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The Subcellular Location of Selenoproteins and the Impact on Their Function

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...

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Autor principal: Diamond, Alan M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446787/
https://www.ncbi.nlm.nih.gov/pubmed/26007340
http://dx.doi.org/10.3390/nu7053938
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author Diamond, Alan M.
author_facet Diamond, Alan M.
author_sort Diamond, Alan M.
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description 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.
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spelling pubmed-44467872015-05-29 The Subcellular Location of Selenoproteins and the Impact on Their Function Diamond, Alan M. Nutrients Review 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. MDPI 2015-05-22 /pmc/articles/PMC4446787/ /pubmed/26007340 http://dx.doi.org/10.3390/nu7053938 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Diamond, Alan M.
The Subcellular Location of Selenoproteins and the Impact on Their Function
title The Subcellular Location of Selenoproteins and the Impact on Their Function
title_full The Subcellular Location of Selenoproteins and the Impact on Their Function
title_fullStr The Subcellular Location of Selenoproteins and the Impact on Their Function
title_full_unstemmed The Subcellular Location of Selenoproteins and the Impact on Their Function
title_short The Subcellular Location of Selenoproteins and the Impact on Their Function
title_sort subcellular location of selenoproteins and the impact on their function
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4446787/
https://www.ncbi.nlm.nih.gov/pubmed/26007340
http://dx.doi.org/10.3390/nu7053938
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