DOI QR코드

DOI QR Code

Chitin from the Extract of Cuttlebone Induces Acute Inflammation and Enhances MMP1 Expression

  • Lee, Ki Man (Institute of Chronic Diseases and College of Pharmacy, Sahmyook University) ;
  • Shim, Hong (Institute of Chronic Diseases and College of Pharmacy, Sahmyook University) ;
  • Lee, Geum Seon (Institute of Chronic Diseases and College of Pharmacy, Sahmyook University) ;
  • Park, Il Ho (Institute of Chronic Diseases and College of Pharmacy, Sahmyook University) ;
  • Lee, Ok Sang (Department of Pharmacy, College of Pharmacy, Chungbuk National University) ;
  • Lim, Sung Cil (Department of Pharmacy, College of Pharmacy, Chungbuk National University) ;
  • Kang, Tae Jin (Institute of Chronic Diseases and College of Pharmacy, Sahmyook University)
  • Received : 2013.04.24
  • Accepted : 2013.05.14
  • Published : 2013.05.31

Abstract

We previously reported that the extract from cuttlebone (CB) has wound healing effect in burned lesion of rat. In present study, the main component of CB extract was analyzed and its wound healing activity was evaluated by using in vitro acute inflammation model. The extract of CB stimulated macrophages to increase the production of TNF-${\alpha}$. The extract also enhanced the production of TGF-${\beta}$ and VEGF, which were involved in angiogenesis and fibroblast activation. The treatment with CB extract enhanced proliferation of murine fibroblast. CB extract also induced the activation of fibroblast to increase the secretion of matrix metalloproteases 1 (MMP1). The constituent of CB extract which has wound healing activity was identified as chitin by HPLC analysis. The mechanism that the CB extract helps to promote healing of burned lesion is associated with that chitin in CB extracts stimulated wound skins to induce acute inflammation and to promoted cell proliferation and MMP expression in fibroblast. Our results suggest that CB or chitin can be a new candidate material for the treatment of skin wound such as ulcer and burn.

