HDACi - Targets beyond chromatin

被引：127
作者：
Buchwald, Marc [1 ]
Kraemer, Oliver H. [1 ]
Heinzel, Thorsten [1 ]
机构：
[1] Univ Jena, CMB, Inst Biochem & Biophys, D-07745 Jena, Germany
来源：
CANCER LETTERS | 2009年 / 280卷 / 02期
关键词：
Acetylation; Proteasomal degradation; STATs; NF-kappaB; Signaling crosstalk; NF-KAPPA-B; HISTONE-DEACETYLASE INHIBITORS; NECROSIS-FACTOR-ALPHA; PROTEASOME INHIBITOR; PROTEIN-KINASE; VALPROIC ACID; CANCER-CELLS; IFN-GAMMA; TRANSCRIPTIONAL ACTIVATION; STIMULATED TRANSCRIPTION;
D O I：
10.1016/j.canlet.2009.02.028
中图分类号：
R73 [肿瘤学];
学科分类号：
100214 ;
摘要：
Histone deacetylases (HDACs) play an important role in gene regulation. Inhibitors of HDACs (HDACi) are novel anti-cancer drugs, which induce histone (hyper-) acetylation and Counteract aberrant gene repression. On the other hand, HDACi treatment can also result in decreased gene expression, and targeting HDACs affects more than chromatin. Recently, HDACi were shown to evoke non-histone protein acetylation, which can alter signaling networks relevant for tumorgenesis. Furthermore, HDACi can promote the degradation of (proto-) oncoproteins. Here, we summarize these findings and discuss how these substances could be beneficial for the treatment and prevention of human ailments, such as cancer and unbalanced immune functions. (C) 2009 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码：160 / 167
页数：8
相关论文
共 87 条
  • [1] Histone deacetylase inhibitor trichostatin a represses estrogen receptor α-dependent transcription and promotes proteasomal degradation of cyclin D1 in human breast carcinoma cell lines
    Alao, JP
    Lam, EWF
    Ali, S
    Buluwela, L
    Bordogna, W
    Lockey, P
    Varshochi, R
    Stavropoulou, AV
    Coombes, RC
    Vigushin, DM
    [J]. CLINICAL CANCER RESEARCH, 2004, 10 (23) : 8094 - 8104
  • [2] Superior activity of the combination of histone deacetylase inhibitor LAQ824 and the FLT-3 kinase inhibitor PKC412 against human acute myelogenous leukemia cells with mutant FLT-3
    Bali, P
    George, P
    Cohen, P
    Tao, JG
    Guo, F
    Sigua, C
    Vishvanath, A
    Scuto, A
    Annavarapu, S
    Fiskus, W
    Moscinski, L
    Atadja, P
    Bhalla, K
    [J]. CLINICAL CANCER RESEARCH, 2004, 10 (15) : 4991 - 4997
  • [3] Control of the SCFSkp2-Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase
    Bashir, T
    Dorrello, NV
    Amador, V
    Guardavaccaro, D
    Pagano, M
    [J]. NATURE, 2004, 428 (6979) : 190 - 193
  • [4] Battle T. E., 2002, Current Molecular Medicine (Hilversum), V2, P381, DOI 10.2174/1566524023362456
  • [5] Histone deacetylase inhibitors: new drugs for the treatment of inflammatory diseases?
    Blanchard, F
    Chipoy, C
    [J]. DRUG DISCOVERY TODAY, 2005, 10 (03) : 197 - 204
  • [6] Anticancer activities of histone deacetylase inhibitors
    Bolden, Jessica E.
    Peart, Melissa J.
    Johnstone, Ricky W.
    [J]. NATURE REVIEWS DRUG DISCOVERY, 2006, 5 (09) : 769 - 784
  • [7] STATs in oncogenesis
    Bowman, T
    Garcia, R
    Turkson, J
    Jove, R
    [J]. ONCOGENE, 2000, 19 (21) : 2474 - 2488
  • [8] Potential roles of Stat1 and Stat3 in cellular transformation
    Bromberg, JF
    Darnell, JE
    [J]. COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 1999, 64 : 425 - 428
  • [9] A pervasive role of histone acetyltransferases and deacetylases in an NF-κB-signaling code
    Calao, Miriam
    Burny, Arsene
    Quivy, Vincent
    Dekoninck, Ann
    Van Lint, Carine
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2008, 33 (07) : 339 - 349
  • [10] Enhancement of in vitro and in vivo tumor cell radiosensitivity by valproic acid
    Camphausen, K
    Cerna, D
    Scott, T
    Sproull, M
    Burgan, WE
    Cerra, MA
    Fine, H
    Tofilon, PJ
    [J]. INTERNATIONAL JOURNAL OF CANCER, 2005, 114 (03) : 380 - 386
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