Openly accessible

Vascular histone deacetylation by pharmacological HDAC inhibition

Rafehi, Haloom, Balcerczyk, Aneta, Lunke, Sebastian, Kaspi, Antony, Ziemann, Mark, Kn, Harikrishnan, Okabe, Jun, Khurana, Ishant, Ooi, Jenny, Khan, Abdul Waheed, Du, Xiao-Jun, Chang, Lisa, Haviv, Izhak, Keating, Samuel T., Karagiannis, Tom C. and El-Osta, Assam 2014, Vascular histone deacetylation by pharmacological HDAC inhibition, Genome research, vol. 24, no. 8, pp. 1271-1284, doi: 10.1101/gr.168781.113.

Attached Files
Name Description MIMEType Size Downloads
ziemann-vascularhistonedea-2014.pdf Published version application/pdf 913.76KB 5

Title Vascular histone deacetylation by pharmacological HDAC inhibition
Author(s) Rafehi, Haloom
Balcerczyk, Aneta
Lunke, Sebastian
Kaspi, Antony
Ziemann, MarkORCID iD for Ziemann, Mark
Kn, Harikrishnan
Okabe, Jun
Khurana, Ishant
Ooi, Jenny
Khan, Abdul Waheed
Du, Xiao-Jun
Chang, Lisa
Haviv, Izhak
Keating, Samuel T.
Karagiannis, Tom C.
El-Osta, Assam
Journal name Genome research
Volume number 24
Issue number 8
Start page 1271
End page 1284
Total pages 14
Publisher Cold Spring Harbor Laboratory Press
Place of publication Cold Spring Harbor, N.Y.
Publication date 2014-08
ISSN 1549-5469
Keyword(s) Acetylation
Anti-Inflammatory Agents
Cells, Cultured
Endothelial Cells
Endothelium, Vascular
Gene Expression Regulation
Genome, Human
Histone Deacetylase Inhibitors
Hydroxamic Acids
Mice, Inbred C57BL
Promoter Regions, Genetic
Protein Binding
Protein Processing, Post-Translational
Transcription Factors
Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Biotechnology & Applied Microbiology
Genetics & Heredity
Summary HDAC inhibitors can regulate gene expression by post-translational modification of histone as well as nonhistone proteins. Often studied at single loci, increased histone acetylation is the paradigmatic mechanism of action. However, little is known of the extent of genome-wide changes in cells stimulated by the hydroxamic acids, TSA and SAHA. In this article, we map vascular chromatin modifications including histone H3 acetylation of lysine 9 and 14 (H3K9/14ac) using chromatin immunoprecipitation (ChIP) coupled with massive parallel sequencing (ChIP-seq). Since acetylation-mediated gene expression is often associated with modification of other lysine residues, we also examined H3K4me3 and H3K9me3 as well as changes in CpG methylation (CpG-seq). RNA sequencing indicates the differential expression of ∼30% of genes, with almost equal numbers being up- and down-regulated. We observed broad deacetylation and gene expression changes conferred by TSA and SAHA mediated by the loss of EP300/CREBBP binding at multiple gene promoters. This study provides an important framework for HDAC inhibitor function in vascular biology and a comprehensive description of genome-wide deacetylation by pharmacological HDAC inhibition.
Language eng
DOI 10.1101/gr.168781.113
Field of Research 06 Biological Sciences
11 Medical And Health Sciences
Copyright notice ©2014, Rafehi et al.
Free to Read? Yes
Use Rights Creative Commons Attribution non-commercial licence
Persistent URL

Connect to link resolver
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact

Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 0 times in TR Web of Science
Scopus Citation Count Cited 40 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 5 Abstract Views, 5 File Downloads  -  Detailed Statistics
Created: Fri, 24 Aug 2018, 14:47:05 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact