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.
Copyright © 2013 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation / drug effects
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Active Transport, Cell Nucleus / drug effects
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DNA-(Apurinic or Apyrimidinic Site) Lyase / chemistry
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DNA-(Apurinic or Apyrimidinic Site) Lyase / genetics
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DNA-(Apurinic or Apyrimidinic Site) Lyase / metabolism*
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Extracellular Space / enzymology
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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HEK293 Cells
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Histone Deacetylase Inhibitors / pharmacology*
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Humans
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Hydroxamic Acids / pharmacology*
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Lysine / chemistry
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Mutagenesis, Site-Directed
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Protein Processing, Post-Translational / drug effects
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
Substances
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Histone Deacetylase Inhibitors
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Hydroxamic Acids
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Recombinant Fusion Proteins
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enhanced green fluorescent protein
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Green Fluorescent Proteins
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trichostatin A
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APEX1 protein, human
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DNA-(Apurinic or Apyrimidinic Site) Lyase
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Lysine