Histone deacetylases inhibitor trichostatin A modulates the extracellular release of APE1/Ref-1
Journal Article
·
· Biochemical and Biophysical Research Communications
- Department of Physiology, School of Medicine, Chungnam National University, Daejeon 301-747 (Korea, Republic of)
- Cardiovascular Institute, University of Pittsburgh, Pittsburgh, PA 15213 (United States)
Highlights: •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. -- Abstract: 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 10 ng/mL in response to TSA (1 μM). 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.
- OSTI ID:
- 22239615
- Journal Information:
- Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 3 Vol. 435; ISSN 0006-291X; ISSN BBRCA9
- Country of Publication:
- United States
- Language:
- English
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