TUFM is involved in Alzheimer’s disease-like pathologies that are associated with ROS
Abstract
Mitochondrial Tu translation elongation factor (TUFM or EF-Tu) is part of the mitochondrial translation machinery. It is reported that TUFM expression is reduced in the brain of Alzheimer's disease (AD), suggesting that TUFM might play a role in the pathophysiology. In this study, we found that TUFM protein level was decreased in the hippocampus and cortex especially in the aged APP/PS1 mice, an animal model of AD. In HEK cells that stably express full-length human amyloid-β precursor protein (HEK-APP), TUFM knockdown or overexpression increased or reduced the protein levels of β-amyloid protein (Aβ) and β-amyloid converting enzyme 1 (BACE1), respectively. TUFM-mediated reduction of BACE1 was attenuated by translation inhibitor cycloheximide (CHX) or α-[2-[4-(3,4-Dichlorophenyl)-2-thiazolyl]hydrazinylidene]-2-nitro-benzenepropanoic acid (4EGI1), and in cells overexpressing BACE1 constructs deleting the 5' untranslated region (5'UTR). TUFM silencing increased the half-life of BACE1 mRNA, suggesting that RNA stability was affected by TUFM. In support, transcription inhibitor Actinomycin D (ActD) and silencing of nuclear factor κB (NFκB) failed to abolish TUFM-mediated regulation of BACE1 protein and mRNA. We further found that the mitochondria-targeted antioxidant TEMPO diminished the effects of TUFM on BACE1, suggesting that reactive oxygen species (ROS) played an important role. Indeed, cellular ROS levels were affected by TUFM knockdown or overexpression, and TUFM-mediated regulation of apoptosis and Tau phosphorylation at selective sites was attenuated by TEMPO. Collectively, TUFM protein levels were decreased in APP/PS1 mice. TUFM is involved in AD pathology by regulating BACE1 translation, apoptosis, and Tau phosphorylation, in which ROS plays an important role.
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TUFM can maintain mitochondrial respiratory chain activity and protect cells against oxidative stress.
“Mitochondrial Tu translation elongation factor (TUFM or EF-Tu) can maintain mitochondrial respiratory chain activity and protect cell against OS.”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [130]
TUFM is involved in AD pathology by regulating BACE1 translation, apoptosis, and Tau phosphorylation, in which ROS plays an important role.
“Taken together these results pointed at TUFM involvement in AD pathology by regulating BACE1 translation, apoptosis, and Tau phosphorylation, in which ROS plays an important role [130].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [130]
Cellular ROS levels are affected by TUFM expression, and TUFM-mediated regulation of apoptosis and Tau phosphorylation is counteracted by TEMPO.
“Further, cellular ROS levels were affected by TUFM expression, and TUFM-mediated regulation of apoptosis and Tau phosphorylation is counteracted by the treatment with TEMPO, a potent antioxidant drug.”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [130]
TUFM protein level is decreased in the hippocampus and cortex in aged APP/PS1 mice.
“TUFM protein level is decreased in the hippocampus and cortex in the aged APP/PS1 mice [130].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [130]
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- Authors
- Zhong, B., Zhou, G., Song, L., Wen, Q., Deng, X., Ma, Y., Hu, L., & Chen, G.
- Affiliations
- The Affiliated Yongchuan Hospital of Chongqing Medical University (CN)
- Department of Neurology the First Affiliated Hospital of Chongqing Medical University Chongqing Key Laboratory of Neurology Chongqing China <!--Query ID="q2" Text="AUTHOR: Please check and confirm whether all the author names, affiliations, and correspondence details have been set correctly."-->
- North Sichuan Medical University (CN)
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2021-03-28
- Volume
- 35
- Issue
- 5
- Pages
- e21445-e21445
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W3150421191
- Cited by
- 28
- References
- 63
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 8 · 2023: 6 · 2022: 3 · 2021: 2
- FWCI
- 2.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81971030)
- Chongqing Science and Technology Commission (cstc2018jcyjAX0067)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- TUFM, elongation factor Tu, Alzheimer's disease, mitochondrial translation, BACE1, amyloid-beta, reactive oxygen species, tempo, apoptosis, tau phosphorylation, APP/PS1 mice, RNA stability, 5' untranslated region, NF-κB, cycloheximide, 4EGI-1
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Humans, Mice, Transgenic, Mitochondria, Peptide Elongation Factor Tu, Phosphorylation, Amyloid beta-Protein Precursor, Reactive Oxygen Species, Mice, Presenilin-1, Amyloid Precursor Protein Secretases
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