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Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation
Metabolic syndrome (MetS) and Type 2 diabetes mellitus (T2DM) increase risk for Alzheimer's disease (AD). The molecular mechanism for this association remains poorly defined. Here we report in human and rodent tissues that elevated glucose, as found in MetS/T2DM, and oligomeric β-amyloid (Aβ) p...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4729876/ https://www.ncbi.nlm.nih.gov/pubmed/26743041 http://dx.doi.org/10.1038/ncomms10242 |
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author | Akhtar, Mohd Waseem Sanz-Blasco, Sara Dolatabadi, Nima Parker, James Chon, Kevin Lee, Michelle S. Soussou, Walid McKercher, Scott R. Ambasudhan, Rajesh Nakamura, Tomohiro Lipton, Stuart A. |
author_facet | Akhtar, Mohd Waseem Sanz-Blasco, Sara Dolatabadi, Nima Parker, James Chon, Kevin Lee, Michelle S. Soussou, Walid McKercher, Scott R. Ambasudhan, Rajesh Nakamura, Tomohiro Lipton, Stuart A. |
author_sort | Akhtar, Mohd Waseem |
collection | PubMed |
description | Metabolic syndrome (MetS) and Type 2 diabetes mellitus (T2DM) increase risk for Alzheimer's disease (AD). The molecular mechanism for this association remains poorly defined. Here we report in human and rodent tissues that elevated glucose, as found in MetS/T2DM, and oligomeric β-amyloid (Aβ) peptide, thought to be a key mediator of AD, coordinately increase neuronal Ca(2+) and nitric oxide (NO) in an NMDA receptor-dependent manner. The increase in NO results in S-nitrosylation of insulin-degrading enzyme (IDE) and dynamin-related protein 1 (Drp1), thus inhibiting insulin and Aβ catabolism as well as hyperactivating mitochondrial fission machinery. Consequent elevation in Aβ levels and compromise in mitochondrial bioenergetics result in dysfunctional synaptic plasticity and synapse loss in cortical and hippocampal neurons. The NMDA receptor antagonist memantine attenuates these effects. Our studies show that redox-mediated posttranslational modification of brain proteins link Aβ and hyperglycaemia to cognitive dysfunction in MetS/T2DM and AD. |
format | Online Article Text |
id | pubmed-4729876 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-47298762016-03-04 Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation Akhtar, Mohd Waseem Sanz-Blasco, Sara Dolatabadi, Nima Parker, James Chon, Kevin Lee, Michelle S. Soussou, Walid McKercher, Scott R. Ambasudhan, Rajesh Nakamura, Tomohiro Lipton, Stuart A. Nat Commun Article Metabolic syndrome (MetS) and Type 2 diabetes mellitus (T2DM) increase risk for Alzheimer's disease (AD). The molecular mechanism for this association remains poorly defined. Here we report in human and rodent tissues that elevated glucose, as found in MetS/T2DM, and oligomeric β-amyloid (Aβ) peptide, thought to be a key mediator of AD, coordinately increase neuronal Ca(2+) and nitric oxide (NO) in an NMDA receptor-dependent manner. The increase in NO results in S-nitrosylation of insulin-degrading enzyme (IDE) and dynamin-related protein 1 (Drp1), thus inhibiting insulin and Aβ catabolism as well as hyperactivating mitochondrial fission machinery. Consequent elevation in Aβ levels and compromise in mitochondrial bioenergetics result in dysfunctional synaptic plasticity and synapse loss in cortical and hippocampal neurons. The NMDA receptor antagonist memantine attenuates these effects. Our studies show that redox-mediated posttranslational modification of brain proteins link Aβ and hyperglycaemia to cognitive dysfunction in MetS/T2DM and AD. Nature Publishing Group 2016-01-08 /pmc/articles/PMC4729876/ /pubmed/26743041 http://dx.doi.org/10.1038/ncomms10242 Text en Copyright © 2016, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Akhtar, Mohd Waseem Sanz-Blasco, Sara Dolatabadi, Nima Parker, James Chon, Kevin Lee, Michelle S. Soussou, Walid McKercher, Scott R. Ambasudhan, Rajesh Nakamura, Tomohiro Lipton, Stuart A. Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation |
title | Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation |
title_full | Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation |
title_fullStr | Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation |
title_full_unstemmed | Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation |
title_short | Elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation |
title_sort | elevated glucose and oligomeric β-amyloid disrupt synapses via a common pathway of aberrant protein s-nitrosylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4729876/ https://www.ncbi.nlm.nih.gov/pubmed/26743041 http://dx.doi.org/10.1038/ncomms10242 |
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