Convergence of amyloid-beta and tau pathologies on mitochondria in vivo
Eckert A, Schulz KL, Rhein V, Götz J.. Molecular neurobiology, 2010-03-09
Topic: Brain proteins, microglia and lab models
Plain-language summary
The histopathological characteristics of Alzheimer's disease (AD) are amyloid-beta (Abeta) containing plaques and neurofibrillary tangles (NFTs) as well as neuronal and synaptic loss. Until today, the underlying mechanisms of the interplay of plaques and tangles remained unresolved. There is increasing evidence that mitochondrial dysfunction might be a possible link, as revealed by studies in several APP and tau transgenic mouse models. Recently, we examined mitochondrial function in a novel triple transgenic mouse model (pR5/APP/PS2)--(triple)AD mice--that combines both pathologic features of the disease in brain. Using comparative, quantitative proteomics (iTRAQ) and mass spectroscopy, we found a massive deregulation of 24 proteins, of which one third were mitochondrial proteins mainly related to complexes I and IV of the oxidative phosphorylation system (OXPHOS). Remarkably, deregulation of complex I was related to tau, whereas deregulation of complex IV was Abeta dependent, both at the protein and activity levels. The (triple)AD mice showed synergistic effects of Abeta and tau already at the age of 8 months, resulting in a depolarized mitochondrial membrane potential. At 12 months, the strongest defects on OXPHOS, synthesis of ATP and reactive oxygen species, were exhibited in the (triple)AD mice, again emphasizing synergistic, age-associated effects of Abeta and tau in impairing mitochondria. This review highlights the convergence of Abeta and tau on mitochondria and establishes a molecular link in AD pathology in vivo.
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APA 7th
Eckert, A., Schulz, K. L., Rhein, V., & Götz, J. (2010). Convergence of amyloid-beta and tau pathologies on mitochondria in vivo. Molecular neurobiology. https://doi.org/10.1007/s12035-010-8109-5
Vancouver
Eckert A, Schulz KL, Rhein V, Götz J. Convergence of amyloid-beta and tau pathologies on mitochondria in vivo. Molecular neurobiology. 2010. doi:10.1007/s12035-010-8109-5. PMID: 20217279.
BibTeX
@article{eckert2010-20217279,
author = {Eckert, A. and Schulz, K. L. and Rhein, V. and Götz, J.},
title = {{Convergence of amyloid-beta and tau pathologies on mitochondria in vivo}},
journal = {Molecular neurobiology},
year = {2010},
doi = {10.1007/s12035-010-8109-5},
pmid = {20217279},
url = {https://doi.org/10.1007/s12035-010-8109-5}
}
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Key findings
- There is increasing evidence that mitochondrial dysfunction might be a possible link, as revealed by studies in several APP and tau transgenic mouse models.
- Using comparative, quantitative proteomics (iTRAQ) and mass spectroscopy, we found a massive deregulation of 24 proteins, of which one third were mitochondrial proteins mainly related to complexes I and IV of the oxidative phosphorylation system (OXPHOS).
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Study details
- Evidence strengthLow
How this study scored 40/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / blinded because the record does not state it. We have no data on journal's citation record, times cited, citations per year, impact for its field and year, cited by studies here, still being cited, senior author's track record, institution's track record and multicenter collaboration, so those were left out: it earned 23 of the 58 points we could judge it on, which is 40 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Molecular neurobiology) |
| Journal's citation record | — / 4 | No journal record from OpenAlex — left out of this score |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2010 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | — / 7 | No citation count (not found in OpenAlex) — left out of this score |
| Citations per year | — / 5 | No citation count or no year — left out of this score |
| Impact for its field and year | — / 6 | No field-weighted citation impact (OpenAlex has none yet) — left out of this score |
| Cited by studies here | — / 6 | Not yet checked against this library's citation graph — left out of this score |
| Still being cited | — / 4 | No yearly citation counts — left out of this score |
| Senior author's track record | — / 4 | Senior author's record not available — left out of this score |
| Institution's track record | — / 3 | No institution listed in OpenAlex — left out of this score |
| Multicenter collaboration | — / 3 | Institutions not listed — left out of this score |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 20217279) |
| Free to read | 2 / 2 | Free to read |
| Points | 23 / 58 | Scored on 11 of 20 parts. We have no data for the rest, so they are left out: 23 of the 58 points we could judge it on is 40 out of 100. |
| Total | 40 / 100 | — |
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