Histone deacetylase inhibitors in multiple myeloma: from bench to bedside

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Abstract

Histone deacetylases (HDACs) deacetylate the lysine residues of both histones and non-histone proteins. Histone acetylation results in a loose local chromatin structure that regulates gene-specific transcription. Non-histone proteins can also be acetylated, leading to dynamic changes in their activity and stability. For these reasons, HDAC inhibition has emerged as a potential approach for the treatment of MM. Specifically, combination treatment with HDAC inhibitors and proteasome inhibitors or immunomodulatory drugs shows remarkable anti-MM activity in both preclinical and clinical settings. However, the clinical studies using non-selective HDAC inhibitors also cause unfavorable side effects in patients, leading us to develop more isoform- and/or class–selective HDAC inhibitors to enhance tolerability without diminishing anti-MM activity, thereby improving patient outcome in MM.

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Harada, T., Hideshima, T., & Anderson, K. C. (2016, September 1). Histone deacetylase inhibitors in multiple myeloma: from bench to bedside. International Journal of Hematology. Springer Tokyo. https://doi.org/10.1007/s12185-016-2008-0

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