Histone deacetylase inhibitors: a review of their clinical status as antineoplastic agents

Cancer Invest. 2005;23(7):635-42. doi: 10.1080/07357900500283119.

Abstract

The histone code refers to specific modifications in the biochemical composition of nucleosome-associated histone proteins involved in the regulation of gene transcription. These modifications include, among several, acetylation, methylation, and phosphorylation of several histone amino acid residues and are associated with different states of chromatin configuration and gene expression. In particular, acetylation of specific residues in histones H3 and H4 has been associated with an open chromatin configuration and a permissive gene transcription state. This particular modification is regulated by several enzymatic activities with the capacity to either transfer acetyl groups or to induce histone deacetylation. This last activity is associated with gene silencing. Several agents have been shown to have histone deacetylase inhibitory activity (HDACI). In vitro, experiments in multiple neoplastic cancer cell lines have demonstrated that treatment with HDACIs results in increased global and gene specific histone acetylation, and reactivation of aberrantly silenced genes. This phenomenon has been associated with cell differentiation and induction of apoptosis. Based on these observations, several of these agents are now in clinical development both for solid tumor and hematological malignancies. In this article, we provide a brief introduction to the field of histone deacetylation inhibition in cancer and review the most relevant clinical data so far published.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Antineoplastic Agents / pharmacology*
  • Antineoplastic Agents / therapeutic use
  • Apoptosis
  • Cell Differentiation
  • Enzyme Inhibitors / pharmacology*
  • Enzyme Inhibitors / therapeutic use
  • Gene Expression Regulation
  • Gene Silencing
  • Histone Deacetylase Inhibitors*
  • Histones / metabolism
  • Humans

Substances

  • Antineoplastic Agents
  • Enzyme Inhibitors
  • Histone Deacetylase Inhibitors
  • Histones