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Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function
Mitochondrial dysfunction and oxidative stress are frequently observed in the early stages of Alzheimer's disease (AD). Studies have shown that presenilin-1 (PS1), the catalytic subunit of γ-secretase whose mutation is linked to familial AD (FAD), localizes to the mitochondrial membrane and reg...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Ivyspring International Publisher
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8419044/ https://www.ncbi.nlm.nih.gov/pubmed/34522215 http://dx.doi.org/10.7150/thno.59776 |
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author | Han, Jihoon Park, Heejin Maharana, Chinmoyee Gwon, A-Ryeong Park, Jinsu Baek, Seung Hyun Bae, Han-Gyu Cho, Yoonsuk Kim, Hark Kyun Sul, Jae Hoon Lee, Jeongmi Kim, Eunae Kim, Junsik Cho, Yongeun Park, Sunyoung Palomera, Leon F. Arumugam, Thiruma V. Mattson, Mark P. Jo, Dong-Gyu |
author_facet | Han, Jihoon Park, Heejin Maharana, Chinmoyee Gwon, A-Ryeong Park, Jinsu Baek, Seung Hyun Bae, Han-Gyu Cho, Yoonsuk Kim, Hark Kyun Sul, Jae Hoon Lee, Jeongmi Kim, Eunae Kim, Junsik Cho, Yongeun Park, Sunyoung Palomera, Leon F. Arumugam, Thiruma V. Mattson, Mark P. Jo, Dong-Gyu |
author_sort | Han, Jihoon |
collection | PubMed |
description | Mitochondrial dysfunction and oxidative stress are frequently observed in the early stages of Alzheimer's disease (AD). Studies have shown that presenilin-1 (PS1), the catalytic subunit of γ-secretase whose mutation is linked to familial AD (FAD), localizes to the mitochondrial membrane and regulates its homeostasis. Thus, we investigated how five PS1 mutations (A431E, E280A, H163R, M146V, and Δexon9) observed in FAD affect mitochondrial functions. Methods: We used H4 glioblastoma cell lines genetically engineered to inducibly express either the wild-type PS1 or one of the five PS1 mutants in order to examine mitochondrial morphology, dynamics, membrane potential, ATP production, mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs), oxidative stress, and bioenergetics. Furthermore, we used brains of PS1M146V knock-in mice, 3xTg-AD mice, and human AD patients in order to investigate the role of PS1 in regulating MAMs formation. Results: Each PS1 mutant exhibited slightly different mitochondrial dysfunction. Δexon9 mutant induced mitochondrial fragmentation while A431E, E280A, H163R, and M146V mutants increased MAMs formation. A431E, E280A, M146V, and Δexon9 mutants also induced mitochondrial ROS production. A431E mutant impaired both complex I and peroxidase activity while M146V mutant only impaired peroxidase activity. All PS1 mutants compromised mitochondrial membrane potential and cellular ATP levels were reduced by A431E, M146V, and Δexon9 mutants. Through comparative profiling of hippocampal gene expression in PS1M146V knock-in mice, we found that PS1M146V upregulates Atlastin 2 (ATL2) expression level, which increases ER-mitochondria contacts. Down-regulation of ATL2 after PS1 mutant induction rescued abnormally elevated ER-mitochondria interactions back to the normal level. Moreover, ATL2 expression levels were significantly elevated in the brains of 3xTg-AD mice and AD patients. Conclusions: Overall, our findings suggest that each of the five FAD-linked PS1 mutations has a deleterious effect on mitochondrial functions in a variety of ways. The adverse effects of PS1 mutations on mitochondria may contribute to MAMs formation and oxidative stress resulting in an accelerated age of disease onset in people harboring mutant PS1. |
format | Online Article Text |
id | pubmed-8419044 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-84190442021-09-13 Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function Han, Jihoon Park, Heejin Maharana, Chinmoyee Gwon, A-Ryeong Park, Jinsu Baek, Seung Hyun Bae, Han-Gyu Cho, Yoonsuk Kim, Hark Kyun Sul, Jae Hoon Lee, Jeongmi Kim, Eunae Kim, Junsik Cho, Yongeun Park, Sunyoung Palomera, Leon F. Arumugam, Thiruma V. Mattson, Mark P. Jo, Dong-Gyu Theranostics Research Paper Mitochondrial dysfunction and oxidative stress are frequently observed in the early stages of Alzheimer's disease (AD). Studies have shown that presenilin-1 (PS1), the catalytic subunit of γ-secretase whose mutation is linked to familial AD (FAD), localizes to the mitochondrial membrane and regulates its homeostasis. Thus, we investigated how five PS1 mutations (A431E, E280A, H163R, M146V, and Δexon9) observed in FAD affect mitochondrial functions. Methods: We used H4 glioblastoma cell lines genetically engineered to inducibly express either the wild-type PS1 or one of the five PS1 mutants in order to examine mitochondrial morphology, dynamics, membrane potential, ATP production, mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs), oxidative stress, and bioenergetics. Furthermore, we used brains of PS1M146V knock-in mice, 3xTg-AD mice, and human AD patients in order to investigate the role of PS1 in regulating MAMs formation. Results: Each PS1 mutant exhibited slightly different mitochondrial dysfunction. Δexon9 mutant induced mitochondrial fragmentation while A431E, E280A, H163R, and M146V mutants increased MAMs formation. A431E, E280A, M146V, and Δexon9 mutants also induced mitochondrial ROS production. A431E mutant impaired both complex I and peroxidase activity while M146V mutant only impaired peroxidase activity. All PS1 mutants compromised mitochondrial membrane potential and cellular ATP levels were reduced by A431E, M146V, and Δexon9 mutants. Through comparative profiling of hippocampal gene expression in PS1M146V knock-in mice, we found that PS1M146V upregulates Atlastin 2 (ATL2) expression level, which increases ER-mitochondria contacts. Down-regulation of ATL2 after PS1 mutant induction rescued abnormally elevated ER-mitochondria interactions back to the normal level. Moreover, ATL2 expression levels were significantly elevated in the brains of 3xTg-AD mice and AD patients. Conclusions: Overall, our findings suggest that each of the five FAD-linked PS1 mutations has a deleterious effect on mitochondrial functions in a variety of ways. The adverse effects of PS1 mutations on mitochondria may contribute to MAMs formation and oxidative stress resulting in an accelerated age of disease onset in people harboring mutant PS1. Ivyspring International Publisher 2021-08-17 /pmc/articles/PMC8419044/ /pubmed/34522215 http://dx.doi.org/10.7150/thno.59776 Text en © The author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/). See http://ivyspring.com/terms for full terms and conditions. |
spellingShingle | Research Paper Han, Jihoon Park, Heejin Maharana, Chinmoyee Gwon, A-Ryeong Park, Jinsu Baek, Seung Hyun Bae, Han-Gyu Cho, Yoonsuk Kim, Hark Kyun Sul, Jae Hoon Lee, Jeongmi Kim, Eunae Kim, Junsik Cho, Yongeun Park, Sunyoung Palomera, Leon F. Arumugam, Thiruma V. Mattson, Mark P. Jo, Dong-Gyu Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
title | Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
title_full | Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
title_fullStr | Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
title_full_unstemmed | Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
title_short | Alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
title_sort | alzheimer's disease-causing presenilin-1 mutations have deleterious effects on mitochondrial function |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8419044/ https://www.ncbi.nlm.nih.gov/pubmed/34522215 http://dx.doi.org/10.7150/thno.59776 |
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