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Volumn 66, Issue , 2008, Pages 335-359

Histone deacetylase inhibitors from microorganisms: The Astellas experience

Author keywords

[No Author keywords available]

Indexed keywords

3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 N ACETYLDINALINE; ANTINEOPLASTIC AGENT; APICIDIN; BUTYRIC ACID; CISPLATIN; CL 994; CRA 024871; DOXORUBICIN; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; MITOMYCIN C; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; PANOBINOSTAT; ROMIDEPSIN; SPIRUCHOSTATIN A; TRAPOXIN A; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT; YM 753; BIOLOGICAL PRODUCT; CYCLOPEPTIDE; DEPSIPEPTIDE; ENZYME INHIBITOR; HISTONE ACETYLTRANSFERASE;

EID: 42949141641     PISSN: 0071786X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-7643-8595-8_7     Document Type: Review
Times cited : (21)

References (96)
  • 1
    • 17844399025 scopus 로고    scopus 로고
    • Natural products to drugs: Natural product derived compounds in clinical trials
    • Butler MS (2005) Natural products to drugs: natural product derived compounds in clinical trials. Nat Prod Rep 22: 162-195
    • (2005) Nat Prod Rep , vol.22 , pp. 162-195
    • Butler, M.S.1
  • 2
    • 0042844744 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the period 1981-2002
    • Newman DJ, Cragg GM, Snader KM (2003) Natural products as sources of new drugs over the period 1981-2002. J Nat Prod 66: 1022-1037
    • (2003) J Nat Prod , vol.66 , pp. 1022-1037
    • Newman, D.J.1    Cragg, G.M.2    Snader, K.M.3
  • 3
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson CL, Laniel MA (2004) Histones and histone modifications. Curr Biol 14: R546-551
    • (2004) Curr Biol , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 4
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes TR, Thorne AW, Crane-Robinson C (1988) A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J 7: 1395-1402
    • (1988) EMBO J , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 5
    • 14844350172 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and cancer: From cell biology to the clinic
    • Hess-Stumpp H (2005) Histone deacetylase inhibitors and cancer: from cell biology to the clinic. Eur J Cell Biol 84: 109-121
    • (2005) Eur J Cell Biol , vol.84 , pp. 109-121
    • Hess-Stumpp, H.1
  • 6
    • 11844278521 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors
    • Monneret C (2005) Histone deacetylase inhibitors. Eur J Med Chem 40: 1-13
    • (2005) Eur J Med Chem , vol.40 , pp. 1-13
    • Monneret, C.1
  • 7
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG (2006) Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 6: 38-51
    • (2006) Nat Rev Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 8
    • 33144484589 scopus 로고    scopus 로고
    • Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene
    • Voelter-Mahlknecht S, Ho AD, Mahlknecht U (2005) Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene. Int J Mol Med 16: 589-598
    • (2005) Int J Mol Med , vol.16 , pp. 589-598
    • Voelter-Mahlknecht, S.1    Ho, A.D.2    Mahlknecht, U.3
  • 14
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW (2002) Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 1: 287-299
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 15
    • 0032989027 scopus 로고    scopus 로고
    • Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • Qiu L, Kelso MJ, Hansen C, West ML, Fairlie DP, Parsons PG (1999) Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate. Br J Cancer 80: 1252-1258
    • (1999) Br J Cancer , vol.80 , pp. 1252-1258
