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dc.contributor.author우현애*
dc.date.accessioned2019-11-05T16:30:10Z-
dc.date.available2019-11-05T16:30:10Z-
dc.date.issued2019*
dc.identifier.issn1942-0900*
dc.identifier.issn1942-0994*
dc.identifier.otherOAK-25591*
dc.identifier.urihttps://dspace.ewha.ac.kr/handle/2015.oak/251755-
dc.description.abstractPhosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a lipid and protein phosphatase that coordinates various cellular processes. Its activity is regulated by the reversible oxidation of an active-site cysteine residue by H2O2 and thioredoxin. However, the potential role of lipid peroxides in the redox regulation of PTEN remains obscure. To evaluate this, 15-hydroperoxy-eicosatetraenoic acid (15s-HpETE), a lipid peroxide, was employed to investigate its effect on PTEN using molecular and cellular-based assays. Exposure to 15s-HpETE resulted in the oxidation of recombinant PTEN. Reversible oxidation of PTEN was also observed in mouse embryonic fibroblast (MEF) cells treated with a 15s-HpETE and Lipofectamine mixture. The oxidative dimerization of thioredoxin was found simultaneously. In addition, the absence of peroxiredoxin III aggravated 15s-HpETE-induced PTEN oxidation in MEF cells. Our study provides novel insight into the mechanism linking lipid peroxidation to the etiology of tumorigenesis.*
dc.languageEnglish*
dc.publisherHINDAWI LTD*
dc.titlePeroxiredoxin III Protects Tumor Suppressor PTEN from Oxidation by 15-Hydroperoxy-eicosatetraenoic Acid*
dc.typeArticle*
dc.relation.volume2019*
dc.relation.indexSCIE*
dc.relation.indexSCOPUS*
dc.relation.journaltitleOXIDATIVE MEDICINE AND CELLULAR LONGEVITY*
dc.identifier.doi10.1155/2019/2828493*
dc.identifier.wosidWOS:000488457000001*
dc.author.googleZhang, Ying*
dc.author.googlePark, Jiyoung*
dc.author.googleHan, Seong-Jeong*
dc.author.googleLim, Yongwoon*
dc.author.googlePark, Iha*
dc.author.googleKim, Jong-Suk*
dc.author.googleWoo, Hyun Ae*
dc.author.googleLee, Seung-Rock*
dc.contributor.scopusid우현애(8068619500)*
dc.date.modifydate20240215164922*


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