Evidence map›Paper›PMID 32977471›Full record

ArticleInternational journal of molecular sciences2020

Inorganic Phosphate (Pi) Signaling in Endothelial Cells: A Molecular Basis for Generation of Endothelial Microvesicles in Uraemic Cardiovascular Disease.

Nima Abbasian, Alan Bevington, James O Burton, Karl E Herbert, Alison H Goodall, Nigel J Brunskill

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 11 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Nima AbbasianDepartment of Cardiovascular Sciences, University of Leicester, and Leicester NIHR Cardiovascular Biomedical Research Unit, Leicester LE3 9QP, UK.ORCID 0000-0002-6906-2563
Alan BevingtonDepartment of Cardiovascular Sciences, University of Leicester, and Leicester NIHR Cardiovascular Biomedical Research Unit, Leicester LE3 9QP, UK.
James O BurtonDepartment of Cardiovascular Sciences, University of Leicester, and Leicester NIHR Cardiovascular Biomedical Research Unit, Leicester LE3 9QP, UK.ORCID 0000-0003-1176-7592
Karl E HerbertDepartment of Cardiovascular Sciences, University of Leicester, and Leicester NIHR Cardiovascular Biomedical Research Unit, Leicester LE3 9QP, UK.
Alison H GoodallDepartment of Cardiovascular Sciences, University of Leicester, and Leicester NIHR Cardiovascular Biomedical Research Unit, Leicester LE3 9QP, UK.
Nigel J BrunskillDepartment of Cardiovascular Sciences, University of Leicester, and Leicester NIHR Cardiovascular Biomedical Research Unit, Leicester LE3 9QP, UK.
University of Leicester · GB

Funding

Kidney Research UK RP30/July 2014
6 · The paper itself

Abstract

Hyperphosphataemia increases cardiovascular mortality in patients with kidney disease. Direct effects of high inorganic phosphate (Pi) concentrations have previously been demonstrated on endothelial cells (ECs), including generation of procoagulant endothelial microvesicles (MVs). However, no mechanism directly sensing elevated intracellular Pi has ever been described in mammalian cells. Here, we investigated the hypothesis that direct inhibition by Pi of the phosphoprotein phosphatase PP2A fulfils this sensing role in ECs, culminating in cytoskeleton disruption and MV generation. ECs were treated with control (1 mM [Pi]) vs. high (2.5 mM [Pi]), a condition that drives actin stress fibre depletion and MV generation demonstrated by confocal microscopy of F-actin and NanoSight Nanoparticle tracking, respectively. Immuno-blotting demonstrated that high Pi increased p-Src, p-PP2A-C and p-DAPK-1 and decreased p-TPM-3. Pi at 100 μM directly inhibited PP2A catalytic activity. Inhibition of PP2A enhanced inhibitory phosphorylation of DAPK-1, leading to hypophosphorylation of Tropomyosin-3 at S284 and MV generation. p-Src is known to perform inhibitory phosphorylation on DAPK-1 but also on PP2A-C. However, PP2A-C can itself dephosphorylate (and therefore inhibit) p-Src. The direct inhibition of PP2A-C by Pi is, therefore, amplified by the feedback loop between PP2A-C and p-Src, resulting in further PP2A-C inhibition. These data demonstrated that PP2A/Src acts as a potent sensor and amplifier of Pi signals which can further signal through DAPK-1/Tropomyosin-3 to generate cytoskeleton disruption and generation of potentially pathological MVs.

Indexed as

Signal TransductionActin CytoskeletonCardiovascular DiseasesCell-Derived MicroparticlesCell Line, TransformedCytoskeletal ProteinsEndothelial CellsHumansHyperphosphatemiaPhosphatesProtein Phosphatase 2Cytoskeletal ProteinsPhosphatesProtein Phosphatase 2DAPK-1inorganic phosphatemicrovesiclesPP2AsignalingSrctropomyosin

Identifiers

PMID32977471
PMCPMC7583816
OpenAlexW3088739391

What Socratic holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.