Archives of Pharmacal Research

  • 제27권5호
  • /
  • Pages.554-561
  • /
  • 2004
  • /
  • 0253-6269(pISSN)
  • /
  • 1976-3786(eISSN)
대한약학회 (The Pharmaceutical Society of Korea)
권호 표지

Estrogen Receptor Enhances the Antiproliferative Effects of Trichostatin A and HC-toxin in Human Breast Cancer Cells

  • 발행 : 2004.05.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Trichostatin A, an antifungal antibiotics, and HC-toxin are potent and specific inhibitors of histone deacetylase activity. Histone deacetylase inhibitors are new class of chemotherapeutic drugs able to induce tumor cell apoptosis and/or cell cycle arrest. In this study, the antiproliferative activities of trichostatin A and HC-toxin were compared between estrogen receptor positive human breast cancer cell MCF-7 and estrogen receptor negative human breast cancer cell MDA-MB-468. Trichostatin A and HC-toxin showed potent antiproliferative activity in both MCF-7 and MDA-MB-468 cells. In MCF-7 cells that contain high level estrogen receptor, trichostatin A and HC-toxin brought about three-times more potent cell growth inhibitory effect than estrogen receptor negative MDA-MB-468 cells. Both trichostatin A and HC-toxin showed cell cycle arrest at G$_2$/M phases of MCF-7 and MDA-MB-468 cells in a dose- and time- depen- dent manner. Trichostatin A and HC-toxin also induced apoptosis from MCF-7 and MDA-MB-468 cells in a dose- and time-dependent manner. Results of this study suggested that antipro-liferative effects of trichostatin A and HC-toxin might be involved in estrogen receptor signaling pathway, but cell cycle arrest and apoptosis of trichostatin A and HC-toxin might not be involved in estrogen receptor system of human breast cancer cells.

