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Open Access Open Badges Letter to the Editor

Histone de-acetylase inhibitors: a promising future for cancer treatment?

Raja Samir Khan1, Harris Hameed2, Ramsha Ali Bhutta3, Abdul Nafey Kazi3* and Haris Riaz4

Author Affiliations

1 Aga Khan University, Karachi, Pakistan

2 Glasgow University, Glasgow, Scotland

3 Dow Medical College, Karachi, Pakistan

4 Department of Medicine, Civil Hospital Karachi, Karachi, Pakistan

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Infectious Agents and Cancer 2013, 8:10  doi:10.1186/1750-9378-8-10

Published: 11 March 2013

First paragraph (this article has no abstract)

Histone de-acetylase proteins or lysine de-acetylases, represent a group of enzymes regulating DNA and gene expression by eliminating acetyl groups (de-acetylation) from lysine amino acids on histones and non-histone proteins [1,2]. Histone de-acetylase functions normally by being involved in a series of cellular pathways like cell growth, cell cycle, signal transduction, notch signaling pathway and especially transcription [3]. Although these functions allows histone de-acetylases to control expression of proteins involved in cancer initiation and cancer progression, abnormal acetylation of histone tails may occur with the resulting transcriptional lesions disrupting the apoptotic program of cells and leading to neoplasia [4,5]. To counter, development of antineoplastic agents called histone de-acetylase inhibitors (HDIs) have been introduced to interact with the catalytic site and blocking substrate access of histone de-acetylases in proliferation of tumor cells [6]. This anti-proliferative effect of HDIs in down regulation of BMI1 and c-MYC protein levels has shown promising results in treatment of the incurable AML as well as silencing estrogen receptor alpha in prevention of breast cancer [7,8].