    • Qiu, L.1    Kelso, M.J.2    Hansen, C.3    West, M.L.4    Fairlie, D.P.5    Parsons, P.G.6
  • 19
    • 0037137896 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis
    • Kwon HJ, Kim MS, Kim MJ, Nakajima H, Kim KW (2002) Histone deacetylase inhibitor FK228 inhibits tumor angiogenesis. Int J Cancer 97: 290-296
    • (2002) Int J Cancer , vol.97 , pp. 290-296
    • Kwon, H.J.1    Kim, M.S.2    Kim, M.J.3    Nakajima, H.4    Kim, K.W.5
  • 22
    • 0032499756 scopus 로고    scopus 로고
    • p21 (WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells
    • Archer SY, Meng S, Shei A, Hodin RA (1998) p21 (WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc Natl Acad Sci USA 95: 6791-6796
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6791-6796
    • Archer, S.Y.1    Meng, S.2    Shei, A.3    Hodin, R.A.4
  • 23
    • 6044264858 scopus 로고    scopus 로고
    • FR901228, a novel histone deacetylase inhibitor, induces cell cycle arrest and subsequent apoptosis in refractory human pancreatic cancer cells
    • Sato N, Ohta T, Kitagawa H, Kayahara M, Ninomiya I, Fushida S, Fujimura T, Nishimura G, Shimizu K, Miwa K (2004) FR901228, a novel histone deacetylase inhibitor, induces cell cycle arrest and subsequent apoptosis in refractory human pancreatic cancer cells. Int J Oncol 24: 679-685
    • (2004) Int J Oncol , vol.24 , pp. 679-685
    • Sato, N.1    Ohta, T.2    Kitagawa, H.3    Kayahara, M.4    Ninomiya, I.5    Fushida, S.6    Fujimura, T.7    Nishimura, G.8    Shimizu, K.9    Miwa, K.10
  • 24
    • 11144358387 scopus 로고    scopus 로고
    • Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells
    • Guo F, Sigua C, Tao J, Bali P, George P, Li Y, Wittmann S, Moscinski L, Atadja P, Bhalla K (2004) Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells. Cancer Res 64: 2580-2589
    • (2004) Cancer Res , vol.64 , pp. 2580-2589
    • Guo, F.1    Sigua, C.2    Tao, J.3    Bali, P.4    George, P.5    Li, Y.6    Wittmann, S.7    Moscinski, L.8    Atadja, P.9    Bhalla, K.10
  • 25
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao Y, Gao Z, Marks PA, Jiang X (2004) Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci USA 101: 18030-18035
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4
  • 27
    • 33644836549 scopus 로고    scopus 로고
    • Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies
    • O'Connor OA, Heaney ML, Schwartz L, Richardson S, Willim R, MacGregor-Cortelli B, Curly T, Moskowitz C, Portlock C, Horwitz S et al (2006) Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies. J Clin Oncol 24: 166-173
    • (2006) J Clin Oncol , vol.24 , pp. 166-173
    • O'Connor, O.A.1    Heaney, M.L.2    Schwartz, L.3    Richardson, S.4    Willim, R.5    MacGregor-Cortelli, B.6    Curly, T.7    Moskowitz, C.8    Portlock, C.9    Horwitz, S.10
  • 31
    • 3042785975 scopus 로고    scopus 로고
    • A review of depsipeptide and other histone deacetylase inhibitors in clinical trials
    • Piekarz RL, Bates S (2004) A review of depsipeptide and other histone deacetylase inhibitors in clinical trials. Curr Pharm Des 10: 2289-2298
    • (2004) Curr Pharm Des , vol.10 , pp. 2289-2298
    • Piekarz, R.L.1    Bates, S.2
  • 35
    • 0141996376 scopus 로고    scopus 로고
    • Modulation of histone acetylation by [4-(acetylamino)-N-(2-amino-phenyl) benzamide in HCT-8 colon carcinoma
    • Kraker AJ, Mizzen CA, Hartl BG, Miin J, Allis CD, Merriman RL (2003) Modulation of histone acetylation by [4-(acetylamino)-N-(2-amino-phenyl) benzamide in HCT-8 colon carcinoma. Mol Cancer Ther 2: 401-408
    • (2003) Mol Cancer Ther , vol.2 , pp. 401-408
