Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis

Abstract Mass spectrometry (MS)-based proteomics is a powerful tool to explore pathogenic changes of a disease in an unbiased manner and has been used extensively in Alzheimer disease (AD) research. Here, by performing a meta-analysis of high-quality proteomic studies, we address which pathological...

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Autores principales: Hazal Haytural, Rui Benfeitas, Sophia Schedin-Weiss, Erika Bereczki, Melinda Rezeli, Richard D. Unwin, Xusheng Wang, Eric B. Dammer, Erik C. B. Johnson, Nicholas T. Seyfried, Bengt Winblad, Betty M. Tijms, Pieter Jelle Visser, Susanne Frykman, Lars O. Tjernberg
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Publicado: Nature Portfolio 2021
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spelling oai:doaj.org-article:d189ee05892c4b5e8df9e6a2031f92462021-12-05T12:18:02ZInsights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis10.1038/s41597-021-01090-82052-4463https://doaj.org/article/d189ee05892c4b5e8df9e6a2031f92462021-12-01T00:00:00Zhttps://doi.org/10.1038/s41597-021-01090-8https://doaj.org/toc/2052-4463Abstract Mass spectrometry (MS)-based proteomics is a powerful tool to explore pathogenic changes of a disease in an unbiased manner and has been used extensively in Alzheimer disease (AD) research. Here, by performing a meta-analysis of high-quality proteomic studies, we address which pathological changes are observed consistently and therefore most likely are of great importance for AD pathogenesis. We retrieved datasets, comprising a total of 21,588 distinct proteins identified across 857 postmortem human samples, from ten studies using labeled or label-free MS approaches. Our meta-analysis findings showed significant alterations of 757 and 1,195 proteins in AD in the labeled and label-free datasets, respectively. Only 33 proteins, some of which were associated with synaptic signaling, had the same directional change across the individual studies. However, despite alterations in individual proteins being different between the labeled and the label-free datasets, several pathways related to synaptic signaling, oxidative phosphorylation, immune response and extracellular matrix were commonly dysregulated in AD. These pathways represent robust changes in the human AD brain and warrant further investigation.Hazal HayturalRui BenfeitasSophia Schedin-WeissErika BereczkiMelinda RezeliRichard D. UnwinXusheng WangEric B. DammerErik C. B. JohnsonNicholas T. SeyfriedBengt WinbladBetty M. TijmsPieter Jelle VisserSusanne FrykmanLars O. TjernbergNature PortfolioarticleScienceQENScientific Data, Vol 8, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Hazal Haytural
Rui Benfeitas
Sophia Schedin-Weiss
Erika Bereczki
Melinda Rezeli
Richard D. Unwin
Xusheng Wang
Eric B. Dammer
Erik C. B. Johnson
Nicholas T. Seyfried
Bengt Winblad
Betty M. Tijms
Pieter Jelle Visser
Susanne Frykman
Lars O. Tjernberg
Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis
description Abstract Mass spectrometry (MS)-based proteomics is a powerful tool to explore pathogenic changes of a disease in an unbiased manner and has been used extensively in Alzheimer disease (AD) research. Here, by performing a meta-analysis of high-quality proteomic studies, we address which pathological changes are observed consistently and therefore most likely are of great importance for AD pathogenesis. We retrieved datasets, comprising a total of 21,588 distinct proteins identified across 857 postmortem human samples, from ten studies using labeled or label-free MS approaches. Our meta-analysis findings showed significant alterations of 757 and 1,195 proteins in AD in the labeled and label-free datasets, respectively. Only 33 proteins, some of which were associated with synaptic signaling, had the same directional change across the individual studies. However, despite alterations in individual proteins being different between the labeled and the label-free datasets, several pathways related to synaptic signaling, oxidative phosphorylation, immune response and extracellular matrix were commonly dysregulated in AD. These pathways represent robust changes in the human AD brain and warrant further investigation.
format article
author Hazal Haytural
Rui Benfeitas
Sophia Schedin-Weiss
Erika Bereczki
Melinda Rezeli
Richard D. Unwin
Xusheng Wang
Eric B. Dammer
Erik C. B. Johnson
Nicholas T. Seyfried
Bengt Winblad
Betty M. Tijms
Pieter Jelle Visser
Susanne Frykman
Lars O. Tjernberg
author_facet Hazal Haytural
Rui Benfeitas
Sophia Schedin-Weiss
Erika Bereczki
Melinda Rezeli
Richard D. Unwin
Xusheng Wang
Eric B. Dammer
Erik C. B. Johnson
Nicholas T. Seyfried
Bengt Winblad
Betty M. Tijms
Pieter Jelle Visser
Susanne Frykman
Lars O. Tjernberg
author_sort Hazal Haytural
title Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis
title_short Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis
title_full Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis
title_fullStr Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis
title_full_unstemmed Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis
title_sort insights into the changes in the proteome of alzheimer disease elucidated by a meta-analysis
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/d189ee05892c4b5e8df9e6a2031f9246
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