Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김희선 | * |
dc.date.accessioned | 2016-08-28T12:08:27Z | - |
dc.date.available | 2016-08-28T12:08:27Z | - |
dc.date.issued | 2009 | * |
dc.identifier.issn | 0009-2797 | * |
dc.identifier.other | OAK-6003 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/220307 | - |
dc.description.abstract | In response to oxidative DNA base damage, oxoguanine glycosylase 1 (OGG1), in a base-excision repair (BER) pathway in mammals, plays a vital role in the repair of 8-hydroxy-2′-deoxyguanosine (8-OHdG), which is a reliable marker of reactive oxygen species (ROS)-induced DNA base modification and contributes to the pathologic process of cancer. Recently, we have shown that butin (7,3′,4′-trihydroxydihydroflavone) protects cells against hydrogen peroxide (H 2O 2)-induced damage of cellular components including DNA. In the present study, we examined the possible protective effect of butin on oxidative stress-induced DNA base modification, especially 8-OHdG. Hydrogen peroxide significantly increased the level of 8-OHdG, which was detected by 8-OHdG ELISA and confocal microscopy, but butin decreased this level. Suppression of 8-OHdG formation by butin was related to the enhanced mRNA and protein expression of OGG1, which was detected by RT-PCR and Western blot analysis. Butin also increased the transcriptional activity of OGG1, which was suppressed by H 2O 2 treatment; this transcriptional activity was detected by OGG1 promoter luciferase assay. Butin enhanced the expression of phosphorylated Akt (active form of Akt), a regulator of OGG1, which was decreased by H 2O 2 treatment. A PI3K-specific inhibitor, LY294002, abolished the phosphorylated Akt and OGG1 expressions induced by butin, suggesting that OGG1 induction by butin involves the PI3K/Akt pathway. © 2009 Elsevier Ireland Ltd. All rights reserved. | * |
dc.language | English | * |
dc.title | Butin decreases oxidative stress-induced 8-hydroxy-2′-deoxyguanosine levels via activation of oxoguanine glycosylase 1 | * |
dc.type | Article | * |
dc.relation.issue | 3 | * |
dc.relation.volume | 181 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 338 | * |
dc.relation.lastpage | 342 | * |
dc.relation.journaltitle | Chemico-Biological Interactions | * |
dc.identifier.doi | 10.1016/j.cbi.2009.07.011 | * |
dc.identifier.wosid | WOS:000271043800008 | * |
dc.identifier.scopusid | 2-s2.0-70349178640 | * |
dc.author.google | Kang K.A. | * |
dc.author.google | Lee J.H. | * |
dc.author.google | Chae S. | * |
dc.author.google | Zhang R. | * |
dc.author.google | Piao M.J. | * |
dc.author.google | Kim H.S. | * |
dc.author.google | You H.J. | * |
dc.author.google | Hyun J.W. | * |
dc.contributor.scopusid | 김희선(57191372551) | * |
dc.date.modifydate | 20240118140922 | * |