    • Kraker, A.J.1    Mizzen, C.A.2    Hartl, B.G.3    Miin, J.4    Allis, C.D.5    Merriman, R.L.6
  • 36
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272: 408-411
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 37
    • 0344431240 scopus 로고    scopus 로고
    • FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • Nakajima H, Kim YB, Terano H, Yoshida M, Horinouchi S (1998) FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor. Exp Cell Res 241: 126-133
    • (1998) Exp Cell Res , vol.241 , pp. 126-133
    • Nakajima, H.1    Kim, Y.B.2    Terano, H.3    Yoshida, M.4    Horinouchi, S.5
  • 38
    • 0028258610 scopus 로고    scopus 로고
    • Ueda H, Nakajima H, Hori Y, Fujita T, Nishimura M, Goto T, Okuhara M (1994) FR901228, A novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968 I. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity. J Antibiot 47: 301-310
    • Ueda H, Nakajima H, Hori Y, Fujita T, Nishimura M, Goto T, Okuhara M (1994) FR901228, A novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968 I. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity. J Antibiot 47: 301-310
  • 40
    • 0028299638 scopus 로고
    • FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968 II. Structure elucidation
    • Shigematsu N, Ueda H, Takase S, Tanaka H, Yamamoto K, Tada T (1994) FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968 II. Structure elucidation. J Antibiot 47: 311-314
    • (1994) J Antibiot , vol.47 , pp. 311-314
    • Shigematsu, N.1    Ueda, H.2    Takase, S.3    Tanaka, H.4    Yamamoto, K.5    Tada, T.6
  • 41
    • 0029785860 scopus 로고    scopus 로고
    • Total synthesis of the antitumor depsipeptide FR-901,228
    • Li KW, Wu J, Xing W, Simon JA (1996) Total synthesis of the antitumor depsipeptide FR-901,228. J Am Chem Soc 118: 7237-7238
    • (1996) J Am Chem Soc , vol.118 , pp. 7237-7238
    • Li, K.W.1    Wu, J.2    Xing, W.3    Simon, J.A.4
  • 42
    • 0028500561 scopus 로고
    • Action of FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968, on Ha-ras transformed NIH3T3 cells
    • Ueda H, Nakajima H, Hori Y, Goto T, Okuhara M (1994) Action of FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968, on Ha-ras transformed NIH3T3 cells. Biosci Biotech Biochem 58: 1579-1583
    • (1994) Biosci Biotech Biochem , vol.58 , pp. 1579-1583
    • Ueda, H.1    Nakajima, H.2    Hori, Y.3    Goto, T.4    Okuhara, M.5
  • 43
    • 0028267278 scopus 로고
    • FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968 III. Antitumor activities on experimental tumors in mice
    • Ueda H, Manda T, Matsumoto S, Mukumoto S, Nishigaki F, Kawamura I, Shimomura K (1994) FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum No. 968 III. Antitumor activities on experimental tumors in mice. J Antibiot 47: 315-323
    • (1994) J Antibiot , vol.47 , pp. 315-323
    • Ueda, H.1    Manda, T.2    Matsumoto, S.3    Mukumoto, S.4    Nishigaki, F.5    Kawamura, I.6    Shimomura, K.7
  • 44
    • 0023195737 scopus 로고
    • Effects of trichostatins on differentiation of murine erythroleukemia cells
    • Yoshida M, Nomura S, Beppu T (1987) Effects of trichostatins on differentiation of murine erythroleukemia cells. Cancer Res 47: 3688-3691
    • (1987) Cancer Res , vol.47 , pp. 3688-3691
    • Yoshida, M.1    Nomura, S.2    Beppu, T.3
  • 45
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, Beppu T (1990) Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 265: 17174-17179
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 46
    • 0023689244 scopus 로고
    • Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by trichostatin A
