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Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease

Selenoproteins form a group of proteins of which its members contain at least one selenocysteine, and most of them serve oxidoreductase functions. Selenoprotein F (SELENOF), one of the 25 currently identified selenoproteins, is located in the endoplasmic reticulum (ER) organelle and is abundantly ex...

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Autores principales: Ren, Bingyu, Liu, Min, Ni, Jiazuan, Tian, Jing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6266307/
https://www.ncbi.nlm.nih.gov/pubmed/30400132
http://dx.doi.org/10.3390/nu10111619
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author Ren, Bingyu
Liu, Min
Ni, Jiazuan
Tian, Jing
author_facet Ren, Bingyu
Liu, Min
Ni, Jiazuan
Tian, Jing
author_sort Ren, Bingyu
collection PubMed
description Selenoproteins form a group of proteins of which its members contain at least one selenocysteine, and most of them serve oxidoreductase functions. Selenoprotein F (SELENOF), one of the 25 currently identified selenoproteins, is located in the endoplasmic reticulum (ER) organelle and is abundantly expressed in many tissues. It is regulated according to its selenium status, as well as by cell stress conditions. SELENOF may be functionally linked to protein folding and the secretion process in the ER. Several studies have reported positive associations between SELENOF genetic variations and several types of cancer. Also, altered expression levels of SELENOF have been found in cancer cases and neurodegenerative diseases. In this review, we summarize the current understanding of the structure, expression, and potential function of SELENOF and discuss its possible relation with various pathological processes.
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spelling pubmed-62663072018-12-06 Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease Ren, Bingyu Liu, Min Ni, Jiazuan Tian, Jing Nutrients Review Selenoproteins form a group of proteins of which its members contain at least one selenocysteine, and most of them serve oxidoreductase functions. Selenoprotein F (SELENOF), one of the 25 currently identified selenoproteins, is located in the endoplasmic reticulum (ER) organelle and is abundantly expressed in many tissues. It is regulated according to its selenium status, as well as by cell stress conditions. SELENOF may be functionally linked to protein folding and the secretion process in the ER. Several studies have reported positive associations between SELENOF genetic variations and several types of cancer. Also, altered expression levels of SELENOF have been found in cancer cases and neurodegenerative diseases. In this review, we summarize the current understanding of the structure, expression, and potential function of SELENOF and discuss its possible relation with various pathological processes. MDPI 2018-11-02 /pmc/articles/PMC6266307/ /pubmed/30400132 http://dx.doi.org/10.3390/nu10111619 Text en © 2018 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ren, Bingyu
Liu, Min
Ni, Jiazuan
Tian, Jing
Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease
title Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease
title_full Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease
title_fullStr Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease
title_full_unstemmed Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease
title_short Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease
title_sort role of selenoprotein f in protein folding and secretion: potential involvement in human disease
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6266307/
https://www.ncbi.nlm.nih.gov/pubmed/30400132
http://dx.doi.org/10.3390/nu10111619
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