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Nutrients 2015, 7(5), 3938-3948; doi:10.3390/nu7053938

The Subcellular Location of Selenoproteins and the Impact on Their Function

Department of Pathology, University of Illinois at Chicago, Chicago, IL 60612, USA
Received: 8 April 2015 / Revised: 14 May 2015 / Accepted: 15 May 2015 / Published: 22 May 2015
(This article belongs to the Special Issue Dietary Selenium and Human Health)
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Abstract

Most human selenium containing proteins contain selenium in the form of the amino acid selenocysteine, which is encoded in the corresponding mRNA as a UGA codon. Only a few non-selenocysteine containing selenoproteins are present and the nature of the association with selenium is not well understood. This review focuses on two selenocysteine-containing proteins that are members of the glutathione peroxidase family, GPx-1 and GPx-4, and the selenium-associated protein referred to as Selenium Binding Protein 1. Each of these proteins have been described to reside in two or more cellular compartments, and in the case of GPx-1 and SBP1, interact with each other. The enzymatic activity of GPx-1 and GPx-4 have been well described, but it is less clear how their cellular location impacts the health related phenotypes associated with activities, while no catalytic function is assigned to SBP1. The distribution of these proteins is presented as is the possible consequences of that compartmentalization. View Full-Text
Keywords: selenium; selenoproteins; peroxidases; compartmentalization; cancer selenium; selenoproteins; peroxidases; compartmentalization; cancer
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Diamond, A.M. The Subcellular Location of Selenoproteins and the Impact on Their Function. Nutrients 2015, 7, 3938-3948.

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