Mouse liver selenium-binding protein decreased in abundance by peroxisome proliferators

ELECTROPHORESISVolume 21, Issue 11 p. 2162-2169 Research Article Mouse liver selenium-binding protein decreased in abundance by peroxisome proliferators Carol S. Giometti, Corresponding Author Carol S. Giometti csgiometti@anl.gov. Biosciences Division, Argonne Laboratory, Argonne, IL, USABioscience Division, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA, Fax: +630-252-5517===Search for more papers by this authorXiaoli Liang, Xiaoli Liang Biosciences Division, Argonne Laboratory, Argonne, IL, USASearch for more papers by this authorSandra L. Tollaksen, Sandra L. Tollaksen Biosciences Division, Argonne Laboratory, Argonne, IL, USASearch for more papers by this authorDaniel B. Wall, Daniel B. Wall Chemistry Department, University of Michigan, Ann Arbor, MI, USASearch for more papers by this authorDavid M. Lubman, David M. Lubman Chemistry Department, University of Michigan, Ann Arbor, MI, USASearch for more papers by this authorVadrevu Subbarao, Vadrevu Subbarao Department of Pathology, Northwestern University Medical School and Lakeside Veterans Affairs, Medical Center, Chicago, IL, USASearch for more papers by this authorM. Sambasiva Rao, M. Sambasiva Rao Department of Pathology, Northwestern University Medical School and Lakeside Veterans Affairs, Medical Center, Chicago, IL, USASearch for more papers by this author Carol S. Giometti, Corresponding Author Carol S. Giometti csgiometti@anl.gov. Biosciences Division, Argonne Laboratory, Argonne, IL, USABioscience Division, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA, Fax: +630-252-5517===Search for more papers by this authorXiaoli Liang, Xiaoli Liang Biosciences Division, Argonne Laboratory, Argonne, IL, USASearch for more papers by this authorSandra L. Tollaksen, Sandra L. Tollaksen Biosciences Division, Argonne Laboratory, Argonne, IL, USASearch for more papers by this authorDaniel B. Wall, Daniel B. Wall Chemistry Department, University of Michigan, Ann Arbor, MI, USASearch for more papers by this authorDavid M. Lubman, David M. Lubman Chemistry Department, University of Michigan, Ann Arbor, MI, USASearch for more papers by this authorVadrevu Subbarao, Vadrevu Subbarao Department of Pathology, Northwestern University Medical School and Lakeside Veterans Affairs, Medical Center, Chicago, IL, USASearch for more papers by this authorM. Sambasiva Rao, M. Sambasiva Rao Department of Pathology, Northwestern University Medical School and Lakeside Veterans Affairs, Medical Center, Chicago, IL, USASearch for more papers by this author First published: 03 July 2000 https://doi.org/10.1002/1522-2683(20000601)21:11<2162::AID-ELPS2162>3.0.CO;2-SCitations: 31AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Several studies with two-dimensional gel electrophoresis (2-DE) have shown that the abundance of numerous mouse liver proteins is altered in response to treatment with chemicals known to cause peroxisome proliferation. The peptide masses from tryptic digests of two liver proteins showing dramatic decreases in abundance in response to numerous peroxisome proliferators were used to search sequence databases. The selenium-binding protein 2 (SBP2 formerly 56 kDa acetaminophen-binding protein, AP 56) and selenium-binding protein 1 (SBP1 formerly 56 kDa selenium-binding protein, SP 56) in mouse liver, proteins with a high degree of sequence similarity, were the highest ranked identities obtained. Identity with SBP2 was subsequently confirmed by immunodetection with specific antiserum. Treatment of mice with 0.025% ciprofibrate resulted in the more basic of this pair of proteins being decreased to 30% of control abundance while the acidic protein was decreased to 7% of the control amount. Dexamethasone treatment, in contrast, caused increases of 80% and 20% in the abundance of the acidic and basic forms, respectively. Administration of dexamethasone to mice in combination with ciprofibrate produced expression of the acidic SBP2 at 23% of the control level and the basic SBP2 at 36%, a slightly moderated reduction compared with the decrease that occurred with ciprofibrate alone. These data suggest that peroxisome proliferators such as ciprofibrate cause a decrease in the abundance of the SBP2, which leads to increased cell proliferation, even in the presence of an inhibitor such as dexamethasone. Such a decrease in SBP, thought to serve as cell growth regulation factors, could be central to the nongenotoxic carcinogenicity of the peroxisome proliferators observed in rodents. Citing Literature Volume21, Issue111 June 2000Pages 2162-2169 RelatedInformation