메뉴 건너뛰기




Volumn 2, Issue 3, 2005, Pages 150-157

Drug insight: Histone deacetylase inhibitors - Development of the new targeted anticancer agent suberoylanilide hydroxamic acid

Author keywords

Apoptosis; Hematologic malignancies; Histones; Solid tumors; Thioredoxin

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; 4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; 4 N ACETYLDINALINE; ANTHRACYCLINE DERIVATIVE; ANTINEOPLASTIC AGENT; ARYLBUTYRIC ACID DERIVATIVE; BORTEZOMIB; CARBOXYCINNAMIC ACID BISHYDROXAMIDE; FLAVOPIRIDOL; FLUDARABINE; FR 901228; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; IMATINIB; LBH 589A; LYSINE; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; NONHISTONE PROTEIN; REGULATOR PROTEIN; TRANSCRIPTION FACTOR; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 20444479514     PISSN: 17434254     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncponc0106     Document Type: Review
Times cited : (302)

References (47)
  • 1
    • 0242522928 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors
    • Miller TA et al. (2003) Histone deacetylase inhibitors. J Med Chem 46: 5097-5116
    • (2003) J. Med. Chem. , vol.46 , pp. 5097-5116
    • Miller, T.A.1
  • 2
    • 4344688693 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors
    • Marks PA et al. (2004) Histone deacetylase inhibitors. Adv Cancer Res 91: 137-168
    • (2004) Adv. Cancer Res. , vol.91 , pp. 137-168
    • Marks, P.A.1
  • 3
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M et al. (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
  • 4
    • 0141526319 scopus 로고    scopus 로고
    • Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases
    • Kyrylenko S et al. (2003) Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases. Cell Mol Life Sci 60: 1990-1997
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1990-1997
    • Kyrylenko, S.1
  • 5
    • 0141953928 scopus 로고    scopus 로고
    • The discovery of NVP-LAQ824: From concept to clinic
    • Remiszewski SW (2003) The discovery of NVP-LAQ824: from concept to clinic. Curr Med Chem 10: 2393-2402
    • (2003) Curr. Med. Chem. , vol.10 , pp. 2393-2402
    • Remiszewski, S.W.1
  • 6
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases
    • Furumai R et al. (2002) FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res 62: 4916-4921
    • (2002) Cancer Res. , vol.62 , pp. 4916-4921
    • Furumai, R.1
  • 7
    • 3042785975 scopus 로고    scopus 로고
    • A review of depsipeptide and other histone deacetylase inhibitors in clinical trials
    • Piekarz R and 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.1    Bates, S.2
  • 8
    • 0028269683 scopus 로고
    • A phase I and pharmacokinetic study of intravenous phenylacetate in patients with cancer
    • Thibault A et al. (1994) A phase I and pharmacokinetic study of intravenous phenylacetate in patients with cancer. Cancer Res 54: 1690-1694
    • (1994) Cancer Res. , vol.54 , pp. 1690-1694
    • Thibault, A.1
  • 9
    • 0033053292 scopus 로고    scopus 로고
    • Phase II study of phenylacetate in patients with recurrent malignant glioma: A North American Brain Tumor Consortium report
    • Chang SM et al. (1999) Phase II study of phenylacetate in patients with recurrent malignant glioma: a North American Brain Tumor Consortium report. J Clin Oncol 17: 984-990
    • (1999) J. Clin. Oncol. , vol.17 , pp. 984-990
    • Chang, S.M.1
  • 10
    • 3843151628 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor pivaloyloxymethyl butyrate (Pivanex, AN-9) in advanced non-small cell lung cancer
    • Reid T et al. (2004) Phase II trial of the histone deacetylase inhibitor pivaloyloxymethyl butyrate (Pivanex, AN-9) in advanced non-small cell lung cancer. Lung Cancer 45: 381-386
    • (2004) Lung Cancer , vol.45 , pp. 381-386
    • Reid, T.1
  • 11
    • 25144473548 scopus 로고    scopus 로고
    • A dose escalating phase I study with valproic acid (VPA) in patients with advanced cancer
    • ASCO Annual Meeting Proceedings (Post-Meeting Edition) [abstract #3169]
    • Atmaca A et al. (2004) A dose escalating phase I study with valproic acid (VPA) in patients with advanced cancer. ASCO Annual Meeting Proceedings (Post-Meeting Edition) [abstract #3169] J Clin Oncol 22 (Suppl)
    • (2004) J. Clin. Oncol. , vol.22 , Issue.SUPPL.
    • Atmaca, A.1
  • 12
    • 3142689788 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells
    • Lucas DM et al. (2004) The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells. Leukemia 18: 1207-1214
    • (2004) Leukemia , vol.18 , pp. 1207-1214
    • Lucas, D.M.1
  • 13
    • 0000165430 scopus 로고    scopus 로고
    • A Phase I dose-finding study of CI-994 in combination with capecitabine in patients with advanced solid tumors
    • [abstract #345]
    • Kimmel KA et al. (2001) A Phase I dose-finding study of CI-994 in combination with capecitabine in patients with advanced solid tumors. [abstract #345] Proc Am Soc Clin Oncol 87: a345
    • (2001) Proc. Am. Soc. Clin. Oncol. , vol.87
    • Kimmel, K.A.1