    • Yoshida M, Beppu T (1988) Reversible arrest of proliferation of rat 3Y1 fibroblasts in both the G1 and G2 phases by trichostatin A. Exp Cell Res 177: 122-131
    • (1988) Exp Cell Res , vol.177 , pp. 122-131
    • Yoshida, M.1    Beppu, T.2
  • 47
    • 0025083327 scopus 로고
    • Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells
    • Yoshida M, Hoshikawa Y, Koseki K, Mori K, Beppu T (1990) Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells. J Antibiot 43: 1101-1106
    • (1990) J Antibiot , vol.43 , pp. 1101-1106
    • Yoshida, M.1    Hoshikawa, Y.2    Koseki, K.3    Mori, K.4    Beppu, T.5
  • 48
    • 0001106950 scopus 로고
    • Expression of differentiation-related markers in teratocarcinoma cells via histone hyperacetylation by trichostatin A
    • Hoshikawa Y, Kijima M, Yoshida M, Beppu T (1991) Expression of differentiation-related markers in teratocarcinoma cells via histone hyperacetylation by trichostatin A. Agric Biol Chem 55: 1491-1495
    • (1991) Agric Biol Chem , vol.55 , pp. 1491-1495
    • Hoshikawa, Y.1    Kijima, M.2    Yoshida, M.3    Beppu, T.4
  • 49
    • 0026548820 scopus 로고
    • Morphological reversion of sis-transformed NIH3T3 cells by trichostatin A
    • Sugita K, Koizumi K, Yoshida H (1992) Morphological reversion of sis-transformed NIH3T3 cells by trichostatin A. Cancer Res 52: 168-172
    • (1992) Cancer Res , vol.52 , pp. 168-172
    • Sugita, K.1    Koizumi, K.2    Yoshida, H.3
  • 50
    • 0027971019 scopus 로고
    • Histone acetylation influences both gene expression and development of Xenopus laevis
    • Almouzni G, Khochbin S, Dimitrov S, Wolffe AP (1994) Histone acetylation influences both gene expression and development of Xenopus laevis. Dev Biol 165: 654-669
    • (1994) Dev Biol , vol.165 , pp. 654-669
    • Almouzni, G.1    Khochbin, S.2    Dimitrov, S.3    Wolffe, A.P.4
  • 51
    • 0028022785 scopus 로고
    • Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines
    • Hoshikawa Y, Kwon HJ, Yoshida M, Horinouchi S, Beppu T (1994) Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp Cell Res 214: 189-197
    • (1994) Exp Cell Res , vol.214 , pp. 189-197
    • Hoshikawa, Y.1    Kwon, H.J.2    Yoshida, M.3    Horinouchi, S.4    Beppu, T.5
  • 53
    • 0028201770 scopus 로고
    • Gene expression within a chromatin domain: The role of core histone hyperacetylation
    • Schlake T, Klehr-Wirth D, Yoshida M, Beppu T, Bode J (1994) Gene expression within a chromatin domain: the role of core histone hyperacetylation. Biochemistry 33: 4197-4206
    • (1994) Biochemistry , vol.33 , pp. 4197-4206
    • Schlake, T.1    Klehr-Wirth, D.2    Yoshida, M.3    Beppu, T.4    Bode, J.5
  • 54
    • 0028986992 scopus 로고
    • Trichostatin A inhibits both ras-induced neurite outgrowth of PC12 cells and morphological transformation of NIH3T3 cells
    • Futamura M, Monden Y, Okabe T, Fujita-Yoshigaki J, Yokoyama S, Nishimura S (1995) Trichostatin A inhibits both ras-induced neurite outgrowth of PC12 cells and morphological transformation of NIH3T3 cells. Oncogene 10: 1119-1123
    • (1995) Oncogene , vol.10 , pp. 1119-1123
    • Futamura, M.1    Monden, Y.2    Okabe, T.3    Fujita-Yoshigaki, J.4    Yokoyama, S.5    Nishimura, S.6
  • 55
    • 0029093123 scopus 로고
    • Temporally restricted spatial localization of acetylated isoforms of histone H4 and RNA polymerase II in the 2-cell mouse embryo
    • Worrad DM, Turner BM, Schultz RM (1995) Temporally restricted spatial localization of acetylated isoforms of histone H4 and RNA polymerase II in the 2-cell mouse embryo. Development 121: 2949-2959
    • (1995) Development , vol.121 , pp. 2949-2959
