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Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity

DC FieldValueLanguage
dc.contributor.author김형중-
dc.date.accessioned2016-02-19T11:07:14Z-
dc.date.available2016-02-19T11:07:14Z-
dc.date.issued2001-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/142441-
dc.description.abstractSix distinct peroxiredoxin (Prx) proteins (Prx I-VI) from distinct genes have been identified in mammalian tissues. Prxs are members of a group of peroxidases that have conserved reactive cysteine residue(s) in the active site(s). An immediate physiological electron donor for the peroxidase catalysis for five Prx proteins (Prx I-V) has been identified as thioredoxin (Trx), but that for Prx VI (1-Cys Prx) is still unclear. To identify an immediate electron donor and a binding protein for Prx VI, we performed a Prx VI protein overlay assay. A 20-kDa binding protein was identified by the Prx VI protein overlay assay with flow-through fractions from a High-Q column with rat lung crude extracts. Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF) and MS-Fit, we identified the 20-kDa Prx VI-binding protein as a cyclophilin A (CyP-A). The binding of recombinant human CyP-A (hCyP-A) to Prx VI was confirmed by using the hCyP-A protein overlay assay and Western immunoblot analysis with hCyP-A-specific antibodies. hCyP-A enhanced the antioxidant activity of Prx VI, as well as the other known mammalian Prx isotypes. hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems. Prx II was reduced by hCyP-A without help from any other reductant, and the reduction was cyclosporin A-independent. These results strongly suggest that CyP-A not only binds to Prx proteins but also supports its peroxidase activity as an immediate electron donor. In addition, Cys(115) and Cys(161) of hCyP-A were found to be involved in the activation and the reduction of Prx.-
dc.description.statementOfResponsibilityopen-
dc.format.extent29826~29832-
dc.relation.isPartOfJournal of Biological Chemistry-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleCyclophilin a binds to peroxiredoxins and activates its peroxidase activity-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Internal Medicine (내과학)-
dc.contributor.googleauthorSang Pil Lee-
dc.contributor.googleauthorYoung Sun Hwang-
dc.contributor.googleauthorYong Jun Kim-
dc.contributor.googleauthorKi-Sun Kwon-
dc.contributor.googleauthorHyung Jung Kim-
dc.contributor.googleauthorKanghwa Kim-
dc.contributor.googleauthorHo Zoon Chae-
dc.identifier.doi10.1074/jbc.M101822200-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA01158-
dc.relation.journalcodeJ01258-
dc.contributor.alternativeNameKim, Hyung Jung-
dc.contributor.affiliatedAuthorKim, Hyung Jung-
dc.rights.accessRightsfree-
dc.citation.volume276-
dc.citation.number32-
dc.citation.startPage29826-
dc.citation.endPage29832-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, Vol.276(32) : 29826-29832, 2001-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers

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