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Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation

Selenoprotein M (SelM), one of the executants of selenium in vivo, is highly expressed in human brain and most probably involved in antioxidation, neuroprotection, and intracellular calcium regulation, which are the key factors for preventing the onset and progression of Alzheimer’s disease (AD). In...

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Autores principales: Chen, Ping, Wang, Ruo-Ran, Ma, Xiao-Jie, Liu, Qiong, Ni, Jia-Zuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634452/
https://www.ncbi.nlm.nih.gov/pubmed/23439548
http://dx.doi.org/10.3390/ijms14034385
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author Chen, Ping
Wang, Ruo-Ran
Ma, Xiao-Jie
Liu, Qiong
Ni, Jia-Zuan
author_facet Chen, Ping
Wang, Ruo-Ran
Ma, Xiao-Jie
Liu, Qiong
Ni, Jia-Zuan
author_sort Chen, Ping
collection PubMed
description Selenoprotein M (SelM), one of the executants of selenium in vivo, is highly expressed in human brain and most probably involved in antioxidation, neuroprotection, and intracellular calcium regulation, which are the key factors for preventing the onset and progression of Alzheimer’s disease (AD). In this paper, human SelM was successfully overexpressed in human embryonic kidney cells HEK293T. Sodium selenite (Na(2)SeO(3) 0.5 μmol/L) increased the expression of full-length SelM and inhibited the expression of truncated SelM. The full-length SelM exhibited higher antioxidant activity than its selenocysteine-to-cysteine mutation form SelM’, whereas the truncated SelM had an adverse effect that increased the oxidative stress level of cells. When β-amyloid (Aβ(42), an AD relevant peptide) was cotransfected with the empty expression vector, SelM, or SelM’ under the induction of 0.5 μmol/L Na(2)SeO(3), the intracellular Aβ(42) aggregation rates were detected to be 57.9% ± 5.5%, or 22.3% ± 2.6%, or 26.3% ± 2.1%, respectively, showing the inhibitory effects on Aβ aggregation by the full-length SelM and SelM’. Meanwhile, the intumescentia of mitochondria caused by Aβ(42) transfection was significantly mitigated by the cotransfection of SelM or SelM’ with Aβ(42) under the induction of 0.5 μmol/L Na(2)SeO(3). On the contrary, cotransfection of SelM and Aβ(42) without the induction of Na(2)SeO(3) increased Aβ(42) aggregation rate to 65.1% ± 3.2%, and it could not inhibit the Aβ-induced intumescent mitochondria. In conclusion, full-length SelM and SelM’ might prevent Aβ aggregation by resisting oxidative stress generated during the formation of Aβ oligomers in cells.
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spelling pubmed-36344522013-05-02 Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation Chen, Ping Wang, Ruo-Ran Ma, Xiao-Jie Liu, Qiong Ni, Jia-Zuan Int J Mol Sci Article Selenoprotein M (SelM), one of the executants of selenium in vivo, is highly expressed in human brain and most probably involved in antioxidation, neuroprotection, and intracellular calcium regulation, which are the key factors for preventing the onset and progression of Alzheimer’s disease (AD). In this paper, human SelM was successfully overexpressed in human embryonic kidney cells HEK293T. Sodium selenite (Na(2)SeO(3) 0.5 μmol/L) increased the expression of full-length SelM and inhibited the expression of truncated SelM. The full-length SelM exhibited higher antioxidant activity than its selenocysteine-to-cysteine mutation form SelM’, whereas the truncated SelM had an adverse effect that increased the oxidative stress level of cells. When β-amyloid (Aβ(42), an AD relevant peptide) was cotransfected with the empty expression vector, SelM, or SelM’ under the induction of 0.5 μmol/L Na(2)SeO(3), the intracellular Aβ(42) aggregation rates were detected to be 57.9% ± 5.5%, or 22.3% ± 2.6%, or 26.3% ± 2.1%, respectively, showing the inhibitory effects on Aβ aggregation by the full-length SelM and SelM’. Meanwhile, the intumescentia of mitochondria caused by Aβ(42) transfection was significantly mitigated by the cotransfection of SelM or SelM’ with Aβ(42) under the induction of 0.5 μmol/L Na(2)SeO(3). On the contrary, cotransfection of SelM and Aβ(42) without the induction of Na(2)SeO(3) increased Aβ(42) aggregation rate to 65.1% ± 3.2%, and it could not inhibit the Aβ-induced intumescent mitochondria. In conclusion, full-length SelM and SelM’ might prevent Aβ aggregation by resisting oxidative stress generated during the formation of Aβ oligomers in cells. Molecular Diversity Preservation International (MDPI) 2013-02-25 /pmc/articles/PMC3634452/ /pubmed/23439548 http://dx.doi.org/10.3390/ijms14034385 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Chen, Ping
Wang, Ruo-Ran
Ma, Xiao-Jie
Liu, Qiong
Ni, Jia-Zuan
Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
title Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
title_full Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
title_fullStr Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
title_full_unstemmed Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
title_short Different Forms of Selenoprotein M Differentially Affect Aβ Aggregation and ROS Generation
title_sort different forms of selenoprotein m differentially affect aβ aggregation and ros generation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634452/
https://www.ncbi.nlm.nih.gov/pubmed/23439548
http://dx.doi.org/10.3390/ijms14034385
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