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A more recent version of this article appeared on April 20, 2007
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M611403200v1
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Papers In Press, published online ahead of print February 21, 2007
J. Biol. Chem, 10.1074/jbc.M611403200
Submitted on December 12, 2006
Revised on February 20, 2007
Accepted on February 21, 2007

Apolipoprotein E receptor-2 (ApoER2) mediates selenium uptake from selenoprotein P by the mouse testis

Gary E. Olson, Virginia P. Winfrey, Subir K. NagDas, Kristina E. Hill, and Raymond F. Burk

Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232

Corresponding Author: gary.olson{at}vanderbilt.edu

Selenium is a micronutrient that is essential for production of normal spermatozoa. The selenium-rich plasma protein, selenoprotein P (Sepp1), is required for maintenance of testis selenium and for fertility of the male mouse. Sepp1 trafficking in the seminiferous epithelium was studied using conventional methods and mice with gene deletions. Immunocytochemistry demonstrated that Sepp1 is present in vesicle-like structures in the basal region of Sertoli cells, suggesting that the protein is taken up intact. Sepp1-affinity chromatography of a testicular extract, followed by mass spectrometry-based identification of bound proteins, identified apolipoprotein E receptor 2 (ApoER2) as a candidate testis Sepp1 receptor. In situ hybridization analysis identified Sertoli cells as the only cell type in the seminiferous epithelium with detectable ApoER2 expression. Testis selenium levels in apoER2-/- males were sharply reduced from those in apoER2+/+ males and were comparable to the depressed levels found in Sepp1-/- males. However liver selenium levels were unchanged by deletion of apoER2. Immunocytochemistry did not detect Sepp1 in the Sertoli cells of apoER2-/- males, consistent with a defect in the receptor-mediated Sepp1 uptake pathway. Phase contrast microscopy revealed identical sperm defects in apoER2-/- and Sepp1-/- mice. Co-immunoprecipitation analysis demonstrated an interaction of testis ApoER2 with Sepp1. These data demonstrate that Sertoli cell ApoER2 is a Sepp1 receptor and a component of the selenium delivery pathway to spermatogenic cells.


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