Recent studies have shown that HDAC8, an enzyme responsible for the deacetylation of lysine residues on the N-terminal part of core histones and non-histone proteins, was overexpressed in multiple myeloma cells and was associated with worse survival outcomes. In this video, Nikhil Munshi, MD, Dana-Farber Cancer Institute, Boston, MA, discusses the results of a pre-clinical study investigating the effect of HDAC8 inhibition in multiple myeloma. It was found that HDAC8 inhibition impacted myeloma cell viability and genomic stability, where it led to a decrease in spontaneous DNA breaks and an increase in homologous recombination through inhibition of HDCA8-mediated RAD51 deacetylation. These effects where confirmed in an animal model. In addition, experiments showed that this agent had a synergistic effect in combination with existing multiple myeloma drugs. These findings suggest HDAC8 as a promising therapeutic target in multiple myeloma. This interview took place at the 63rd ASH Annual Meeting and Exposition congress in Atlanta, GA.