    • Worrad, D.M.1    Turner, B.M.2    Schultz, R.M.3
  • 56
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation
    • Van Lint C, Emiliani S, Ott M, Verdin E (1996) Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. EMBO J 15: 1112-1120
    • (1996) EMBO J , vol.15 , pp. 1112-1120
    • Van Lint, C.1    Emiliani, S.2    Ott, M.3    Verdin, E.4
  • 57
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett SE, Carmen AA, Kobayashi R, Bavykin S, Turner BM, Grunstein M (1996) HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci USA 93: 14503-14508
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1    Carmen, A.A.2    Kobayashi, R.3    Bavykin, S.4    Turner, B.M.5    Grunstein, M.6
  • 58
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 59
    • 33646002067 scopus 로고    scopus 로고
    • Chemistry and biology of chromatin remodeling agents: State of art and future perspectives of HDAC inhibitors
    • Rodriqueza M, Aquino M, Bruno I, De Martino G, Taddei M, Gomez-Paloma L (2006) Chemistry and biology of chromatin remodeling agents: State of art and future perspectives of HDAC inhibitors. Curr Med Chem 13: 1119-1139
    • (2006) Curr Med Chem , vol.13 , pp. 1119-1139
    • Rodriqueza, M.1    Aquino, M.2    Bruno, I.3    De Martino, G.4    Taddei, M.5    Gomez-Paloma, L.6
  • 62
    • 0037261269 scopus 로고    scopus 로고
    • Identification of thiols and glutathione conjugates of depsipeptide FK228 (FR901228), a novel histone protein deacetylase inhibitor, in the blood
    • Xiao JJ, Byrd J, Marcucci G, Grever M, Chan KK (2003) Identification of thiols and glutathione conjugates of depsipeptide FK228 (FR901228), a novel histone protein deacetylase inhibitor, in the blood. Rapid Commun Mass Spectrom 17: 757-766
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 757-766
    • Xiao, J.J.1    Byrd, J.2    Marcucci, G.3    Grever, M.4    Chan, K.K.5
  • 63
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint C, Emiliani S, Verdin E (1996) The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr 5: 245-253
    • (1996) Gene Expr , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 64
    • 0034086168 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells
    • Qiu L, Burgess A, Fairlie DP, Leonard H, Parsons PG, Gabrielli BG (2000) Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells. Mol Biol Cell 11: 2069-2083
    • (2000) Mol Biol Cell , vol.11 , pp. 2069-2083
    • Qiu, L.1    Burgess, A.2    Fairlie, D.P.3    Leonard, H.4    Parsons, P.G.5    Gabrielli, B.G.6
  • 66
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell RP Jr, He LZ, Richon V, Calleja E, Pandolfi PP (1998) Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J Natl Cancer Inst 90: 1621-1625
    • (1998) J Natl Cancer Inst , vol.90 , pp. 1621-1625
    • Warrell Jr, R.P.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 67
    • 0034548836 scopus 로고    scopus 로고
    • Up-regulation of costimulatory/adhesion molecules by histone deacetylase inhibitors in acute myeloid leukemia cells
    • Maeda T, Towatari M, Kosugi H, Saito H (2000) Up-regulation of costimulatory/adhesion molecules by histone deacetylase inhibitors in acute myeloid leukemia cells. Blood 96: 3847-3856
    • (2000) Blood , vol.96 , pp. 3847-3856
    • Maeda, T.1    Towatari, M.2    Kosugi, H.3    Saito, H.4
  • 68
    • 0033822112 scopus 로고    scopus 로고
    • P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228
    • Sandor V, Senderowicz A, Mertins S, Sackett D, Sausville E, Blagosklonny MV, Bates SE (2000) P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228. British J Cancer 83: 817-825
    • (2000) British J Cancer , vol.83 , pp. 817-825
    • Sandor, V.1    Senderowicz, A.2    Mertins, S.3    Sackett, D.4    Sausville, E.5    Blagosklonny, M.V.6    Bates, S.E.7
  • 69
    • 18544367699 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells
    • Kwon SH, Ahn SH, Kim YK, Bae GU, Yoon JW, Hong S, Lee HY, Lee YW, Lee HW, Han JW (2002) Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells. J Biol Chem 277: 2073-2080
    • (2002) J Biol Chem , vol.277 , pp. 2073-2080
    • Kwon, S.H.1    Ahn, S.H.2    Kim, Y.K.3    Bae, G.U.4    Yoon, J.W.5    Hong, S.6    Lee, H.Y.7    Lee, Y.W.8    Lee, H.W.9    Han, J.W.10
  • 70
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • Henderson C, Mizzau M, Paroni G, Maestro R, Schneider C, Brancolini C (2003) Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J Biol Chem 278: 12579-12589
    • (2003) J Biol Chem , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 71
    • 0035724488 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t(15;17)
    • Amin HM, Saeed S, Alkan S (2001) Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t(15;17). British J Haematology 115: 287-297
    • (2001) British J Haematology , vol.115 , pp. 287-297
    • Amin, H.M.1    Saeed, S.2    Alkan, S.3
  • 72
    • 16344380408 scopus 로고    scopus 로고
    • Involvement of the tumor necrosis factor (TNF)/TNF receptor system in leukemic cell apoptosis induced by histone deacetylase inhibitor depsipeptide (FK228)
    • Sutheesophon K, Nishimura N, Kobayashi Y, Furukawa Y, Kawano M, Itoh K, Kano Y, Ishii H, Furukawa Y (2005) Involvement of the tumor necrosis factor (TNF)/TNF receptor system in leukemic cell apoptosis induced by histone deacetylase inhibitor depsipeptide (FK228). J Cellular Physiology 203: 387-397
    • (2005) J Cellular Physiology , vol.203 , pp. 387-397
    • Sutheesophon, K.1    Nishimura, N.2    Kobayashi, Y.3    Furukawa, Y.4    Kawano, M.5    Itoh, K.6    Kano, Y.7    Ishii, H.8    Furukawa, Y.9
  • 73
    • 0031768386 scopus 로고    scopus 로고
    • Effects of a novel antitumor depsipeptide, FR901228, on human breast cancer cells
    • Rajgolikar G, Chan KK, Wang HC (1998) Effects of a novel antitumor depsipeptide, FR901228, on human breast cancer cells. Breast Cancer Res & Treatment 51: 29-38
    • (1998) Breast Cancer Res & Treatment , vol.51 , pp. 29-38
    • Rajgolikar, G.1    Chan, K.K.2    Wang, H.C.3
  • 74
    • 0042261694 scopus 로고    scopus 로고
    • Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors
    • Sasakawa Y, Naoe Y, Noto T, Inoue T, Sasakawa T, Matsuo M, Manda T, Mutoh S (2003) Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors. Biochem Pharmacology 66: 897-906
    • (2003) Biochem Pharmacology , vol.66 , pp. 897-906
    • Sasakawa, Y.1    Naoe, Y.2    Noto, T.3    Inoue, T.4    Sasakawa, T.5    Matsuo, M.6    Manda, T.7    Mutoh, S.8
  • 75
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity
    • Mie Lee Y, Kim SH, Kim HS, Jin Son M, Nakajima H, Jeong Kwon H, Kim KW (2003) Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity. Biochem Biophys Res Commun 300: 241-246
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 241-246
    • Mie Lee, Y.1    Kim, S.H.2    Kim, H.S.3    Jin Son, M.4    Nakajima, H.5    Jeong Kwon, H.6    Kim, K.W.7
  • 76
    • 0028283519 scopus 로고
    • Reversible transcriptional activation of mdr1 by sodium butyrate treatment of human colon cancer cells
    • Morrow CS, Nakagawa M, Goldsmith ME, Madden MJ, Cowan KH (1994) Reversible transcriptional activation of mdr1 by sodium butyrate treatment of human colon cancer cells. J Biol Chem 269: 10739-10746
