Absence of cytosolic 2-Cys Prx subtypes I and II exacerbates TNF-α-induced apoptosis via different routes

Cited 12 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorS Lee-
dc.contributor.authorJ Y Lee-
dc.contributor.authorEun Woo Lee-
dc.contributor.authorS Park-
dc.contributor.authorD H Kang-
dc.contributor.authorC Min-
dc.contributor.authorD J Lee-
dc.contributor.authorD Kang-
dc.contributor.authorJ Song-
dc.contributor.authorJ Kwon-
dc.contributor.authorS W Kang-
dc.date.accessioned2019-04-09T16:30:18Z-
dc.date.available2019-04-09T16:30:18Z-
dc.date.issued2019-
dc.identifier.issn2211-1247-
dc.identifier.uri10.1016/j.celrep.2019.01.081ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/18447-
dc.description.abstractThere are abundant peroxiredoxin (Prx) enzymes, but an increase of cellular H2O2 level always happens in apoptotic cells. Here, we show that cellular H2O2 switches different apoptosis pathways depending on which type of Prx enzyme is absent. TNF-α-induced H2O2 burst preferentially activates the DNA damage-dependent apoptosis pathway in the absence of PrxI. By contrast, the same H2O2 burst stimulates the RIPK1-dependent apoptosis pathway in the absence of PrxII by inducing the destruction of cIAP1 in caveolar membrane. Specifically, H2O2 induces the oxidation of Cys308 residue in the cIAP1-BIR3 domain, which induces the dimerization-dependent E3 ligase activation. Thus, the reduction in cIAP level by the absence of PrxII triggers cell-autonomous apoptosis in cancer cells and tumors. Such differential functions of PrxI and PrxII are mediated by interaction with H2AX and cIAP1, respectively. Collectively, this study reveals the distinct switch roles of 2-Cys Prx isoforms in apoptosis signaling.-
dc.publisherElsevier-Cell Press-
dc.titleAbsence of cytosolic 2-Cys Prx subtypes I and II exacerbates TNF-α-induced apoptosis via different routes-
dc.title.alternativeAbsence of cytosolic 2-Cys Prx subtypes I and II exacerbates TNF-α-induced apoptosis via different routes-
dc.typeArticle-
dc.citation.titleCell Reports-
dc.citation.number8-
dc.citation.endPage2211-
dc.citation.startPage2194-
dc.citation.volume26-
dc.contributor.affiliatedAuthorEun Woo Lee-
dc.contributor.alternativeName이순미-
dc.contributor.alternativeName이주영-
dc.contributor.alternativeName이은우-
dc.contributor.alternativeName박수진-
dc.contributor.alternativeName강동훈-
dc.contributor.alternativeName민청춘-
dc.contributor.alternativeName이두재-
dc.contributor.alternativeName강동민-
dc.contributor.alternativeName송재환-
dc.contributor.alternativeName권종범-
dc.contributor.alternativeName강상원-
dc.identifier.bibliographicCitationCell Reports, vol. 26, no. 8, pp. 2194-2211-
dc.identifier.doi10.1016/j.celrep.2019.01.081-
dc.subject.keywordDNA damage-
dc.subject.keywordH(2)O(2)-
dc.subject.keywordRIPK1-
dc.subject.keywordTNF-α-
dc.subject.keywordapoptosis-
dc.subject.keywordcIAP-
dc.subject.keywordperoxiredoxin-
dc.subject.localDNA damage-
dc.subject.localH 2O 2-
dc.subject.localH(2)O(2)-
dc.subject.localH2O2-
dc.subject.localRIPK1-
dc.subject.localTumor necrosis fa tor-α-
dc.subject.localTNFα-
dc.subject.localTumor necrosis factor (TNF)-α-
dc.subject.localTnf-α-
dc.subject.localTNF-a-
dc.subject.localTNF-alpha-
dc.subject.localTumor necrosis factor-α-
dc.subject.localtumor necrosis factor-alpha-
dc.subject.localTNFa-
dc.subject.localTumor necrosis factor alpha-
dc.subject.localTumor necrosis factor-alpha-
dc.subject.localTNF-α-
dc.subject.localtumor necrosis factor-α-
dc.subject.localapoptosis-
dc.subject.localApoptosis-
dc.subject.localcIAP-
dc.subject.localcIAPs-
dc.subject.localPeroxiredoxin-
dc.subject.localperoxiredoxin-
dc.subject.localPeroxiredoxins-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.