Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 435, Issue 3, Pages 403-407Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2013.04.101
Keywords
APE1/Ref-1; Trichostatin A; Secretion; Acetylation
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Funding
- National Research Foundation of Korea (NRF)
- Korea government (MEST) [2011-0006231, 2011-0016797, 2012R1A1A3015385]
- National Research Foundation of Korea [2011-0016797, 2012R1A1A3015385] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 APEI/Ref-1 secretion without changing cell viability. In a fluorescence quantitative assay, the secreted APEI/Ref-1 was estimated to be about 10 ng/mL in response to TSA (1 mu M). 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. (C) 2013 Elsevier Inc. All rights reserved.
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