Effects of Water Extracts from Chaenomeles sinensis, Polygonum cuspidatum and Boswellia carterii on LPS-Induced MMP-9 Activation in Raw 264.7 Cell

목과(木瓜), 호장근(虎杖根) 및 유향(乳香) 추출물이 Raw 264.7 cell에서 LPS로 유도된 MMP-9 의 활성에 미치는 영향

  • Lee Tae-Jin (Department of Immunology, College of Medicine, Keimyung University) ;
  • Kim Yeoun-Hee (Department of Immunology, College of Medicine, Keimyung University) ;
  • Shu Seong-Il (Department of Microbiology, College of Medicine, Keimyung University) ;
  • Shin Sang-Woo (College of Oriental Medicine, Daegu Haay University) ;
  • Kim Sang-Chan (College of Oriental Medicine, Daegu Haay University) ;
  • Kwon Young-Kyu (College of Oriental Medicine, Daegu Haay University) ;
  • Park Jong-Wook (Department of Immunology, College of Medicine, Keimyung University) ;
  • Kwon Taeg-Kyu (Department of Immunology, College of Medicine, Keimyung University)
  • 이태진 (계명대학교 의과대학 면역학교실) ;
  • 김연희 (계명대학교 의과대학 면역학교실) ;
  • 서성일 (계명대학교 의과대학 미생물학교실) ;
  • 신상우 (대구한의대학교 한의과대학) ;
  • 김상찬 (대구한의대학교 한의과대학) ;
  • 권영규 (대구한의대학교 한의과대학) ;
  • 박종욱 (계명대학교 의과대학 면역학교실) ;
  • 권택규 (계명대학교 의과대학 면역학교실)
  • Published : 2006.02.01

Abstract

Matrix metalloproteinase-9 (MMP-9) is considered to be an important component in the progression of inflammation. Monocytes/macrophages are prominent at inflammation sites, and activation of these cells by stimulants such as lipopolysaccharide (LPS) leads to the production of significant amounts of MMP-9. Here, we show that LPS-induced MMP-9 production and activation was inhibited by the water extract from the fruit of Chaenomeles sinensis (CS), the root of Polygonum cuspidatum (PC), but increased by the extract from Boswellia carterii (BC). To investigate the mechanism by which those extracts inhibits MMP-9 activation, we examined the level of MMP-9 mRNA expression. We observed a significant change in the MMP-9 expression between LPS alone and LPS plus Chaenomeles sinensis and Polygonum cuspidatum extracts-treated cells. In addition, LPS significantly up-regulated MMP-9 promoter activity in Raw 264.7 cells, which was attenuated by the CS and PS extracts. However, water extracts from Boswellia carterii increased MMP-9 expression and MMP-9 promoter activity which were induced by LPS treatment in Raw 264.7 cells. These data suggest that water extracts from Chaenomeles sinensis and Polygonum cuspidatum can modulate anti-inflammatory immune response, which may be in part associated with the regulation of MMP-9 production and/or activation through the regulation of MMP-9 expression in mouse macrophage cells.

