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Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York
Requests for reprints: Paul A. Marks, Cell Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021. Phone: 212-639-6568; Fax: 212-639-2861. E-mail: Marksp{at}mskcc.org
Abstract
Histone deacetylase inhibitors (HDACi) comprise structurally diverse compounds that are a group of targeted anticancer agents. The first of these new HDACi, vorinostat (suberoylanilide hydroxamic acid), has received Food and Drug Administration approval for treating patients with cutaneous T-cell lymphoma. This review focuses on the activities of the 11 zinc-containing HDACs, their histone and nonhistone protein substrates, and the different pathways by which HDACi induce transformed cell death. A hypothesis is presented to explain the relative resistance of normal cells to HDACi-induced cell death. (Mol Cancer Res 2007;5(10):981–9)
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