<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>6</volume><submitter>Park MS</submitter><pubmed_abstract>Apurinic apyrimidinic endonuclease 1/Redox factor-1 (APE1/Ref-1) is a multifunctional protein with redox activity and is proved to be secreted from stimulated cells. The aim of this study was to evaluate the functions of extracellular APE1/Ref-1 with respect to leading anti-inflammatory signaling in TNF-α-stimulated endothelial cells in response to acetylation. Treatment of TNF-α-stimulated endothelial cells with an inhibitor of deacetylase that causes intracellular acetylation, considerably suppressed vascular cell adhesion molecule-1 (VCAM-1). During TSA-mediated acetylation in culture, a time-dependent increase in secreted APE1/Ref-1 was confirmed. The acetyl moiety of acetylated-APE1/Ref-1 was rapidly removed based on the removal kinetics. Additionally, recombinant human (rh) APE1/Ref-</pubmed_abstract><journal>Scientific reports</journal><pagination>23015</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4786854</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Secreted APE1/Ref-1 inhibits TNF-α-stimulated endothelial inflammation via thiol-disulfide exchange in TNF receptor.</pubmed_title><pmcid>PMC4786854</pmcid><pubmed_authors>Choi S</pubmed_authors><pubmed_authors>Lee YR</pubmed_authors><pubmed_authors>Kang G</pubmed_authors><pubmed_authors>Kim CS</pubmed_authors><pubmed_authors>Jeon BH</pubmed_authors><pubmed_authors>Lee SD</pubmed_authors><pubmed_authors>Park MS</pubmed_authors><pubmed_authors>Joo HK</pubmed_authors><pubmed_authors>Kim SJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Secreted APE1/Ref-1 inhibits TNF-α-stimulated endothelial inflammation via thiol-disulfide exchange in TNF receptor.</name><description>Apurinic apyrimidinic endonuclease 1/Redox factor-1 (APE1/Ref-1) is a multifunctional protein with redox activity and is proved to be secreted from stimulated cells. The aim of this study was to evaluate the functions of extracellular APE1/Ref-1 with respect to leading anti-inflammatory signaling in TNF-α-stimulated endothelial cells in response to acetylation. Treatment of TNF-α-stimulated endothelial cells with an inhibitor of deacetylase that causes intracellular acetylation, considerably suppressed vascular cell adhesion molecule-1 (VCAM-1). During TSA-mediated acetylation in culture, a time-dependent increase in secreted APE1/Ref-1 was confirmed. The acetyl moiety of acetylated-APE1/Ref-1 was rapidly removed based on the removal kinetics. Additionally, recombinant human (rh) APE1/Ref-</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Mar</publication><modification>2025-04-18T22:04:15.196Z</modification><creation>2019-03-27T02:10:52Z</creation></dates><accession>S-EPMC4786854</accession><cross_references><pubmed>26964514</pubmed><doi>10.1038/srep23015</doi></cross_references></HashMap>