References

  1. Higuchi, M., Higashi, N., Taki, H., Osawa, T. Cytolytic mechanisms of activated macrophages. Tumor necrosis factor and L-arginine-dependent mechanisms act synergistically as the major cytolytic mechanisms of activated macrophages. J Immunol. 144(4):1425-1431, 1990
  2. MacMicking, J., Xie, Q.W., Nathan, C. Nitric oxide and macrophage function. Annu Rev Immunol. 15:323-350, 1997 https://doi.org/10.1146/annurev.immunol.15.1.323
  3. Cetkovic-Cvrlje, M., Eizirik, D.L. TNF-alpha and IFN-gamma potentiate the deleterious effects of IL-1 beta on mouse pancreatic islets mainly via generation of nitric oxide. Cytokine. 6(4):399-406, 1994
  4. MacMicking, J.D., Nathan, C., Hom, G., Chartrain, N., Fletcher, D.S., Trumbauer, M., Stevens, K., Xie, Q.W., Sokol, K., Hutchinson, N., et al. Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase. Cell. 81(4):641-650, 1995 https://doi.org/10.1016/0092-8674(95)90085-3
  5. Liu, R.H., Hotchkiss, J.H. Potential genotoxicity of chronically elevated nitric oxide: a review. Mutat Res. 339(2):73-89, 1995 https://doi.org/10.1016/0165-1110(95)90004-7
  6. Watanabe, H., Nakanishi, I., Yamashita, K., Hayakawa, T., Okada, Y. Matrix metalloproteinase-9 (92 kDa gelatinase/ type IV collagenase) from U937 monoblastoid cells: correlation with cellular invasion. J Cell Sci. 104 (Pt4):991-999, 1993
  7. Cheon, H., Yu, S.J., Yoo, D.H., Chae, I.J., Song, G.G., Sohn, J. Increased expression of pro-inflammatory cytokines and metalloproteinase-1 by TGF-beta1 in synovial fibroblasts from rheumatoid arthritis and normal individuals. Clin Exp Immunol. 127(3):547-552, 2002 https://doi.org/10.1046/j.1365-2249.2002.01785.x
  8. Nikkola, J., Vihinen, P., Vlaykova, T., Hahka-Kemppinen, M., Kahari, V.M., Pyrhonen, S. High expression levels of collagenase-1 and stromelysin-1 correlate with shorter disease-free survival in human metastatic melanoma. Int J Cancer. 97(4):432-438, 2002 https://doi.org/10.1002/ijc.1636
  9. Parsons, S.L., Watson, S.A., Brown, P.D., Collins, H.M., Steele, R.J. Matrix metalloproteinases. Br J Surg. 84(2):160-166, 1997 https://doi.org/10.1002/bjs.1800840206
  10. McMillan, J.I., Weeks, R., West, J.W., Bursten, S., Rice, G.C., Lovett, D.H. Pharmacological inhibition of gelatinase B induction and tumor cell invasion. Int J Cancer. 67(4):523-531, 1996 https://doi.org/10.1002/(SICI)1097-0215(19960807)67:4<523::AID-IJC11>3.0.CO;2-8
  11. Visse, R., Nagase, H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res. 92(8):827-839, 2003 https://doi.org/10.1161/01.RES.0000070112.80711.3D
  12. Woo, C.H., Lim, J.H., Kim, J.H. Lipopolysaccharide induces matrix metalloproteinase-9 expression via a mitochondrial reactive oxygen species-p38 kinase-activator protein-1 pathway in Raw 264.7 cells. J Immunol. 173(11):6973-6980, 2004 https://doi.org/10.4049/jimmunol.173.11.6973
  13. Kishnani, N.S., Tabrizi-Fard, M.A., Fung, H.L. Diethyldithiocarbamate prolongs survival of mice in a lipopolysaccharide-induced endotoxic shock model: evidence for multiple mechanisms. Shock. 11(4):264-268, 1999 https://doi.org/10.1097/00024382-199904000-00007
  14. Douglas, D.A., Shi, Y.E., Sang, Q.A. Computational sequence analysis of the tissue inhibitor of metalloproteinase family. J Protein Chem. 16(4):237-255, 1997 https://doi.org/10.1023/A:1026348808069
