.05.020
  43. Yang X, Fullerton DA, Su X, Ao L, Cleveland JC Jr, Meng X (2009) Pro-osteogenic phenotype of human aortic valve interstitial cells is associated with higher levels of Toll-like receptors 2 and 4 and enhanced expression of bone morphogenetic protein 2. J Am Coll Cardiol 53(6), 491-500. https://doi.org/10.1016/j.jacc.2008.09.052
  44. Yun H, Kim MK, Kwak HW, Lee JY, Kim MH, Kim EH, et al. (2013) Preparation and characterization of silk seiricn/glycerol/grapheme oxidenanocomposite film. Fiber Polym 14(12), 2111-2116. https://doi.org/10.1007/s12221-013-2111-2
  45. Yun H, Kim MK, Kwak HW, Lee JY, Kim MH, Lee KH (2016) The role of glycerol and water in flexible silk sericin film. Int J Biol Macromol 82, 945-951. https://doi.org/10.1016/j.ijbiomac.2015.11.016
  46. Vagenende V, Yap MGS, Trout BL (2009) Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry 48, 11084-11096. https://doi.org/10.1021/bi900649t
  47. Zhang YQ (2002) Applications of natural silk protein sericin in biomaterials. Biotechnol Adv 20, 91-100. https://doi.org/10.1016/S0734-9750(02)00003-4
  48. Zhang D, Zhang G, Hayden MS, Greenblatt MB, Bussey C, Flavell RA, et al. (2004) A toll-like receptor that prevents infection by uropathogenic bacteria. Science 303, 1522-1526. https://doi.org/10.1126/science.1094351
  49. 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(4), e0123403. https://doi.org/10.1371/journal.pone.0123403
  50. Zhao H, Perez JS, Lu K, George AJ, Ma D (2014) Role of Toll-like receptor-4 in renal graft ischemia-reperfusion injury. Am J Physiol Renal Physiol 306(8), F801-811.