Histone deacetylases inhibitor trichostatin A modulates the extracellular release of APE1/Ref-1

Sunga Choi; Yu Ran Lee; Myoung Soo Park; Hee Kyoung Joo; Eun Jung Cho; Hyo Shin Kim; Cuk Seong Kim; Jin Bong Park; Kaikobad Irani; Byeong Hwa Jeon

doi:10.1016/j.bbrc.2013.04.101

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Histone deacetylases inhibitor trichostatin A modulates the extracellular release of APE1/Ref-1

Journal article

Peer reviewed

Histone deacetylases inhibitor trichostatin A modulates the extracellular release of APE1/Ref-1

Sunga Choi, Yu Ran Lee, Myoung Soo Park, Hee Kyoung Joo, Eun Jung Cho, Hyo Shin Kim, Cuk Seong Kim, Jin Bong Park, Kaikobad Irani and Byeong Hwa Jeon

Biochemical and biophysical research communications, Vol.435(3), pp.403-407

06/07/2013

DOI: 10.1016/j.bbrc.2013.04.101

PMID: 23665318

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Abstract

•Trichostatin A (TSA) increased APE1/Ref-1 secretion in HEK293 cells.•Lysine-mutated APE1/Ref-1 (K6R/K7R) was not secreted by TSA.•TSA induced cytoplasmic translocation of APE1/Ref-1.•APE1/Ref-1 is a protein whose secretion is governed by lysine acetylation. Apurinic/apyrimidinic endonuclease 1/Redox factor-1 (APE1/Ref-1) can be acetylated via post-translational modification. We investigated the effect of an inhibitor of histone deacetylases on the extracellular release of APE1/Ref-1 in HEK293 cells. Trichostatin A (TSA), an inhibitor of histone deacetylases, induced APE1/Ref-1 secretion without changing cell viability. In a fluorescence quantitative assay, the secreted APE1/Ref-1 was estimated to be about 10ng/mL in response to TSA (1μM). However, TSA did not induce the secretion of lysine-mutated APE1/Ref-1 (K6R/K7R). TSA also caused nuclear to cytoplasmic translocation of APE1/Ref-1. Taken together, these findings suggest that APE1/Ref-1 is a protein whose secretion is governed by lysine acetylation.

APE1/Ref-1

Trichostatin A

Acetylation

Secretion

Details

Title: Subtitle: Histone deacetylases inhibitor trichostatin A modulates the extracellular release of APE1/Ref-1
Creators: Sunga Choi - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Yu Ran Lee - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Myoung Soo Park - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Hee Kyoung Joo - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Eun Jung Cho - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Hyo Shin Kim - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Cuk Seong Kim - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Jin Bong Park - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Kaikobad Irani - Cardiovascular Institute, University of Pittsburgh, Pittsburgh, PA 15213, USA
Byeong Hwa Jeon - Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747, Republic of Korea
Resource Type: Journal article
Publication Details: Biochemical and biophysical research communications, Vol.435(3), pp.403-407
Publisher: Elsevier Inc
DOI: 10.1016/j.bbrc.2013.04.101
PMID: 23665318
ISSN: 0006-291X
eISSN: 1090-2104
Grant note: name: National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST), award: (2011-0006231, 2011-0016797 and 2012R1A1A3015385)
Language: English
Date published: 06/07/2013
Academic Unit: Cardiovascular Medicine; Radiation Oncology; Fraternal Order of Eagles Diabetes Research Center; Internal Medicine
Record Identifier: 9984047625602771

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