    • (1994) J Biol Chem , vol.269 , pp. 10739-10746
    • Morrow, C.S.1    Nakagawa, M.2    Goldsmith, M.E.3    Madden, M.J.4    Cowan, K.H.5
  • 77
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • Gottesman MM, Fojo T, Bates SE (2002) Multidrug resistance in cancer: role of ATP-dependent transporters. Nat Rev Cancer 2: 48-58
    • (2002) Nat Rev Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 78
    • 0031861729 scopus 로고    scopus 로고
    • Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y
    • Jin S, Scotto KW (1998) Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y. Mol Cell Biol 18: 4377-4384
    • (1998) Mol Cell Biol , vol.18 , pp. 4377-4384
    • Jin, S.1    Scotto, K.W.2
  • 79
    • 0028030228 scopus 로고
    • Rhodamine efflux patterns predict P-glycoprotein substrates in the National Cancer Institute drug screen
    • Lee JS, Paull K, Alvarez M, Hose C, Monks A, Grever M, Fojo AT, Bates SE (1994) Rhodamine efflux patterns predict P-glycoprotein substrates in the National Cancer Institute drug screen. Mol Pharmacol 46: 627-638
    • (1994) Mol Pharmacol , vol.46 , pp. 627-638
    • Lee, J.S.1    Paull, K.2    Alvarez, M.3    Hose, C.4    Monks, A.5    Grever, M.6    Fojo, A.T.7    Bates, S.E.8
  • 82
    • 23044440043 scopus 로고    scopus 로고
    • Xiao JJ, Huang Y, Dai Z, Sadee W, Chen J, Liu S, Marcucci G, Byrd J, Covey JM, Wright J et al (2005) Chemoresistance to depsipeptide FK228 [(E)-(1S,4S,10S,21R)-7-[(Z)-ethylidene]-4,21-diisopropyl-2-oxa-12,13-dithia-5,8, 20,23-tetraazabicyclo[8,7,6]-tricos-16-ene-3,6,9,22-pentanone] is mediated by reversible MDR1 induction in human cancer cell lines. J Pharmacol Exp Ther 314: 467-475
    • Xiao JJ, Huang Y, Dai Z, Sadee W, Chen J, Liu S, Marcucci G, Byrd J, Covey JM, Wright J et al (2005) Chemoresistance to depsipeptide FK228 [(E)-(1S,4S,10S,21R)-7-[(Z)-ethylidene]-4,21-diisopropyl-2-oxa-12,13-dithia-5,8, 20,23-tetraazabicyclo[8,7,6]-tricos-16-ene-3,6,9,22-pentanone] is mediated by reversible MDR1 induction in human cancer cell lines. J Pharmacol Exp Ther 314: 467-475
  • 83
    • 33645069138 scopus 로고    scopus 로고
    • Increased MDR1 expression in normal and malignant peripheral blood mononuclear cells obtained from patients receiving depsipeptide (FR901228, FK228, N5C630176)
    • Robey RW, Zhan Z, Piekarz RL, Kayastha GL, Fojo T, Bates SE (2006) Increased MDR1 expression in normal and malignant peripheral blood mononuclear cells obtained from patients receiving depsipeptide (FR901228, FK228, N5C630176). Clin Cancer Res 12: 1547-1555
    • (2006) Clin Cancer Res , vol.12 , pp. 1547-1555
    • Robey, R.W.1    Zhan, Z.2    Piekarz, R.L.3    Kayastha, G.L.4    Fojo, T.5    Bates, S.E.6
  • 84
    • 0034913856 scopus 로고    scopus 로고
    • Low concentrations of the histone deacetylase inhibitor, depsipeptide (FR901228), increase expression of the Na(+)/I(-) symporter and iodine accumulation in poorly differentiated thyroid carcinoma cells
    • Kitazono M, Robey R, Zhan Z, Sarlis NJ, Skarulis MC, Aikou T, Bates S, Fojo T (2005) Low concentrations of the histone deacetylase inhibitor, depsipeptide (FR901228), increase expression of the Na(+)/I(-) symporter and iodine accumulation in poorly differentiated thyroid carcinoma cells. J Clin Endocrinology & Metab 86: 3430-3435
    • (2005) J Clin Endocrinology & Metab , vol.86 , pp. 3430-3435
    • Kitazono, M.1    Robey, R.2    Zhan, Z.3    Sarlis, N.J.4    Skarulis, M.C.5    Aikou, T.6    Bates, S.7    Fojo, T.8
  • 85
    • 2542616162 scopus 로고    scopus 로고
