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Nucleic Acids Research Advance Access originally published online on June 6, 2007
Nucleic Acids Research 2007 35(12):3963-3973; doi:10.1093/nar/gkm355
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Nucleic Acids Research, 2007, Vol. 35, No. 12 3963-3973
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.


Molecular Biology

The selenoproteome exhibits widely varying, tissue-specific dependence on selenoprotein P for selenium supply

Peter R. Hoffmann*, Simone C. Höge, Ping-An Li, Fukun W. Hoffmann, Ann C. Hashimoto and Marla J. Berry

Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI 96813, USA

*To whom correspondence should be addressed. Tel: +1 808 692 1510; Fax: +1 808 692 1970; Email: peterh{at}pbrc.hawaii.edu

Received March 16, 2007. Revised April 18, 2007. Accepted April 23, 2007.

Selenoprotein P (Sel P) is a selenium-rich glycoprotein believed to play a key role in selenium (Se) transport throughout the body. Development of a Sel P knockout mouse model has supported this notion and initial studies have indicated that selenium supply to various tissues is differentially affected by genetic deletion of Sel P. Se in the form of the amino acid, selenocysteine, is incorporated into selenoproteins at UGA codons. Thus, Se availability affects not only selenoprotein levels, but also the turnover of selenoprotein mRNAs via the nonsense-mediated decay pathway. We investigated how genetic deletion of Sel P in mice affected levels of the mRNAs encoding all known members of the murine selenoprotein family, as well as three non-selenoprotein factors involved in their synthesis, selenophosphate synthetase 1 (SPS1), SECIS-binding protein 2 (SBP2) and SECp43. Our findings present a comprehensive description of selenoprotein mRNA expression in the following murine tissues: brain, heart, intestine, kidney, liver, lung, spleen and testes. We also describe how abundance of selenoproteins and selenoprotein-synthesis factors are affected by genetic deletion of Sel P in some of these tissues, providing insight into how the presence of this selenoprotein influences selenoprotein mRNA levels, and thus, the selenoproteome.


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