Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이서구 | * |
dc.contributor.author | 창동신 | * |
dc.date.accessioned | 2016-08-28T12:08:44Z | - |
dc.date.available | 2016-08-28T12:08:44Z | - |
dc.date.issued | 2012 | * |
dc.identifier.issn | 0021-9258 | * |
dc.identifier.other | OAK-8321 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/222237 | - |
dc.description.abstract | Sulfiredoxin (Srx) is an enzyme that catalyzes the reduction of cysteine sulfinic acid of hyperoxidized peroxiredoxins (Prxs). Having high affinity toward H 2O 2, 2-Cys Prxs can efficiently reduce H 2O 2 at low concentration. We previously showed that Prx I is hyperoxidized at a rate of 0.072% per turnover even in the presence of low steady-state levels ofH 2O 2. Here we examine the novel role of Srx in cells exposed to low steady-state levels of H 2O 2, which can be achieved by using glucose oxidase. Exposure of low steady-state levels of H 2O 2 (10-20 μM) to A549 or wild-type mouse embryonic fibroblast (MEF) cells does not lead to any significant change in oxidative injury because of the maintenance of balance between H 2O 2 production and elimination. In contrast, loss-of-function studies using Srx-depleted A549 and Srx -/- MEF cells demonstrate a dramatic increase in extra- and intracellular H 2O 2, sulfinic 2-Cys Prxs, and apoptosis. Concomitant with hyperoxidation of mitochondrial Prx III, Srx-depleted cells show an activation of mitochondria-mediated apoptotic pathways including mitochondria membrane potential collapse, cytochrome c release, and caspaseactivation.Furthermore, adenoviralre-expressionofSrxin Srx-depleted A549 or Srx -/- MEF cells promotes the reactivation of sulfinic 2-Cys Prxs and results in cellular resistance to apoptosis, with enhanced removal of H 2O 2. These results indicate that Srx functions as a novel component to maintain the balance between H 2O 2 production and elimination and then protects cells from apoptosis even in the presence of low steady-state levels of H 2O 2. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc. | * |
dc.language | English | * |
dc.title | Sulfiredoxin protein is critical for redox balance and survival of cells exposed to low steady-state levels of H 2O 2 | * |
dc.type | Article | * |
dc.relation.issue | 1 | * |
dc.relation.volume | 287 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 81 | * |
dc.relation.lastpage | 89 | * |
dc.relation.journaltitle | Journal of Biological Chemistry | * |
dc.identifier.doi | 10.1074/jbc.M111.316711 | * |
dc.identifier.wosid | WOS:000298682400011 | * |
dc.identifier.scopusid | 2-s2.0-84855263802 | * |
dc.author.google | Baek J.Y. | * |
dc.author.google | Han S.H. | * |
dc.author.google | Sung S.H. | * |
dc.author.google | Lee H.E. | * |
dc.author.google | Kim Y.-M. | * |
dc.author.google | Noh Y.H. | * |
dc.author.google | Bae S.H. | * |
dc.author.google | Rhee S.G. | * |
dc.author.google | Chang T.-S. | * |
dc.contributor.scopusid | 이서구(7401852092) | * |
dc.contributor.scopusid | 창동신(7404726037) | * |
dc.date.modifydate | 20240423081003 | * |