The Structure and Function of Histone Deacetylases: The Target for Anti-cancer Therapy

被引：51

作者：

Zhang, Yingjie ^{[1
]}

Fang, Hao ^{[1
]}

Jiao, Jie ^{[1
]}

Xu, Wenfang ^{[1
]}

机构：

[1] Shandong Univ, Sch Pharmaceut Sci, Dept Med Chem, Jinan 250012, Shandong, Peoples R China

来源：

CURRENT MEDICINAL CHEMISTRY | 2008年 / 15卷 / 27期

关键词：

Histone deacetylases; Structure; Function; HDAC inhibitors; Anti-cancer agents;

D O I：

10.2174/092986708786242796

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Histone deacetylases (HDACs) and Histone acetyltransferases (HATs) are two kinds of enzymes, which can, by reversible deacetylation and acetylation, modify the structure and function of chromatin histones that are involved in the regulation of gene expression, as well as many non-histone proteins that regulate cell function in eukaryotes. Compared with HATs, HDACs have attracted more and more attentions for two main reasons over the past few years. First, the relationship of HDACs and cancer, as well as several other diseases has been confirmed. Second, many HDAC inhibitors (HDACi) have entered pre-clinical or clinical research as anti-cancer agents and shown satisfying effects. HDACs, including 18 members at least, are subdivided into 4 classes that generally have high structure similarity and related substrate specificity within classes, but have divergent sequence and different functions even between within classes. This review will introduce the relationship between HDACs and cancer along with the enzymes' structure and main function.

引用

页码：2840 / 2849

页数：10

共 129 条

[1] p21WAF1 is required for butyrate-mediated growth inhibition of human colon cancer cells [J].

Archer, SY ;

Meng, SF ;

Shei, A ;

Hodin, RA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (12) :6791-6796

[2] Apoptosis on hepatoma cells but not on primary hepatocytes by histone deacetylase inhibitors valproate and ITF2357 [J].

Armeanu, S ;

Pathil, A ;

Venturelli, S ;

Mascagni, P ;

Weiss, TS ;

Göttlicher, M ;

Gregor, M ;

Lauer, UM ;

Bitzer, M .

JOURNAL OF HEPATOLOGY, 2005, 42 (02) :210-217

[3] R306465 is a novel potent inhibitor of class I histone deacetylases with broad-spectrum antitumoral activity against solid and haematological malignancies [J].

Arts, J. ;

Angibaud, P. ;

Marieen, A. ;

Floren, W. ;

Janssens, B. ;

King, P. ;

van Dun, J. ;

Janssen, L. ;

Geerts, T. ;

Tuman, R. W. ;

Johnson, D. L. ;

Andries, L. ;

Jung, M. ;

Janicot, M. ;

van Emelen, K. .

BRITISH JOURNAL OF CANCER, 2007, 97 (10) :1344-1353

[4] Annexin I is an endogenous ligand that mediates apoptotic cell engulfment [J].

Arur, S ;

Uche, UE ;

Rezaul, K ;

Fong, M ;

Scranton, V ;

Cowan, AE ;

Mohler, W ;

Han, DK .

DEVELOPMENTAL CELL, 2003, 4 (04) :587-598

[5] Acetylation of importin-α nuclear import factors by CBP/p300 [J].

Bannister, AJ ;

Miska, EA ;

Görlich, D ;

Kouzarides, T .

CURRENT BIOLOGY, 2000, 10 (08) :467-470

[6] Class II histone deacetylases: Structure, function, and regulation [J].

Bertos, NR ;

Wang, AH ;

Yang, XJ .

BIOCHEMISTRY AND CELL BIOLOGY, 2001, 79 (03) :243-252

[7] Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1α and is not induced by hypoxia or HIF [J].

Bilton, R ;

Mazure, N ;

Trottier, E ;

Hattab, M ;

Déry, MA ;

Richard, DE ;

Pouysségur, J ;

Brahimi-Horn, MC .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (35) :31132-31140

[8] Post-translational modification of p53 in tumorigenesis [J].

Bode, AM ;

Dong, ZG .

NATURE REVIEWS CANCER, 2004, 4 (10) :793-805

[9] Anticancer activities of histone deacetylase inhibitors [J].

Bolden, Jessica E. ;

Peart, Melissa J. ;

Johnstone, Ricky W. .

NATURE REVIEWS DRUG DISCOVERY, 2006, 5 (09) :769-784

[10] Regulation of activity of the transcription factor GATA-1 by acetylation [J].

Boyes, J ;

Byfield, P ;

Nakatani, Y ;

Ogryzko, V .

NATURE, 1998, 396 (6711) :594-598

← 1 2 3 4 5 6 7 8 9 10 →