THE JOURNAL OF KOREAN ORIENTAL ONCOLOGY (대한한방종양학회지)

Korean Association of Traditional Oncology (대한암한의학회)
권호 표지

Anti-metastastic Effects of Xuefezhuyutang

혈부축어탕(血府逐瘀湯)이 암전이(癌轉移) 억제(抑制)에 미치는 영향(影響)

  • Lee, Jin-Hwa (Dept. of Oriental Pathology, College of Oriental Medicine, Kyung Hee University) ;
  • Shim, Bum-Sang (Dept. of Oriental Pathology, College of Oriental Medicine, Kyung Hee University) ;
  • Ahn, Kyoo-Seok (Oriental Pathology, College of Oriental Medicine, Kyung Hee University, Seoul, Korea) ;
  • Choi, Seung-Hoon (Dept. of Oriental Pathology, College of Oriental Medicine, Kyung Hee University)
  • Published : 1999.12.30
Download PDF
⟨ Previous Next ⟩

Abstract

To examine the effect of Xuefuzhuyutang on the metastasis of cancer, the following experiments were carried out. Before the main experiments, the cytotoxicity was measured by putting Xuefuzhuyutant sample in HT1080. Then zymography was made to examine the change of gelatinolytic activity. Western blotting was carried out to examine the changes of Fos, Jun, Ets, Erk, md JNK. In vitro invasion assay with transwells coated by collagen and matrigel was carried out. From the above results the following conclusions were obtained. 1. The experimental result about cytotoxicity of Xuefuzhuyutang agaitst HT1080 was a below. The stained cell count after being treated by by Xuefuzhuyutang sample $400{\mu}g/ml$ for 24 hours was 0.9% of total cells, and the stained cell count by Xuefuzhuyutang sample $100{\mu}g/ml$ was 1.5% of total cells. Both were near the level of control group which showed 0.6% stained. 2. The result of collagenase assay was as below. In Xuefuzhuyutang sample $400{\mu}g/ml$, MMP2 was reduced as compared with TPA control group, and the band of MMP-9 induced by TPA disapappeared. In Xuefuzhuyutang samle $800{\mu}g/ml$ both bands of MMP-2 and MMP-9 disapeared. 3. The results of western blots for Jun, Fos, Ets, Erk, JNK were a below. In Xuefuzhuyutang sample $200{\mu}g/ml$, Ets was reduced, and Jun, Fos were increased. 4 The result of invasion assay was as below. The number of cells which migrated across transwell membrane in Xuefuzhuyutang-treated group was less than that of control(+TPA) group. From the above results, it was concluded that Xuefuzhuyutang might inhibit the activity of collagenase not by the MMP-2, MMP-9 promoter but by the other way.

