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Glutaredoxin 2a, a mitochondrial isoform, plays a protective role in a human cell line under serum deprivation

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dc.contributor.authorKim, Su-Jung-
dc.contributor.authorJung, Hyun-Joo-
dc.contributor.authorChoi, Hojin-
dc.contributor.authorLim, Chang-Jin-
dc.date.accessioned2022-07-16T15:59:28Z-
dc.date.available2022-07-16T15:59:28Z-
dc.date.created2021-05-12-
dc.date.issued2012-04-
dc.identifier.issn0301-4851-
dc.identifier.urihttps://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/165915-
dc.description.abstractThe roles of mitochondrial glutaredoxin (Grx2a) under serum deprivation were assessed using the human stable HepG2 cell lines overexpressing or down-regulating Grx2a. The Grx2a-overexpressing stable cells displayed enhanced proliferation, decreased reactive oxygen species (ROS) and caspase-3 activity levels, and increased total GSH level, compared to the vector control cells. These characteristics of the overexpressing stable cells were reversed by down-regulating Grx2a in the same cell line. In the limited serum conditions, the Grx2a-overexpressing stable pcDNA3.0/HA-Grx2a cells exhibited higher cellular viabilities and total GSH level, and showed much lower enhancement in ROS and caspase-3 activity levels than the vector control pcDNA3.0/HA cells. However, the Grx2a-down-regulating stable cells gave rise to diminished cellular viabilities and further decreased total GSH level, and contained significantly higher ROS and caspase-3 activity levels, under serum deprivation than the vector control cells. These results suggest that Grx2a plays proliferative and anti-apoptotic roles under serum deprivation.-
dc.language영어-
dc.language.isoen-
dc.publisherSPRINGER-
dc.titleGlutaredoxin 2a, a mitochondrial isoform, plays a protective role in a human cell line under serum deprivation-
dc.typeArticle-
dc.contributor.affiliatedAuthorChoi, Hojin-
dc.identifier.doi10.1007/s11033-011-1152-0-
dc.identifier.scopusid2-s2.0-84862998387-
dc.identifier.wosid000301108500044-
dc.identifier.bibliographicCitationMOLECULAR BIOLOGY REPORTS, v.39, no.4, pp.3755 - 3765-
dc.relation.isPartOfMOLECULAR BIOLOGY REPORTS-
dc.citation.titleMOLECULAR BIOLOGY REPORTS-
dc.citation.volume39-
dc.citation.number4-
dc.citation.startPage3755-
dc.citation.endPage3765-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.subject.keywordPlusPROTEIN S-GLUTATHIONYLATION-
dc.subject.keywordPlusLENS EPITHELIAL-CELLS-
dc.subject.keywordPlusINDUCED APOPTOSIS-
dc.subject.keywordPlusOXIDATIVE STRESS-
dc.subject.keywordPlusTHIOREDOXIN REDUCTASE-
dc.subject.keywordPlusREDOX REGULATION-
dc.subject.keywordPlusDNA-DAMAGE-
dc.subject.keywordPlusDEATH-
dc.subject.keywordPlusTHIOLTRANSFERASE-
dc.subject.keywordPlusOVEREXPRESSION-
dc.subject.keywordAuthorGlutaredoxin-
dc.subject.keywordAuthorReactive oxygen species-
dc.subject.keywordAuthorSerum deprivation-
dc.subject.keywordAuthorApoptosis-
dc.identifier.urlhttps://link.springer.com/article/10.1007/s11033-011-1152-0-
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