Keywords

References

  1. Amendt, C., Mann, A., Schirmacher, P. and Blessing, M. (2002) Resistance of keratinocytes to TGFbeta-mediated growth restriction and apoptosis induction accelerates re-epithelialization in skin wounds. J. Cell Sci. 115, 2189-2198.
  2. Birkedal-Hansen, H., Moore, W. G., Bodden, M. K., Windsor, L. J., Birkedal-Hansen, B., DeCarlo, A. and Engler, J. A. (1993) Matrix metalloproteinases: a review. Crit. Rev. Oral Biol. Med. 4, 197-250.
  3. Broughton, G. 2nd., Janis, J. E. and Attinger, C. E. (2006) The basic science of wound healing. Plast. Reconstr. Surg. 117, 12S-34S. https://doi.org/10.1097/01.prs.0000225430.42531.c2
  4. Ferrara, N. (1999) Molecular and biological properties of vascular endothelial growth factor. J. Mol. Med. 77, 527-543. https://doi.org/10.1007/s001099900019
  5. Folkman J. (2007) Angiogenesis: an organizing principle for drug discovery? Nat. Rev. Drug Discov. 6, 273-286. https://doi.org/10.1038/nrd2115
  6. Garcia-Enriquez, S., Guadarrama, H. E., Reyes-Gonzalez, I., Mendizabal, E., Jasso-Gastinel, C. F., Garcia-Enriquez, B., Rembao-Bojorquez, D. and Pane-Pianese, C. (2010) Mechanical performance and in vivo tests of an acrylic bone cement fi lled with bioactive sepia offi cinalis cuttlebone. J. Biomater. Sci. Polym. Ed. 21, 113-125. https://doi.org/10.1163/156856209X410265
  7. Gavard, J. and Gutkind, J. S. (2006) VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin. Nat. Cell Biol. 8, 1223-1234. https://doi.org/10.1038/ncb1486
  8. Hackman, R. H. and Goldberg, M. (1965) Studies on chitin VI. The nature of $\alpha$- and $\beta$-chitin. Aust. J. Biol. Sci. 18, 935-946.
  9. Hackman, R. H. (1954) Studies on chitin. I. Enzymic degradation of chitin and chitin esters. Aust. J. Biol. Sci. 7, 168-178.
  10. Jang, J. K., Lee, O. S., Kang, T. J. and Lim, S.C. (2013) Wound healing effect of cuttlebone extract in burn injury of rat. Food Sci. Biotechnol. 22(Suppl), 99-105.
  11. Lee, C. G. (2009) Chitin, chitinases, and chitinase-like proteins in allergic infl ammation and tissue remodeling. Yonsei Med. J. 50, 22-30. https://doi.org/10.3349/ymj.2009.50.1.22
  12. Li, Y., Hazarika, S., Xie, D., Pippen, A. M., Kontos, C. D. and Annex, B. H. (2007) In mice with type 2 diabetes, a vascular endothelial growth factor (VEGF)-activating transcription factor modulates VEGF signaling and induces therapeutic angiogenesis after hindlimb ischemia. Diabetes 56, 656-665. https://doi.org/10.2337/db06-0999
  13. Michaels, J. 5th, Dobryansky, M., Galiano, R. D., Bhatt, K. A., Ashinoff, R., Ceradini, D. J. and Gurtner, G. C. (2005) Topical vascular endothelial growth factor reverses delayed wound healing secondary to angiogenesis inhibitor administration. Wound Repair Regen. 13, 506-512. https://doi.org/10.1111/j.1067-1927.2005.00071.x
  14. Peppa, M., Brem, H., Ehrlich, P., Zhang, J. G., Cai, W., Li, Z., Croitoru, A., Thung, S. and Vlassara, H. (2003) Adverse effects of dietary glycotoxins on wound healing in genetically diabetic mice. Diabetes 52, 2805-2813. https://doi.org/10.2337/diabetes.52.11.2805
  15. Raghow, R. (1994) The role of extracellular matrix in post infl ammatory wound healing and fi brosis. FASEB J. 8, 823-831.
  16. Saaristo, A., Tammela, T., Farkkila, A., Karkkainen, M., Suominen, E., Yla-Herttuala, S. and Alitalo, K. (2006) Vascular endothelial growth factor-C accelerates diabetic wound healing. Am. J. Pathol. 169, 1080-1087. https://doi.org/10.2353/ajpath.2006.051251
  17. Shanmugam, A., Mahalakshmi, T. S. and Barwin Vino, A. (2008) Antimicrobial activity of polysaccharides isolated from the cuttlebone of Sepia aculeate and Sepia brevimana: An approach to selected antimicrobial activity for human pathogenic microorganisms. J. Fish. Aquat. Sci. 3, 268-274. https://doi.org/10.3923/jfas.2008.268.274
  18. Singer, A. J. and Clark, R. A. (1999) Cutaneous wound healing. N. Eng. J. Med. 341, 738-746. https://doi.org/10.1056/NEJM199909023411006
  19. Sternlicht, M. D. and Werb, Z. (2001) How matrix metalloproteinases regulate cell hbehavior. Annu. Rev. Cell Dev. Biol. 17, 463-516. https://doi.org/10.1146/annurev.cellbio.17.1.463
  20. Ueno, H., Nakamura, F., Murakami, M., Okumura, M., Kadosawa, T. and Fujinag, T. (2001) Evaluation effects of chitosan for the extracellular matrix production by fi broblasts and the growth factors production by macrophages. Biomaterials 22, 2125-2130. https://doi.org/10.1016/S0142-9612(00)00401-4
  21. Valentine, R., Athanasiadis, T., Moratti, S., Hanton, L., Robinson, S. and Wormald, P. J. (2010) The effi cacy of a novel chitosan gel on hemostasis and wound healing after endoscopic sinus surgery. Am. J. Rhinol. Allergy 24, 70-75. https://doi.org/10.2500/ajra.2010.24.3422
  22. Yamagishi, S., Yonekura, H., Yamamoto,Y., Fujimori, H., Sakurai, S., Tanaka, N. and Yamamoto, H. (1999) Vascular endothelial growth factor acts as a pericyte mitogen under hypoxic conditions. Lab. Invest. 79, 501-509.

Cited by

  1. Nonenzymatic Transformation of Amorphous CaCO3into Calcium Phosphate Mineral after Exposure to Sodium Phosphate in Vitro: Implications for in Vivo Hydroxyapatite Bone Formation vol.16, pp.9, 2015, https://doi.org/10.1002/cbic.201500057
  2. Therapeutic and prophylactic uses of invertebrates in contemporary Spanish ethnoveterinary medicine vol.12, pp.1, 2016, https://doi.org/10.1186/s13002-016-0111-1
  3. Cephalopods: The potential for their use in medicine vol.43, pp.2, 2017, https://doi.org/10.1134/S1063074017020031
  4. Chitin from Cuttlebone Activates Inflammatory Cells to Enhance the Cell Migration vol.23, pp.4, 2015, https://doi.org/10.4062/biomolther.2015.062
  5. Transcriptome analysis of gene expression patterns during embryonic development in golden cuttlefish (Sepia esculenta) vol.40, pp.3, 2018, https://doi.org/10.1007/s13258-017-0588-6
  6. Evaluation of the Wound-healing Activity of Rice Cell Extracts in Vitro vol.44, pp.3, 2013, https://doi.org/10.4014/mbl.1605.05003
  7. Soy protein and chitin sponge-like scaffolds: from natural by-products to cell delivery systems for biomedical applications vol.22, pp.11, 2020, https://doi.org/10.1039/d0gc00089b