Cited 188 times in
Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity
DC Field | Value | Language |
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dc.contributor.author | 김형중 | - |
dc.date.accessioned | 2016-02-19T11:07:14Z | - |
dc.date.available | 2016-02-19T11:07:14Z | - |
dc.date.issued | 2001 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/142441 | - |
dc.description.abstract | Six 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.statementOfResponsibility | open | - |
dc.format.extent | 29826~29832 | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Animals | - |
dc.subject.MESH | Antioxidants/pharmacology | - |
dc.subject.MESH | Ascorbic Acid/pharmacology | - |
dc.subject.MESH | Binding Sites | - |
dc.subject.MESH | Blotting, Western | - |
dc.subject.MESH | Catalysis | - |
dc.subject.MESH | Cyclophilin A/pharmacology* | - |
dc.subject.MESH | Cyclosporine/pharmacology | - |
dc.subject.MESH | Cysteine/chemistry | - |
dc.subject.MESH | Dose-Response Relationship, Drug | - |
dc.subject.MESH | Enzyme Activation | - |
dc.subject.MESH | Escherichia coli/metabolism | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Lung/metabolism | - |
dc.subject.MESH | Peroxidases/metabolism* | - |
dc.subject.MESH | Peroxiredoxin VI | - |
dc.subject.MESH | Peroxiredoxins | - |
dc.subject.MESH | Protein Binding | - |
dc.subject.MESH | Protein Conformation | - |
dc.subject.MESH | Rats | - |
dc.subject.MESH | Recombinant Proteins/metabolism | - |
dc.subject.MESH | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | - |
dc.subject.MESH | Subcellular Fractions | - |
dc.subject.MESH | Time Factors | - |
dc.title | Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Internal Medicine (내과학) | - |
dc.contributor.googleauthor | Sang Pil Lee | - |
dc.contributor.googleauthor | Young Sun Hwang | - |
dc.contributor.googleauthor | Yong Jun Kim | - |
dc.contributor.googleauthor | Ki-Sun Kwon | - |
dc.contributor.googleauthor | Hyung Jung Kim | - |
dc.contributor.googleauthor | Kanghwa Kim | - |
dc.contributor.googleauthor | Ho Zoon Chae | - |
dc.identifier.doi | 10.1074/jbc.M101822200 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A01158 | - |
dc.relation.journalcode | J01258 | - |
dc.identifier.eissn | 1083-351X | - |
dc.identifier.pmid | 11390385 | - |
dc.contributor.alternativeName | Kim, Hyung Jung | - |
dc.contributor.affiliatedAuthor | Kim, Hyung Jung | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 276 | - |
dc.citation.number | 32 | - |
dc.citation.startPage | 29826 | - |
dc.citation.endPage | 29832 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.276(32) : 29826-29832, 2001 | - |
dc.identifier.rimsid | 31005 | - |
dc.type.rims | ART | - |
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