Ishika Gupta, Ashley Nwafor, Robert A Casero, Tracy Murray Stewart
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引用次数: 0
Abstract
Among histone deacetylases, HDAC10 is unique in its substrate preference for a specific acetylated polyamine, N8-acetylspermidine (N8-AcSpd), over other acetylated polyamines and peptides. As a polyamine deacetylase, HDAC10 catalyzes the conversion of N8-AcSpd into spermidine, thereby enabling the cell to utilize this acetylated derivative to support polyamine homeostasis. Therefore, the level of HDAC10-mediated PDAC activity in a particular tissue and its exposure to extracellular N8-AcSpd, a byproduct of certain intestinal microbes, may directly contribute to the maintenance of intracellular polyamine concentrations. This chapter provides detailed methods for determining relative levels of HDAC10-mediated polyamine deacetylase activity using cell-based assays. These cost-efficient methods are useful for identifying tissue-specific differences in PDAC activity and may also be adapted to enable high-throughput screening of effectors of HDAC10 function, such as HDAC inhibitors.
期刊介绍：
The critically acclaimed laboratory standard for almost 50 years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Each volume is eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 500 volumes the series contains much material still relevant today and is truly an essential publication for researchers in all fields of life sciences, including microbiology, biochemistry, cancer research and genetics-just to name a few. Five of the 2013 Nobel Laureates have edited or contributed to volumes of MIE.
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