  15. Kallakury, B.V., Karikehalli, S., Haholu, A., Sheehan, C.E., Azumi, N., Ross, J.S. Increased expression of matrix metalloproteinases 2 and 9 and tissue inhibitors of metalloproteinases 1 and 2 correlate with poor prognostic variables in renal cell carcinoma. Clin Cancer Res. 7(10):3113-3119, 2001
  16. 全國韓醫科大學 本草學敎授. 本草學. 永林社, 서울, pp 272-273, 420-421, 410-411, 2003
  17. Lee, M.H., Han, Y.N. A new in vitro tissue factor inhibitory triterpene from the fruits of Chaenomeles sinensis. Planta Med. 69(4):327-331, 2003 https://doi.org/10.1055/s-2003-38884
  18. Hamauzu, Y., Yasui, H., Inno, T., Kume, C., Omanyuda, M. Phenolic profile, antioxidant property, and anti-influenza viral activity of Chinese quince (Pseudocydonia sinensis Schneid.), quince (Cydonia oblonga Mill.), and apple (Malus domestica Mill.) fruits. J Agric Food Chem. 53(4):928-934, 2005 https://doi.org/10.1021/jf0494635
  19. Takada, Y., Aggarwal, B.B. Betulinic acid suppresses carcinogen-induced NF-kappa B activation through inhibition of I kappa B alpha kinase and p65 phosphorylation: abrogation of cyclooxygenase-2 and matrix metalloprotease-9. J Immunol. 171(6):3278-3286, 2003 https://doi.org/10.4049/jimmunol.171.6.3278
  20. Chen, L., Han, Y., Yang, F., Zhang, T. High-speed counter- current chromatography separation and purification of resveratrol and piceid from Polygonum cuspidatum. J Chromatogr A. 907(1-2):343-346, 2001 https://doi.org/10.1016/S0021-9673(00)00960-2
  21. Yang, F., Zhang, T., Ito, Y. Large-scale separation of resveratrol, anthraglycoside A and anthraglycoside B from Polygonum cuspidatum Sieb. et Zucc by high-speed counter- urrent chromatography. J Chromatogr A. 919(2):443-448, 2001 https://doi.org/10.1016/S0021-9673(01)00846-9
  22. Jayasuriya, H., Koonchanok, N.M., Geahlen, R.L., McLaughlin, J.L., Chang, C.J. Emodin, a protein tyrosine kinase inhibitor from Polygonum cuspidatum. J Nat Prod. 55(5):696-698, 1992 https://doi.org/10.1021/np50083a026
  23. Xiao, K., Xuan, L., Xu, Y., Bai, D., Zhong, D. Constituents from Polygonum cuspidatum. Chem Pharm Bull (Tokyo). 50(5):605-608, 2002 https://doi.org/10.1248/cpb.50.605
  24. Woo, J.H., Lim, J.H., Kim, Y.H., Suh, S.I., Min do, S., Chang, J.S., Lee, Y.H., Park, J.W., Kwon, T.K. Resveratrol inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting JNK and PKC delta signal transduction. Oncogene. 23(10):1845-1853, 2004 https://doi.org/10.1038/sj.onc.1207307
  25. Kim, M.S., Park, M.J., Kim, S.J., Lee, C.H., Yoo, H., Shin, S.H., Song, E.S., Lee, S.H. Emodin suppresses hyaluronic acid-induced MMP-9 secretion and invasion of glioma cells. Int J Oncol. 27(3):839-846, 2005
  26. 박래길, 오광록, 이광규, 문연자, 김정훈, 우원홍, 유향추출물의 HL-60 혈액암세포에서 세포사멸 유도효과. 약학회지 45(2):161-168, 2001
  27. Sato, H., Seiki, M. Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells. Oncogene, 8:395-405, 1993
  28. Woo, J.H., Park, J.W., Lee, S.H., Kim, Y.H., Lee, I.K., Gabrielson, E., Lee, S.H., Lee, H.J., Kho, Y.H., Kwon, T.K. Dykellic acid inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting nuclear factor kappa B transcriptional activity. Cancer Res. 63(12):3430-3434, 2003
  29. Lu, Y., Wahl, L.M. Production of matrix metalloproteinase-9 by activated human monocytes involves a phosphatidylinositol-3 kinase/Akt/IKKalpha/NF-kappaB pathway. J Leukoc Biol. 78(1):259-265, 2005 https://doi.org/10.1189/jlb.0904498