Histone deacetylase inhibitors

被引:403
作者
Marks, PA [1 ]
Richon, VM
Miller, T
Kelly, WK
机构
[1] Mem Sloan Kettering Canc Ctr, New York, NY 10021 USA
[2] Aton Pharma, Tarrytown, NY 10591 USA
来源
ADVANCES IN CANCER RESEARCH, VOL 91 | 2004年 / 91卷
关键词
D O I
10.1016/S0065-230X(04)91004-4
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
The base sequence of DNA provides the genetic code for proteins. The regulation of expression or suppression of gene transcription is largely determined by the structure of the chromatin-referred to as epigenetic gene regulation (Agaliori et al., 2002: Jenuwein and Allis, 2001; Richards and Elgin, 2002; Spotswood and Turner, 2002; Zhang and Reinberg, 2001). Posttranslational modifications of the histories of chromatin play an important role in regulating gene expression. Some of the most extensively studied epigenetic modifications involve acetylation/deacetylation of lysines in the tails of the core histones, which is controlled by the action of histone deacetylases (HDACs) and histone aceryltransferases (HATs). A controlled balance between histone acerylation and deacetylation appears to be essential for normal cell growth (Waterborg. 2002). Alterations in the structure or expression of HATs and HDACs occur in many cancers (Jones and Baylin, 2002; Marks et al., 2001, 2003; Timmermann et al.. 2001; Wang et al., 2001). A structurally diverse group of molecules has been developed that can inhibit HDACs (HDACi) (Arts et al., 2003; Bouchain and Delorme, 2003; Curtin and Glaser, 2003; Johnstone and Licht, 2003; Marks et al., 2003, Remiszewski, 2003: Richon e. al., 1998; Yoshida et al., 2003). These inhibitors induce growth arrest, differentiation, and/or apoptosis of cancer cells in vitro and in in vivo tumor-bearing animal models. Clinical trials with several of these agents have shown that certain HDACi have antitumor activity against various cancers at doses that are well tolerated by patients (Gottlicher et al.,. 200 1: Kelly et al., 2002a,b; Piekarz et al., 2001; Wozniak et al.. 1999). (C) 2004 Elsevier Inc.
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页码:137 / +
页数:34
相关论文
共 137 条
  • [1] Deciphering the transcriptional histone acetylation code for a human gene
    Agalioti, T
    Chen, GY
    Thanos, D
    [J]. CELL, 2002, 111 (03) : 381 - 392
  • [2] Ardizzoni A, 2002, TUMORI J, pS52
  • [3] Histone deacetylase inhibitors: From chromatin remodeling to experimental cancer therapeutics
    Arts, J
    de Schepper, S
    Van Emelen, K
    [J]. CURRENT MEDICINAL CHEMISTRY, 2003, 10 (22) : 2343 - 2350
  • [4] Direct interaction of Ca2+/calmodulin inhibits histone deacetylase 5 repressor core binding to myocyte enhancer factor 2
    Berger, I
    Bieniossek, C
    Schaffitzel, C
    Hassler, M
    Santelli, E
    Richmond, TJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (20) : 17625 - 17635
  • [5] Antineoplastic action of 5-aza-2′-deoxycytidine and phenylbutyrate on human lung carcinoma cells
    Boivin, AJ
    Momparler, LF
    Hurtubise, A
    Momparler, RL
    [J]. ANTI-CANCER DRUGS, 2002, 13 (08) : 869 - 874
  • [6] Novel hydroxamate and anilide derivatives as potent histone deacetylase inhibitors: Synthesis and antiproliferative evaluation
    Bouchain, G
    Delorme, D
    [J]. CURRENT MEDICINAL CHEMISTRY, 2003, 10 (22) : 2359 - 2372
  • [7] The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
    Butler, LM
    Zhou, XB
    Xu, WS
    Scher, HI
    Rifkind, RA
    Marks, PA
    Richon, VM
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (18) : 11700 - 11705
  • [8] Butler LM, 2000, CANCER RES, V60, P5165
  • [9] Butler LM, 2001, CLIN CANCER RES, V7, P962
  • [10] Carducci M., 1997, Anticancer Research, V17, P3972