Evidence map›Paper›PMID 32486485›Full record

ArticleInternational journal of molecular sciences2020

P2X7 Receptor is Involved in Mitochondrial Dysfunction Induced by Extracellular Alpha Synuclein in Neuroblastoma SH-SY5Y Cells.

Anna Wilkaniec, Magdalena Cieślik, Emilia Murawska, Lidia Babiec, Magdalena Gąssowska-Dobrowolska, Ewelina Pałasz, Henryk Jęśko, Agata Adamczyk

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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 47 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

8 authors at 2 institutions in 1 country.

Anna WilkaniecDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Magdalena CieślikDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Emilia MurawskaDepartment of Applied Microbiology, Institute of Microbiology, Warsaw University, Miecznikowa 1 Street, 02-096 Warsaw, Poland.
Lidia BabiecDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Magdalena Gąssowska-DobrowolskaDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Ewelina PałaszDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Henryk JęśkoDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Agata AdamczykDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences Pawińskiego 5, 02-106 Warsaw, Poland.
Mossakowski Medical Research Institute, Polish Academy of Sciences · PLUniversity of Warsaw · PL

Funding

Narodowe Centrum Nauki 2013/09/D/NZ3/0135
6 · The paper itself

Abstract

The purinergic P2X7 receptor (P2X7R) belongs to a family of trimeric ion channels that are gated by extracellular adenosine 5'-triphosphate (ATP). Several studies have pointed to a role of P2X7R-dependent signalling in Parkinson's disease (PD)-related neurodegeneration. The pathology of (PD) is characterized by the formation of insoluble alpha-synuclein (α-Syn) aggregates-Lewy bodies, but the mechanisms underlying α-Syn-induced dopaminergic cell death are still partially unclear. Our previous studies indicate that extracellular α-Syn directly interact with neuronal P2X7R and induces intracellular free calcium mobilization in neuronal cells. The main objective of this study was to examine the involvement of P2X7R receptor in α-Syn-induced mitochondrial dysfunction and cell death. We found that P2X7R stimulation is responsible for α-Syn-induced oxidative stress and activation of the molecular pathways of programmed cell death. Exogenous α-Syn treatment led to P2X7R-dependent decrease in mitochondrial membrane potential as well as elevation of mitochondrial ROS production resulting in breakdown of cellular energy production. Moreover, P2X7R-dependent deregulation of AMP-activated protein kinase as well as decrease in parkin protein level could be responsible for α-Syn-induced mitophagy impairment and accumulation of dysfunctional mitochondria. P2X7R might be putative pharmacological targets in molecular mechanism of extracellular α-Syn toxicity.

Indexed as

Gene Expression Regulation, NeoplasticAdenosine Triphosphatealpha-SynucleinAMP-Activated Protein KinasesBrain NeoplasmsCell Line, TumorCell SurvivalFree RadicalsHumansMembrane Potential, MitochondrialMitochondriaMitophagyNeuroblastomaNeuronsOxidation-ReductionOxidative StressAdenosine Triphosphatealpha-SynucleinAMP-Activated Protein KinasesFree RadicalsP2RX7 protein, humanReceptors, Purinergic P2X7SNCA protein, humanAMP-activated protein kinasemitochondria dysfunctionP2X7 receptorparkin-synuclein

Identifiers

PMID32486485
PMCPMC7312811
OpenAlexW3030398152

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Registered trials

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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.