ArticleInternational journal of clinical and experimental pathology2009
Concentration-dependent effects of proteasomal inhibition on tau processing in a cellular model of tauopathy.
Article in International journal of clinical and experimental pathology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- D-peptide-magnetic nanoparticles fragment tau fibrils and rescue behavioral deficits in a mouse model of Alzheimer's disease.Science advances · 2024Article
- Clioquinol Decreases Levels of Phosphorylated, Truncated, and Oligomerized Tau Protein.International journal of molecular sciences · 2021Article
- Autophagy and Tau Protein.International journal of molecular sciences · 2021Review
- Rho-kinase ROCK inhibitors reduce oligomeric tau protein.Neurobiology of aging · 2020Article
- Homocysteine Increases Tau Phosphorylation, Truncation and Oligomerization.International journal of molecular sciences · 2018Article
- The Involvement of NR2B and tau Protein in MG132-Induced CREB Dephosphorylation.Journal of molecular neuroscience : MN · 2017Article
- LRRK2 Promotes Tau Accumulation, Aggregation and Release.Molecular neurobiology · 2016Article
- Cycloheximide Treatment Causes a ZVAD-Sensitive Protease-Dependent Cleavage of Human Tau in Drosophila Cells.Journal of Alzheimer's disease : JAD · 2016Article
- Morphological Changes within the Rat Lateral Ventricle after the Administration of Proteasome Inhibitors.PloS one · 2015Article
- Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.Frontiers in neurology · 2013Review
- Tau phosphorylation affects its axonal transport and degradation.Neurobiology of aging · 2013Article
- Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes.The Journal of biological chemistry · 2012Article
- Proteasome inhibition drives HDAC6-dependent recruitment of tau to aggresomes.Journal of molecular neuroscience : MN · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Tauopathies are characterized by accumulation of filamentous tau aggregates. These aggregates can be recapitulated in transfectant M1C overproducing wild-type human brain tau 4R0N via the tetracycline off (TetOff) inducible expression mechanism. To determine the contribution of proteasomes to tau degradation and aggregation, we exposed M1C cells to epoxomicin (Epx; 2-50 nM) or MG132 (0.5 microM) on the 3(rd) or 4(th) day of a 5-day TetOff induction and demonstrated a reduction of proteasomal activity. Cultures treated with 2 nM Exp showed accumulation of full-length tau without affecting ubiquitin and beta-catenin immunoblotting profiles. In contrast, cells treated with 10, 50 nM Epx or MG132 displayed changes in ubiquitin or beta-catenin immunoblotting profiles and extensive tau degradation/truncation. The increase of tau degradation/truncation was accompanied with accumulation of oligomers and sarkosyl-insoluble aggregates of tau, augmented thioflavin-binding and activation of caspases and calpains. Truncated, oligomeric and sarkosyl-insoluble tau derivatives appeared with caspase-specific cleavage and their production was diminished when pretreated with a pan-caspase inhibitor. The results demonstrate (i) a dose-dependent, opposite effect of proteasome inhibition on tau processing, (ii) the participation of proteasome-dependent, ubiquitination-independent mechanisms in tau degradation and aggregation, and (iii) the promotion of tau aggregation by caspase-mediated tau degradation/truncation.
Indexed as
Identifiers
19636403PMC2713451W1963248720What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.