Targeting histone deacetylases for the treatment of disease : Epigenetics Review Series

Lawless, M. W., Norris, S., O'Byrne, Kenneth J., & Gray, S. G. (2009) Targeting histone deacetylases for the treatment of disease : Epigenetics Review Series. Journal of Cellular and Molecular Medicine, 13(5), pp. 826-852.

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The 'histone code' is a well-established hypothesis describing the idea that specific patterns of post-translational modifications to histones act like a molecular 'code' recognized and used by non-histone proteins to regulate specific chromatin functions. One modification, which has received significant attention, is that of histone acetylation. The enzymes that regulate this modification are described as lysine acetyltransferases or KATs, and histone deacetylases or HDACs. Due to their conserved catalytic domain HDACs have been actively targeted as a therapeutic target. The pro-inflammatory environment is increasingly being recognized as a critical element for both degenerative diseases and cancer. The present review will discuss the current knowledge surrounding the clinical potential and current development of histone deacetylases for the treatment of diseases for which a pro-inflammatory environment plays important roles, and the molecular mechanisms by which such inhibitors may play important functions in modulating the pro-inflammatory environment. © 2009 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd.

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29 citations in Web of Science®

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ID Code: 65178
Item Type: Journal Article
Refereed: Yes
Additional URLs:
Keywords: Cancer, Chromatin, Disease, Histone deacetylase, Targeting, antidiabetic agent, antineoplastic agent, histone acetyltransferase, nonsteroid antiinflammatory agent, acetylation, animal, article, diabetes mellitus, drug antagonism, endoplasmic reticulum, enzymology, human, metabolism, neoplasm, protein processing, Animals, Anti-Inflammatory Agents, Non-Steroidal, Antineoplastic Agents, Histone Acetyltransferases, Histone Deacetylases, Humans, Hypoglycemic Agents, Neoplasms, Protein Processing, Post-Translational, Catha edulis
DOI: 10.1111/j.1582-4934.2008.00571.x
ISSN: 1582-1838
Divisions: Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
Copyright Owner: Copyright 2009 Wiley-Blackwell Publishing Ltd.
Deposited On: 06 Dec 2013 02:27
Last Modified: 12 Mar 2014 05:14

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