키워드

참고문헌

  1. Archer, S. Y., Meng, S., Shei, A., and Hodin, R. A., p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc. Natl. Acad. Sci. U.S.A., 95, 6791-6796 (1998) https://doi.org/10.1073/pnas.95.12.6791
  2. Bannister, A. J. and Miskam E. A., Regulation of gene expression by transcription factor acetylation. Cell Mol. Life Sci., 57, 1184-1192 (2000) https://doi.org/10.1007/PL00000758
  3. Bernhard, D., Loffler, M., Hartmann, B. L., Yoshida, M., Kofler, R., and Csordas, A., Interaction between dexamethasone and butyrate in apoptosis induction: non-additive in thymocytes and synergistic in a T cell-derived leukemia cell line. Cell Death Different., 6, 609-617 (1999) https://doi.org/10.1038/sj.cdd.4400531
  4. Boyes, J., Byfield, P., Nakatani, Y., and Ogryzko, V., Regulation of activity of the transcription factor GATA-1 by acetylation. Nature, 396, 594-598 (1998) https://doi.org/10.1038/25166
  5. Brehm, A., Miska, E. A., McCance, D. J., Reid, J. L., Bannister, A. J., and Kouzarides, T., Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature, 391, 597-601 (1998) https://doi.org/10.1038/35404
  6. Cameron, E. E., Bachman, K. E., Myohanen, S., Herman, J. G., and Baylin, S. B., Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat. Genet., 21, 103-107 (1999) https://doi.org/10.1038/5047
  7. Chang, T. H. and Szabo, E., Enhanced growth inhibition by combination differentiation therapy with ligands of peroxisome proliferator-activated receptor-${\gamma}$ and inhibitors of histone deacetylase in adenocarcinoma of the lung. Clin. Cancer Res., 8, 1206-1212 (2002)
  8. Eden, S., Hashimshony, T., Keshet, I., Cedar, H., and Thorne, A.W., DNA methylation models histone acetylation. Nature, 394, 842 (1998) https://doi.org/10.1038/29680
  9. Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., and Pavletich, N. P., Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature, 401, 188-193 (1999) https://doi.org/10.1038/43710
  10. Fuks, F., Burgers, W. A., Brehm, A., Hughes-Davies, L., and Kouzarides, T., DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat. Genet., 24, 2488-2491 (2000)
  11. Futamura, M., Monden, Y., Okabe, T., Fujita-Yoshigaki, J., Yokoyama, S., and Nishimura, S., Trichostatin A inhibits both ras-induced neurite outgrowth of PC12 cells and morphological transformation of NIH3T3 cells. Oncogene, 10, 1119-1123 (1995)
  12. Glick, R. D., Swendeman, S. L., and Coffey, D. C., Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/ CD95 ligand expression in human neuroblastoma. Cancer Res., 59, 4392-4399 (1999)
  13. Gray, S. G., Yakovleva, T., Hartmann, W., Tally, M., Bakalkin, G., and Ekstrom, T. J., IGF-II enhances trichostatin A-induced TGFbeta1 and p21(Waf1, Cip1, sdi1) expression in Hep3B cells. Exp. Cell Res., 253, 618-628 (1999) https://doi.org/10.1006/excr.1999.4661
  14. Greenspan, P., Mayer, E. P., and Fowler, S. D., Nile red: a selective fluorescent stain for intracellular lipid droplets. J. Cell Biol., 100, 965-973 (1985) https://doi.org/10.1083/jcb.100.3.965
  15. Grignani, F., De Matteis, S., and Nervi, C., et al., Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. Nature, 391, 815-818 (1998) https://doi.org/10.1038/35901
  16. Grunstein, M., Histone acetylation in chromatin structure and transcription. Nature, 389, 349-352 (1997) https://doi.org/10.1038/38664
  17. Hoshikawa, Y., Kwon, H. J., Yoshida, M., Horinouchi, S., and Beppu, T., Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp. Cell Res., 214, 189-197 (1994) https://doi.org/10.1006/excr.1994.1248
  18. Huang, H., Reed, C. P., Zhang, J. S., Shridhar, V., Wang, L., and Smith, D. I., Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. Cancer Res., 59, 2981-2188 (1999)
  19. Kitamura, K., Hoshi, S., Koike, M., Kiyoi, H., Saito, H., and Naoe, T., Histone deacetylase inhibitor but not arsenic trioxide differentiates acute promyelocytic leukaemia cells with t(11;17) in combina-tion with all-trans retinoic acid. Br. J. Haematol., 108, 696-702 (2000) https://doi.org/10.1046/j.1365-2141.2000.01933.x
  20. Koyama, Y., Adachi, M., Sekiya, M., Takekawa, M., and Imai, K., Histone deacetylase inhibitors suppress IL-2-mediated gene expression prior to induction of apoptosis. Blood, 96, 1490-1495 (2000)
  21. Kuo, M. H. and Allis, C. D., Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays, 20, 615-626 (1998) https://doi.org/10.1002/(SICI)1521-1878(199808)20:8<615::AID-BIES4>3.0.CO;2-H
  22. Laherty, C. D., Yang, W. M., Sun, J. M., Davie, J. R., Seto, E., and Eisenman, R. N., Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell, 89, 349-356 (1997) https://doi.org/10.1016/S0092-8674(00)80215-9
  23. Lee, E., Furukubo, T., Miyabe, T., Yamauchi, A., and Kariya, K., Involvement of histone hyperacetylation in triggering DNA fragmentation of rat thymocytes undergoing apoptosis. FEBS Lett., 395, 183-187 (1996) https://doi.org/10.1016/0014-5793(96)01033-2
