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dc.contributor.authorFeng, S.
dc.contributor.authorDaw, J.N.
dc.contributor.authorChen, Q.M.
dc.date.accessioned2021-06-17T01:09:29Z
dc.date.available2021-06-17T01:09:29Z
dc.date.issued2020
dc.identifier.citationFeng, S., Daw, J. N., & Chen, Q. M. (2020). Histone deacetylase inhibitors prevent H2O2 from inducing stress granule formation. Current Research in Toxicology, 1, 141-148.
dc.identifier.issn2666-027X
dc.identifier.doi10.1016/j.crtox.2020.10.004
dc.identifier.urihttp://hdl.handle.net/10150/659933
dc.description.abstractReactive Oxygen Species (ROS) are generated as by-products of aerobic metabolism. The production of ROS increases during xenobiotic stress and under multiple pathological conditions. Although ROS are considered harmful historically, mounting evidence recently indicates a signaling function of ROS, preceding to and regulating transcriptional or post-transcriptional events, contributing to cell death or cell survival and adaptation. Among the cellular defense mechanisms activated by ROS is formation of stress granules (SGs). The stalled translational apparatus, together with mRNA, aggregates into microscopically detectable and molecularly dynamic granules. We found that with H2O2, the dose most potent for inducing SGs in HeLa cells is 400–600 μM. With 200 μM H2O2, 2 h treatment induced the highest percentage of cells containing SGs. Whether ROS signaling pathways regulate the formation of SGs was tested using pharmacological inhibitors. We probed the potential role of PI3K, MAPKs, PKC or histone deacetylation in SG formation. Using deferoxamine as a positive control, we found a lack of inhibitory effect of wortmannin, LY-294002, JNK-I, SB-202190, PD-98059, or H89 when the percentage of cells containing SGs was counted. About 35% inhibition was observed with HDAC6 inhibitor Tubastatin A, whereas general HDAC inhibitor Trichostatin A provided a complete inhibition of SG formation. Our data point to the need of investigating the role of HDACs in SG formation during oxidative stress. © 2020 The Authors
dc.language.isoen
dc.publisherElsevier B.V.
dc.rightsCopyright © 2020 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectCytoprotection
dc.subjectOxidative stress
dc.subjectProtein translation
dc.subjectRibosomes
dc.subjectSignaling transduction
dc.titleHistone deacetylase inhibitors prevent H2O2 from inducing stress granule formation
dc.typeArticle
dc.typetext
dc.contributor.departmentDepartment of Pharmacology, College of Medicine, University of Arizona
dc.identifier.journalCurrent Research in Toxicology
dc.description.noteOpen access journal
dc.description.collectioninformationThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
dc.eprint.versionFinal published version
dc.source.journaltitleCurrent Research in Toxicology
refterms.dateFOA2021-06-17T01:09:29Z


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Copyright © 2020 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Except where otherwise noted, this item's license is described as Copyright © 2020 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).