MsrB1 Methionine R sulfoxide Reductase 1 Knock out Mice ROLES OF MsrB1 IN REDOX REGULATION AND IDENTIFICATION OF A NOVEL SELENOPROTEIN FORM

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dc.contributor.authorDima, Fomenko
dc.contributor.authorSergey, Novoselov
dc.contributor.authorSathish, Natarajan
dc.contributor.authorKoç, Ahmet
dc.contributor.authorBrad, Carlson
dc.contributor.authorLee, TH
dc.contributor.authorHatfield, Dolph
dc.contributor.authorVadim, Nebraska
dc.date.accessioned2017-06-12T13:18:36Z
dc.date.available2017-06-12T13:18:36Z
dc.date.issued2009
dc.departmentİnönü Üniversitesien_US
dc.descriptionJournal of Biological Chemistryen_US
dc.description.abstractProtein oxidation has been linked to accelerated aging and is a contributing factor to many diseases.Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively. Here, we describe a knock-out mouse deficient in selenoprotein MsrB1, the main mammalian MsrB located in the cytosol and nucleus. In these mice, in addition to the deletion of 14-kDa MsrB1, a 5-kDa selenoprotein form was specifically removed. Further studies revealed that the 5-kDa protein occurred in both mouse tissues and human HEK 293 cells; was down-regulated by MsrB1 small interfering RNA, selenium deficiency, and selenocysteine tRNA mutations; and was immunoprecipitated and recognized by MsrB1 antibodies. Specific labeling with 75Se and mass spectrometry analyses revealed that the 5-kDa selenoprotein corresponded to the C-terminal sequence of MsrB1. The MsrB1 knock-out mice lacked both 5- and 14-kDa MsrB1 forms and showed reduced MsrB activity, with the strongest effect seen in liver and kidney. In addition, MsrA activity was decreased by MsrB1 deficiency. Liver and kidney of the MsrB1 knock-out mice also showedincreasedlevels ofmalondialdehyde, protein carbonyls, protein methionine sulfoxide, and oxidized glutathione as well as reduced levels of free and protein thiols, whereas these parameters were little changed in other organs examined. Overall, this study established an important contribution of MsrB1 to the redox controlinmouseliver and kidney andidentified a novel form of this protein.en_US
dc.identifier.citationDima, F., Sergey, N., Sathish, N., BC, L., KOÇ, A., Brad, C., … Vadim, N. (2009). Msrb1 Methionine R Sulfoxide Reductase 1 Knock Out Mice ROLES OF Msrb1 IN REDOX REGULATION AND IDENTIFICATION OF A NOVEL SELENOPROTEIN FORM. Journal Of Biological Chemistry, 284(9), 5986–5993.en_US
dc.identifier.doi10.1074/jbc.M805770200en_US
dc.identifier.endpage5993en_US
dc.identifier.issue9en_US
dc.identifier.startpage5986en_US
dc.identifier.urihttp://www.jbc.org/cgi/doi/10.1074/jbc.M805770200
dc.identifier.urihttps://hdl.handle.net/11616/7086
dc.identifier.volume284en_US
dc.language.isoenen_US
dc.publisherJournal of Biological Chemistryen_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleMsrB1 Methionine R sulfoxide Reductase 1 Knock out Mice ROLES OF MsrB1 IN REDOX REGULATION AND IDENTIFICATION OF A NOVEL SELENOPROTEIN FORMen_US
dc.typeArticleen_US

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