    • Synergistic effect of histone deacetylase inhibitors FK228 and m-carboxycinnamic acid bis-hydroxamide with proteasome inhibitors PSI and PS-341 against gastrointestinal adenocarcinoma cells
    • Adachi M, Zhang Y, Zhao X, Minami T, Kawamura R, Hinoda Y, Imai K (2004) Synergistic effect of histone deacetylase inhibitors FK228 and m-carboxycinnamic acid bis-hydroxamide with proteasome inhibitors PSI and PS-341 against gastrointestinal adenocarcinoma cells. Clin Cancer Res 10: 3853-3862
    • (2004) Clin Cancer Res , vol.10 , pp. 3853-3862
    • Adachi, M.1    Zhang, Y.2    Zhao, X.3    Minami, T.4    Kawamura, R.5    Hinoda, Y.6    Imai, K.7
  • 86
    • 6444226076 scopus 로고    scopus 로고
    • Depsipeptide enhances imatinib mesylate-induced apoptosis of Bcr-Abl-positive cells and ectopic expression of cyclin D1, c-Myc or active MEK abrogates this effect
    • Kawano T, Horiguchi-Yamada J, Iwase S, Akiyama M, Furukawa Y, Kan Y, Yamada H (2004) Depsipeptide enhances imatinib mesylate-induced apoptosis of Bcr-Abl-positive cells and ectopic expression of cyclin D1, c-Myc or active MEK abrogates this effect. Anticancer Res 24: 2705-2712
    • (2004) Anticancer Res , vol.24 , pp. 2705-2712
    • Kawano, T.1    Horiguchi-Yamada, J.2    Iwase, S.3    Akiyama, M.4    Furukawa, Y.5    Kan, Y.6    Yamada, H.7
  • 88
    • 0035098329 scopus 로고    scopus 로고
    • Construction of gene therapy vectors targeting thyroid cells: Enhancement of activity and specificity with histone deacetylase inhibitors and agents modulating the cyclic adenosine 3′,5′-monophosphate pathway and demonstration of activity in follicular and anaplastic thyroid carcinoma cells
    • Kitazono M, Chuman Y, Aikou T, Fojo T (2001) Construction of gene therapy vectors targeting thyroid cells: enhancement of activity and specificity with histone deacetylase inhibitors and agents modulating the cyclic adenosine 3′,5′-monophosphate pathway and demonstration of activity in follicular and anaplastic thyroid carcinoma cells. J Clin Endocrinology & Metabolism 86: 834-840
    • (2001) J Clin Endocrinology & Metabolism , vol.86 , pp. 834-840
    • Kitazono, M.1    Chuman, Y.2    Aikou, T.3    Fojo, T.4
  • 89
    • 85117737624 scopus 로고    scopus 로고
    • M Kitazono M, Rao VK, Robey R, Aikou T, Bates S, Fojo T, Goldsmith ME (2002) Histone deacetylase inhibitor FR901228 enhances adenovirus infection of hematopoietic cells. Blood 99: 2248-2251
    • M Kitazono M, Rao VK, Robey R, Aikou T, Bates S, Fojo T, Goldsmith ME (2002) Histone deacetylase inhibitor FR901228 enhances adenovirus infection of hematopoietic cells. Blood 99: 2248-2251
  • 90
    • 58849129614 scopus 로고    scopus 로고
    • International multicenter phase II study of the HDAC inhibitor depsipeptide (FK228) in cutaneous T-cell lymphoma (CTCL)-interim report
    • abstract 3063
    • Whittaker S, Robak T, Baran E, McCulloch W, Prentice AG (2006) International multicenter phase II study of the HDAC inhibitor depsipeptide (FK228) in cutaneous T-cell lymphoma (CTCL)-interim report. ASCO 2006 Annual Meeting: abstract 3063
    • (2006) ASCO 2006 Annual Meeting
    • Whittaker, S.1    Robak, T.2    Baran, E.3    McCulloch, W.4    Prentice, A.G.5
  • 96
    • 0942265466 scopus 로고    scopus 로고
    • Total synthesis of spiruchostatin A, a potent histone deacetylase inhibitor
    • Yurek-George A, Habens F, Brimmell M, Packham G, Ganesan A (2004) Total synthesis of spiruchostatin A, a potent histone deacetylase inhibitor. J Am Chem Soc 126: 1030-1031
    • (2004) J Am Chem Soc , vol.126 , pp. 1030-1031
    • Yurek-George, A.1    Habens, F.2    Brimmell, M.3    Packham, G.4    Ganesan, A.5


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