  24. Lin, R. J., Nagy, L., Inoue, S., Shao, W., Miller, Jr, W. H., and Evans, R. M., Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature, 391, 811-814 (1998) https://doi.org/10.1038/35895
  25. Magnaghi-Jaulin, L., Groisman, R., Naguibneva, I., Robin, P., Trouche, D., and Harel-Bellan, A., Histone deacetylase and retinoblastoma protein. Bull. Cancer, 85, 606-607 (1998)
  26. Medina, V., Edmonds, B., Young, G. P., James, R., Appleton, S., and Zalewski, P. D., Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res., 57, 3697-3707 (1997)
  27. Pazin, M. J. and Kadonage, J. T., What's Up and Down with Histone Deacetylation and Transcription. Cell, 89, 325-328 (1997) https://doi.org/10.1016/S0092-8674(00)80211-1
  28. Nusse, M., Beisker, W., Hoffmann, C., and Tarnok, A., Flow cytometric analysis of G1- and G2/M-phase subpopulations in mammalian cell nuclei using side scatter and DNA content measurements. Cytometry, 11, 813-821 (1990) https://doi.org/10.1002/cyto.990110707
  29. Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., and Nakatani, Y., The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell, 87, 953-959 (1996) https://doi.org/10.1016/S0092-8674(00)82001-2
  30. Rashid, S. F., Moore, J. S., Walker, E., Driver, P. M., Engel, J., Edwards, C. E., Brown, G., Uskokovic, M. R., and Campbell, M. J., Synergistic growth inhibition of prostate cancer cells by $1{\alpha}$,25 dihydroxyvitamin $D_{3}$ and its 19-nor-hexafluoride analogs in combination with either sodium butyrate or trichostatin A. Oncogene, 20, 1860-1872 (2001) https://doi.org/10.1038/sj.onc.1204269
  31. Richon, V. M., Webb, Y., Merger, R., Sheppard, T., Jursic, B., Ngo, L., Civoli, F., Breslow, R., Rifkind, R. A., and Marks, P. A., Second generation hybrid polar compounds are potent inducers of transformed cell differentiation. Proc. Natl. Acad. Sci. U.S.A., 93, 5705-5708 (1996) https://doi.org/10.1073/pnas.93.12.5705
  32. Robertson, K. D., Ait-Si-Ali, S., Yokochi, T., Wade, P. A., Jones, P. L., and Wolffe, A. P., DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat. Genet., 25, 338-342 (2000) https://doi.org/10.1038/77124
  33. Rountree, M. R., Bachman, K. E., and Baylin, S. B., DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat. Genet., 25, 269-277 (2000) https://doi.org/10.1038/77023
  34. Sealy, L. and Chalkley, R., DNA associated with hyperacetylated histone is preferentially digested by DNase I. Nucleic Acids Res., 5, 1863-1876 (1978) https://doi.org/10.1093/nar/5.6.1863
  35. Sowa, Y., Orita, T. and Hiranabe-Minamikawa, S., et al., Histone deacetylase inhibitor activates the p21/WAF1/Cip1 gene promoter through the Sp1 sites. Ann. NY Acad. Sci., 886, 195-199 (1999) https://doi.org/10.1111/j.1749-6632.1999.tb09415.x
  36. Spencer, T. E., Jenster, G., Burcin, M. M., Allis, C. D., Zhou, J., Mizzen, C. A., McKenna, N. J., Onate, S. A., Tsai, S. Y., and Tsai, M. J., O'Malley, B.W., Steroid receptor coactivator-1 is a histone acetyltransferase. Nature, 389, 194-198 (1997) https://doi.org/10.1038/38304
  37. Tanaka, M., Mullauer, L., and Ogiso, Y. et al., Gelsolin: a candidate for suppressor of human baldder cancer. Cancer Res., 55, 3228-3232 (1995)
  38. Van Lint, C., Emiliani, S., and Verdin, E., The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr., 5, 245-253 (1996)
  39. Vigushin, D. M., Ali, S., and Pace, P. E. et al., Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo. Clin. Cancer Res., 7, 971-976 (2001)
  40. Wahrman, M. Z., Gagnier, S. E., Kobrin, D. R., Higgins, P. J., and Augenlicht, L. H., Cellular and molecular changes in 3T3 cells transformed spontaneously or by DNA transfection. Tumour Biol., 6, 41-56 (1985)
  41. Wang, C., Fu, M., and Angeletti, R. H. et al., Direct acetylation of the estrogen receptor alpha hinge region by p300 regulates transactivation and hormone sensitivity. J. Biol. Chem., 276, 18375-18383 (2001) https://doi.org/10.1074/jbc.M100800200
  42. Wang, E. and Goldberg, A. R., Changes in microfilament organization and surface topogrophy upon transformation of chick embryo fibroblasts with Rous sarcoma virus. Proc. Natl. Acad. Sci. USA., 73, 4065-4069 (1976) https://doi.org/10.1073/pnas.73.11.4065
  43. Yang, X., Ferguson, A. T., and Nass, S. J. et al., Transcriptional activation of estrogen receptor alpha in human breast cancer cells by histone deacetylase inhibition. Cancer Res., 60, 6890-6894 (2000)
  44. Yoshida, M., Horinouchi, S., and Beppu, T., Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. BioEssays, 17, 423-430 (1995) https://doi.org/10.1002/bies.950170510
  45. Zhu, W. G., Lakshmanan, R. R., Beal, M. D., and Otterson, G. A., DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res., 61, 1327-1333 (2001)