ArticleCell stress & chaperones2015
Evidence against a role of P-glycoprotein in the clearance of the Alzheimer's disease Aβ1-42 peptides.
Article in Cell stress & chaperones, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
5 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- New Evidence for P-gp-Mediated Export of Amyloid-β PEPTIDES in Molecular, Blood-Brain Barrier and Neuronal Models.International journal of molecular sciences · 2020Article
- Mamma Mia, P-glycoprotein binds again.FEBS letters · 2020Review
- Elimination of substances from the brain parenchyma: efflux via perivascular pathways and via the blood-brain barrier.Fluids and barriers of the CNS · 2018Review
- Cellular Models and In Vitro Assays for the Screening of modulators of P-gp, MRP1 and BCRP.Molecules (Basel, Switzerland) · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been proposed that the amyloid-β peptides (Aβ) cause the neuronal degeneration in the Alzheimer's disease brain. An imbalance between peptide production at the neuronal level and their elimination across the blood-brain-barrier (BBB) results in peptide accumulation inside the brain. The identification and functional characterization of the transport systems in the BBB with the capacity to transport Aβ is crucial for the understanding of Aβ peptide traffic from the brain to the blood. In this context, it has been suggested that the P-glycoprotein (P-gp), expressed in endothelial cells of the BBB, plays a role in the elimination of Aβ. However, there is little, if any, experimental evidence to support this; therefore, the aim of this investigation was to determine whether P-gp is capable of transporting Aβ peptides. Our results show that ATPase activity measured in plasma membrane vesicles of K562 cells overexpressing P-gp is not increased by the presence of Aβ42, suggesting that Aβ42 is not a P-gp substrate. Similarly, P-gp of pirarubicin was unaffected by Aβ42. Moreover, the overexpression of P-gp does not protect cells against Aβ42 toxicity. Taken together, our results support the conclusion that Aβ42 is not transported by P-gp.
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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.