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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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Msrb1 (Methionine-R-Sulfoxide Reductase 1) Knock-Out Mice: Roles of Msrb1 in Redox Regulation and Identification of a Novel Selenoprotein Form University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Vadim Gladyshev Publications Biochemistry, Department of 2-27-2009 MsrB1 (Methionine-R-sulfoxide Reductase 1) Knock-out Mice: Roles of MsrB1 in Redox Regulation and Identification of a Novel Selenoprotein Form Dmitri E. Fomenko University of Nebraska-Lincoln, [email protected] Sergey V. Novoselov University of Nebraska-Lincoln, [email protected] Sathish Kumar Natarajan University of Nebraska-Lincoln, [email protected] Byung Cheon Lee University of Nebraska-Lincoln Ahmet Koc Izmir Institute of Technology, 35430 Urla, Izmir, Turkey See next page for additional authors Follow this and additional works at: https://digitalcommons.unl.edu/biochemgladyshev Part of the Biochemistry, Biophysics, and Structural Biology Commons Fomenko, Dmitri E.; Novoselov, Sergey V.; Natarajan, Sathish Kumar; Lee, Byung Cheon; Koc, Ahmet; Carlson, Bradley A.; Lee, Tae-Hyung; Kim, Hwa-Young; Hatfield, Dolph L.; and Gladyshev, Vadim N., "MsrB1 (Methionine-R-sulfoxide Reductase 1) Knock-out Mice: Roles of MsrB1 in Redox Regulation and Identification of a Novel Selenoprotein Form" (2009). Vadim Gladyshev Publications. 99. https://digitalcommons.unl.edu/biochemgladyshev/99 This Article is brought to you for free and open access by the Biochemistry, Department of at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Vadim Gladyshev Publications by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Authors Dmitri E. Fomenko, Sergey V. Novoselov, Sathish Kumar Natarajan, Byung Cheon Lee, Ahmet Koc, Bradley A. Carlson, Tae-Hyung Lee, Hwa-Young Kim, Dolph L. Hatfield, and adimV N. Gladyshev This article is available at DigitalCommons@University of Nebraska - Lincoln: https://digitalcommons.unl.edu/ biochemgladyshev/99 Supplemental Material can be found at: http://www.jbc.org/cgi/content/full/M805770200/DC1 THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 284, NO. 9, pp. 5986–5993, February 27, 2009 Printed in the U.S.A. MsrB1 (Methionine-R-sulfoxide Reductase 1) Knock-out Mice ROLES OF MsrB1 IN REDOX REGULATION AND IDENTIFICATION OF A NOVEL SELENOPROTEIN FORM*□S Received for publication, July 28, 2008, and in revised form, October 28, 2008 Published, JBC Papers in Press, November 6, 2008, DOI 10.1074/jbc.M805770200 Dmitri E. Fomenko‡, Sergey V. Novoselov‡, Sathish Kumar Natarajan‡, Byung Cheon Lee‡, Ahmet Koc§, Bradley A. Carlson¶, Tae-Hyung Leeʈ, Hwa-Young Kimʈ, Dolph L. Hatfield¶, and Vadim N. Gladyshev‡1 From the ‡Department of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, the §Department of Molecular Biology and Genetics, Izmir Institute of Technology, 35430 Urla, Izmir, Turkey, the ¶Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, CCR, NCI, National Institutes of Health, Bethesda, Maryland 20892, and the ʈDepartment of Biochemistry and Molecular Biology, Aging-associated Vascular Disease Research Center, Yeungnam University College of Medicine, Daegu 705-717, Republic of Korea Protein oxidation has been linked to accelerated aging and is a most other amino acids in proteins, Met is particularly suscep- contributing factor to many diseases. Methionine residues are par- tible to oxidation by reactive oxygen species. The product of ticularly susceptible to oxidation, but the resulting mixture of such oxidation is a diastereomeric mixture of Met sulfoxides: methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide Met R-sulfoxide (Met-RO)2 and Met S-sulfoxide (Met-SO). (Met-SO) can be repaired by thioredoxin-dependent enzymes These oxidized forms, however, can be reduced back to Met by MsrB and MsrA, respectively. Here, we describe a knock-out two enzyme families, MsrA (specific for Met-SO) and MsrB mouse deficient in selenoprotein MsrB1, the main mammalian (specific for Met-RO) (4, 5). MsrB located in the cytosol and nucleus. In these mice, in addition Mammals contain one MsrA, which is targeted to different to the deletion of 14-kDa MsrB1, a 5-kDa selenoprotein form was cellular compartments by alternative splicing and variable use specifically removed. Further studies revealed that the 5-kDa pro- of signal peptides (6, 7), and three MsrB isozymes, which are tein occurred in both mouse tissues and human HEK 293 cells; was individually targeted to different compartments (8–10). MsrB down-regulated by MsrB1 small interfering RNA, selenium defi- located in the cytosol and nucleus is known as MsrB1 (also ciency, and selenocysteine tRNA mutations; and was immunopre- designated as SelR or SelX). This protein is interesting in that it cipitated and recognized by MsrB1 antibodies. Specific