  • 14
    • 0030069082 scopus 로고    scopus 로고
    • Deviant nucleosomes: The functional specialization of chromatin
    • Wolffe AP and Pruss D (1996) Deviant nucleosomes: the functional specialization of chromatin. Trends Genet 12: 58-62
    • (1996) Trends Genet. , vol.12 , pp. 58-62
    • Wolffe, A.P.1    Pruss, D.2
  • 15
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K et al. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389: 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1
  • 16
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T and Allis CD (2001) Translating the histone code. Science 293: 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 18
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W et al. (2003) Binary switches and modification cassettes in histone biology and beyond. Nature 425: 475-479
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1
  • 19
    • 0842277812 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1
    • Gui CY et al. (2004) Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1. Proc Natl Acad Sci U S A 101: 1241-1246
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1241-1246
    • Gui, C.Y.1
  • 20
    • 0141953936 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: From chromatin remodeling to experimental cancer therapeutics
    • Arts J et al. (2003) Histone deacetylase inhibitors: from chromatin remodeling to experimental cancer therapeutics. Curr Med Chem 10: 2343-2350
    • (2003) Curr. Med. Chem. , vol.10 , pp. 2343-2350
    • Arts, J.1
  • 21
    • 0141570564 scopus 로고    scopus 로고
    • Role of class I and class II histone deacetylases in carcinoma cells using siRNA
    • Glaser KB et al. (2003) Role of class I and class II histone deacetylases in carcinoma cells using siRNA. Biochem Biophys Res Commun 310: 529-536
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 529-536
    • Glaser, K.B.1
  • 22
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress WD and Seto E (2000) Histone deacetylases, transcriptional control, and cancer. J Cell Physiol 184: 1-16
    • (2000) J. Cell Physiol. , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 23
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • de Ruijter AJ et al. (2003) Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem J 370 (Part 3): 737-749
    • (2003) Biochem. J. , vol.370 , Issue.PART 3 , pp. 737-749
    • de Ruijter, A.J.1
  • 24
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones PA and Baylin SB (2002) The fundamental role of epigenetic events in cancer. Nat Rev Genet 3: 415-428
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 25
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone RW and Licht JD (2003) Histone deacetylase inhibitors in cancer therapy: is transcription the primary target? Cancer Cell 4: 13-18
    • (2003) Cancer Cell , vol.4 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 26
    • 0035189761 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia
    • He LZ et al. (2001) Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia. J Clin Invest 108: 1321-1330
    • (2001) J. Clin. Invest. , vol.108 , pp. 1321-1330
    • He, L.Z.1
  • 27
    • 0035339491 scopus 로고    scopus 로고
    • Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome
    • Murata T et al. (2001) Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome. Hum Mol Genet 10: 1071-1076
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1071-1076
    • Murata, T.1
  • 28
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin MS (1999) Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401: 188-193
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1
  • 29
    • 1842830815 scopus 로고    scopus 로고
    • Microarray profiling of the effects of histone deacetylase inhibitors on gene expression in cancer cell lines
    • Gray SG et al. (2004) Microarray profiling of the effects of histone deacetylase inhibitors on gene expression in cancer cell lines. Int J Oncol 24: 773-795
    • (2004) Int. J. Oncol. , vol.24 , pp. 773-795
    • Gray, S.G.1
  • 30
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM et al. (2000) Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci USA 97: 10014-10019
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10014-10019
    • Richon, V.M.1
  • 31
    • 9144220841 scopus 로고    scopus 로고
    • Transcriptional signature of histone deacetylase inhibition in multiple myeloma: Biological and clinical implications
    • Mitsiades CS et al. (2004) Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications. Proc Natl Acad Sci U S A 101: 540-545
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 540-545
    • Mitsiades, C.S.1
  • 32
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
    • Butler LM et al. (2002) The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc Natl Acad Sci U S A 99: 11700-11705
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11700-11705
    • Butler, L.M.1
  • 33
    • 0042704723 scopus 로고    scopus 로고