Keywords

References

  1. 활락효령단이 Angiogenesis억제기전에 미치는 영향 나기환
  2. 입안산이 Angiogenesis억제기전에 미치는 영향 이기룡
  3. 97국제어혈심포지움 논문집 수종어혈약물의 배합에 의한 항암 및 암전이 효과에 대한 연구 김성훈;김동희
  4. 개정판 종양학 서울대학교 의과대학(編)
  5. 제 4회 한중 학술세미나 발표논문집 죽엽석고탕가감방이 항암화학요법제의 세포독성과 종양세포의 라이소좀에 미치는 영향 전승훈(외)
  6. 제 4회 한중 학술대회 발표논문집 가미자도환의 항암 및 면역증강효과에 관한 실험적 연구 전영수;최승훈;안규석
  7. 동의종양학 최승훈
  8. 대한한방종양학회지 v.1 no.1 한의학의 종양에 대한 인식과 병리론 최승훈
  9. 혈부축어탕이 혈전증과 피하혈종에 미치는 영향 최승훈
  10. 의림개착평주 협서성중의연구소혁위회
  11. Molecular and cellular biology v.17 Transcriptional activation by p53 of the human type IV collagenase (Gelatinase A or Matrix metalloproteinase 2) promoter Bian, J.;Sun, Y.
  12. Critical reviews in eukaryotic gene expression v.7 no.1;2 Transcriptional control of matrix matalloproteinases and the tissue inhibitors of matrix matalloproteinases Boren, P.;Heller, R.A.
  13. J Biol Chem v.269 Retinoids modulate endothelial cell production of matrix-degrading proteases and tissue inhibitors of metalloproteinases (TIMP) Braunhut, S.J.;Moses, M.A.
  14. MOLECULAR BIOLOGY OF THE CELL Alberts, Bruce;Bray, Dennis;Lewis, Julian;Raff, Martin;Roberts, Keith;Watson, James D.
  15. Anal. Biochem. v.112 Western Blotting Burnette, W.H.
  16. Robbins pathologic basis of disease Cotran, R.S.;Robbins, S.L.;Kumar, V.
  17. International Review of Experimental Pathology v.16 Folkman, J.;Cotran, R.;Richterr, G.W.(ed.);Epstein, M.A.(ed.)
  18. Int J Cancer v.58 Human recombinant interferons-beta and -gamma decrease gelatinase production and invasion by human KG-s renal-carcinoma cells Gohji, K.(et al.)
  19. Lancet v.339 Biology of tumor metastasis Hart, I.R.;Saini, A.
  20. Cancer Res. v.33 Collagenolytic activities of squamous-cell carcinoma of skin Hashimoto, K.;Yamanishi, Y.;Maeyens, E.;Dabbous, M.K.;Kanzaki, T.
  21. Anal. Biochem. v.102 Electrophoretic analysis of plasminogen activators in ployacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates Heussen, C.;Dowdle, E.B.
  22. J. Biol. Chem. v.266 Complete structure of the human gene for 92-kDa type IV collagenase Huhtala, P.;Tuuttila, A.;Chow, L.T.;Lohi, J.;Keski-Oja, J.;Tryggvason, K.
  23. J Biol Chem v.269 1,25-Dihydroxyvitamin D3 dissociates production of interstitial collagenase and 92-kDa gelatinase in human mononuclear phagocytes Lacraz, S.(et al.)
  24. Nature v.227 Cleavage of strutural proteins during the assembly of the head of bacteriophage T4 Laemmli, U.K.
  25. Cell v.64 Cancer metastasis and angiogensis, An imbalance of positive and negative regulation Liotta, L.A.(et al.)
  26. J. Biol. Chem. v.268 Interleukin-1${\beta}$ and transforming growth factor-${\alpha}$/epidermal growth factor induce expression of Mr 95,000 type IV collagenase/gelatinase and interstitial fibroblast-type collagenase by rat mucosal keratinocytes Lyons, J.G.;Birkedal-Hansen, B.;Pierson, M.C.;Whitelock, J.M.;Birkedal-Hansen, H.
  27. JNCI v.74 Collagenase secretion by human breast neoplasm: A clinicopathologic investigation Ogilvie, D.J.;Hailey, J.A.;Juacaba, S.F.;Lee, E.C.G.;Tarin, D.
  28. Cancer Biology Ruddon, Raymond W.
  29. Oncogene v.8 Regulatory mechanism of 92 kDa type IV collagenase gene expression Sato, H.;Seiki, M.
  30. JBC v.264 Stetler-Stevenson(et al.)
  31. Mol. Cell. Biol. v.5 Thorgeirsson(et al.)
  32. Proc Natl Acd Sci USA v.90 Transforming growth factor ${\beta}$ enhances integrin expression and type IV collagenase secretion in human monocytes Wahl, S.M.;Allen, J.B.;Weeks, B.S.;Wong, H.L.;Klotman, P.E.
  33. J. Biol. Chem. v.264 SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrohpages Wilhelm, S.M.;Collier, I.E.;Marmer, B.L.;Eisen, A.Z.;Grant, G.A.;Goldberg, G.I.