labeling is a selenoprotein that contains selenocysteine (Sec) in place of with 75Se and mass spectrometry analyses revealed that the 5-kDa cysteine normally present in the catalytic sites of MsrBs and selenoprotein corresponded to the C-terminal sequence of MsrB1. MsrAs (11). Dietary selenium is known to regulate the expres- The MsrB1 knock-out mice lacked both 5- and 14-kDa MsrB1 sion of selenoproteins and to ultimately control the redox forms and showed reduced MsrB activity, with the strongest effect homeostasis in cells (12). Being a selenoprotein, the expression seen in liver and kidney. In addition, MsrA activity was decreased of MsrB1 can also be regulated by dietary selenium (13–15). by MsrB1 deficiency. Liver and kidney of the MsrB1 knock-out Knock-out of the MsrA gene in mice was described several mice also showed increased levels of malondialdehyde, protein car- years ago (16). The lack of MsrA results in the accumulation of bonyls, protein methionine sulfoxide, and oxidized glutathione as carbonyl derivatives (indicative of protein oxidation) (17), well as reduced levels of free and protein thiols, whereas these increased susceptibility to exposure to 100% oxygen, and vari- parameters were little changed in other organs examined. Overall, ous neurological abnormalities, such as tip-toe walking, abnor- this study established an important contribution of MsrB1 to the mal behavior, and lower locomotor activity (16, 18, 19). In addi- redox control in mouse liver and kidney and identified a novel form tion, MsrB expression and activity were down-regulated in of this protein. these mice (13). Most interestingly, MsrA knock-out mice showed a dramatically reduced life span (16), whereas overex- pression of this protein in fruit flies increased their life span (20, Oxidation of proteins has been implicated in a variety of dis- 21). These studies are consistent with the idea that repair of eases and is a factor that influences aging (1–3). Compared with oxidized proteins is a critical factor in neurological diseases and the aging process (4). * This work was supported, in whole or in part, by National Institutes of Health In contrast to MsrA, the consequence of MsrB deficiency in Grant AG021518 (to V. N. G.) and the Intramural Research Program of the mice or other animal models is not known (although MsrB also Center for Cancer Research, NCI, National Institutes of Health (to D. L. H.). can regulate the life span of yeast cells (22)). Selenium defi- The Nebraska Redox Biology Center is supported by National Institutes of Health Grant RR017675. This work was also supported by Korea Science ciency was used to reduce MsrB1 expression (13, 16), which and Engineering Foundation Grant R13-2005-005-01004-0 (to H. Y. K.). The resulted in lower MsrB activity as well as in a reduction in the costs of publication of this article were defrayed in part by the payment of levels of other selenoproteins. This treatment increased protein page charges. This article must therefore be hereby marked “advertise- ment” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. □S The on-line version of this article (available at http://www.jbc.org) contains 2 The abbreviations used are: Met-RO, methionine R-sulfoxide; Met-SO, supplemental Figs. S1–S3. methionine S-sulfoxide; KO, knock-out; Sec, selenocysteine; PBS, phos- 1 To whom correspondence should be addressed. Tel.: 402-472-4948; E-mail: phate-buffered saline; siRNA, small interfering RNA; LC, liquid chromatog- [email protected]. raphy; MS, mass spectrometry; Se, selenium. 5986 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME 284•NUMBER 9•FEBRUARY 27, 2009 MsrB1 Knock-out Mouse oxidation and the amount of Met sulfoxide residues (13). cells were detected, probably because of the high content of Whereas the knock-out of MsrA removed this protein in all repetitive elements in the vicinity of the MsrB1 gene (predicted tissues and compartments, the specific removal of individual with RepeatMasker, available on the World Wide Web). MsrBs offers an opportunity to examine the effects of MsrB As an alternative strategy, a mouse (in a 129/Sv genetic back- deficiency in different organs, cells, and compartments. ground) was generated at Texas Institute for Genomic Medi- In this work, we describe mice lacking MsrB1. We show that cine by taking advantage of the genetrap cassette inserted MsrB1 knock-out led to protein oxidation and affected other immediately downstream of the MsrB1 gene (Fig. 1B). parameters indicative of oxidative stress. Most effects were Homozygous MsrB1 KO mice were obtained by mating het- observed in the liver and kidney, where MsrB1 levels were par- erozygous mice and selecting for homozygous MsrB1 KO by ticularly high, whereas several other organs were not affected. genetic screening. Mice were handled following the
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