Journal article
Inhibition of histone deacetylases
Methods in molecular biology (Clifton, N.J.), Vol.791, pp.297-311
01/01/2011
DOI: 10.1007/978-1-61779-316-5_22
PMID: 21913088
Abstract
Lysine acetylation of histones is one of the major epigenetic regulators of chromatin conformation and gene expression. The dynamic nature of histone acetylation is determined by the counterbalancing activity of histone acetyltransferase and histone deacetylase (HDAC) enzymes. Acetylation of histones is generally associated with open and transcriptionally active chromatin, whereas the activity of HDACs leads to histone deacetylation, condensation of chromatin, and inhibition of transcription. Aberrant silencing of tumor suppressors and other genes has been found in different types of cancer. Abnormal activity of HDACs has been implicated in tumorigenesis and therefore considerable effort has been put into the development of HDAC inhibitors as a means of modifying histone acetylation status and reexpressing aberrantly silenced tumor suppressor genes. This has led to the generation of a number of structurally diverse compounds that can effectively inhibit HDAC activity, thus altering chromatin structure in cancer cells. This unit discusses the methods and recent technological developments with respect to the studies of HDAC inhibition in cancer.
Details
- Title: Subtitle
- Inhibition of histone deacetylases
- Creators
- Yi Huang - UPMC Hillman Cancer CenterPatrick G ShawNancy E Davidson - UPMC Hillman Cancer Center
- Resource Type
- Journal article
- Publication Details
- Methods in molecular biology (Clifton, N.J.), Vol.791, pp.297-311
- DOI
- 10.1007/978-1-61779-316-5_22
- PMID
- 21913088
- eISBN
- 1617793167; 9781617793165
- ISSN
- 1064-3745
- eISSN
- 1940-6029
- Grant note
- CA88843 / NCI NIH HHS
- Language
- English
- Date published
- 01/01/2011
- Academic Unit
- Internal Medicine
- Record Identifier
- 9984383925602771
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