    • Tumor cell-selective cytotoxicity by targeting cell cycle checkpoints
    • Warrener R et al. (2003) Tumor cell-selective cytotoxicity by targeting cell cycle checkpoints. FASEB J 17: 1550-1552
    • (2003) FASEB J. , vol.17 , pp. 1550-1552
    • Warrener, R.1
  • 34
    • 0032989027 scopus 로고    scopus 로고
    • Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • Qiu L et al. (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
  • 35
    • 0036261826 scopus 로고    scopus 로고
    • The diversity of acetylated proteins
    • reviews 0006
    • Polevoda B and Sherman F (2002) The diversity of acetylated proteins. Genome Biol 3: reviews 0006
    • (2002) Genome Biol. , vol.3
    • Polevoda, B.1    Sherman, F.2
  • 36
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T (2000) Acetylation: a regulatory modification to rival phosphorylation? EMBO J 19: 1176-1179
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 37
    • 2542523228 scopus 로고    scopus 로고
    • Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors
    • Pei XY et al. (2004) Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors. Clin Cancer Res 10: 3839-3852
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3839-3852
    • Pei, X.Y.1
  • 38
    • 0345734267 scopus 로고    scopus 로고
    • Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells
    • Rahmani M et al. (2003) Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells. Cancer Res 63: 8420-8427
    • (2003) Cancer Res. , vol.63 , pp. 8420-8427
    • Rahmani, M.1
  • 39
    • 12444321545 scopus 로고    scopus 로고
    • Phase I clinical trial of histone deacetylase inhibitor: Suberoylanilide hydroxamic acid administered intravenously
    • Kelly WK et al. (2003) Phase I clinical trial of histone deacetylase inhibitor: suberoylanilide hydroxamic acid administered intravenously. Clin Cancer Res 9: 3578-3588
    • (2003) Clin. Cancer Res. , vol.9 , pp. 3578-3588
    • Kelly, W.K.1
  • 40
    • 20444435915 scopus 로고    scopus 로고
    • Phase II trial of oral suberoylanilide hydroxamic acid (SAHA) for cutaneous T-cell lymphoma (CTCL) and peripheral T-cell lymphoma (PTCL)
    • [abstract #625]
    • Duvic M et al. (2003) Phase II trial of oral suberoylanilide hydroxamic acid (SAHA) for cutaneous T-cell lymphoma (CTCL) and peripheral T-cell lymphoma (PTCL). [abstract #625] Proc Am Soc Hematol
    • (2003) Proc. Am. Soc. Hematol.
    • Duvic, M.1
  • 41
    • 28644438582 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Novel targeted anti-cancer agents
    • (Ed. Esteller M) Boston, Dordrecht, London: Kluwer Academic Publisher, in press
    • Marks PA and Kelly WK Histone deacetylase inhibitors: novel targeted anti-cancer agents. In DNA Methylation Epigenetics and Metastasis. (Ed. Esteller M) Boston, Dordrecht, London: Kluwer Academic Publisher, in press
    • DNA Methylation Epigenetics and Metastasis
    • Marks, P.A.1    Kelly, W.K.2
  • 42
    • 20044390016 scopus 로고    scopus 로고
    • Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitor
    • Ungerstedt JS et al. (2005) Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitor. Proc Natl Acad Sci U S A 102: 673-678
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 673-678
    • Ungerstedt, J.S.1
  • 43
    • 0042090495 scopus 로고    scopus 로고
    • Novel mechanisms of apoptosis induced by histone deacetylase inhibitors
    • Peart MJ et al. (2003) Novel mechanisms of apoptosis induced by histone deacetylase inhibitors. Cancer Res 63: 4460-4471
    • (2003) Cancer Res. , vol.63 , pp. 4460-4471
    • Peart, M.J.1
  • 44
    • 0034665124 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo
    • Butler LM et al. (2000) Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo. Cancer Res 60: 5165-5170
    • (2000) Cancer Res. , vol.60 , pp. 5165-5170
    • Butler, L.M.1
  • 45
    • 21244464349 scopus 로고    scopus 로고
    • Phase I study of the oral histone deacetylase inhibitor: Suberoylanilide hydroxamic acid (SAHA), in patients with advanced cancer
    • in press
    • Kelly WK et al: Phase I study of the oral histone deacetylase inhibitor: suberoylanilide hydroxamic acid (SAHA), in patients with advanced cancer. J Clin Oncol, in press
    • J. Clin. Oncol.
    • Kelly, W.K.1
  • 46
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report
    • Piekarz RL et al. (2001) Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report. Blood 98: 2865-2868
    • (2001) Blood , vol.98 , pp. 2865-2868
    • Piekarz, R.L.1
  • 47
    • 2942535832 scopus 로고    scopus 로고
    • T-cell lymphoma as a model for the use of histone deacetylase inhibitors in cancer therapy: Impact of depsipeptide on molecular markers, therapeutic targets, and mechanisms of resistance
    • Piekarz RL et al. (2004) T-cell lymphoma as a model for the use of histone deacetylase inhibitors in cancer therapy: impact of depsipeptide on molecular markers, therapeutic targets, and mechanisms of resistance. Blood 103: 4636-4643
    • (2004) Blood , vol.103 , pp. 4636-4643
    • Piekarz, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.