Evidence map›Paper›PMID 28516276›Full record

ArticlePurinergic signalling2017

P2X7 receptor-pannexin 1 interaction mediates extracellular alpha-synuclein-induced ATP release in neuroblastoma SH-SY5Y cells.

Anna Wilkaniec, Magdalena Gąssowska, Grzegorz A Czapski, Magdalena Cieślik, Grzegorz Sulkowski, Agata Adamczyk

Open access · hybridAbstract read
In one paragraph

Article in Purinergic signalling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 59 citations in OpenAlex.

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  13. Alpha Synuclein: Neurodegeneration and Inflammation.International journal of molecular sciences · 2023
    Review
  14. The ATP-dependent Pathways and Human Diseases.Current medicinal chemistry · 2023
    Article
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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.

Anna WilkaniecDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences, Pawińskiego 5 St., 02-106, Warsaw, Poland. awilkaniec@imdik.pan.pl.ORCID http://orcid.org/0000-0002-1121-5168
Magdalena GąssowskaDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences, Pawińskiego 5 St., 02-106, Warsaw, Poland.
Grzegorz A CzapskiDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences, Pawińskiego 5 St., 02-106, Warsaw, Poland.
Magdalena CieślikDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences, Pawińskiego 5 St., 02-106, Warsaw, Poland.
Grzegorz SulkowskiDepartment of Neurochemistry, Laboratory of Pathoneurochemistry, Mossakowski Medical Research Centre, Polish Academy of Sciences, Pawińskiego 5 St., 02-106, Warsaw, Poland.
Agata AdamczykDepartment of Cellular Signalling, Mossakowski Medical Research Centre, Polish Academy of Sciences, Pawińskiego 5 St., 02-106, Warsaw, Poland.
Mossakowski Medical Research Institute, Polish Academy of Sciences · PL

Funding

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

Abstract

Abnormalities of alpha-synuclein (ASN), the main component of protein deposits (Lewy bodies), were observed in Parkinson's disease (PD), dementia with Lewy bodies, Alzheimer's disease, and other neurodegenerative disorders. These alterations include increase in the levels of soluble ASN oligomers in the extracellular space. Numerous works have identified several mechanisms of their toxicity, including stimulation of the microglial P2X7 receptor leading to oxidative stress. While the significant role of purinergic signaling-particularly, P2 family receptors-in neurodegenerative disorders is well known, the interaction of extracellular soluble ASN with neuronal purinergic receptors is yet to be studied. Therefore, in this study, we have investigated the effect of ASN on P2 purinergic receptors and ATP-dependent signaling. We used neuroblastoma SH-SY5Y cell line and rat synaptoneurosomes treated with exogenous soluble ASN. The experiments were performed using spectrofluorometric, radiochemical, and immunochemical methods. We found the following: (i) ASN-induced intracellular free calcium mobilization in neuronal cells and nerve endings depends on the activation of purinergic P2X7 receptors; (ii) activation of P2X7 receptors leads to pannexin 1 recruitment to form an active complex responsible for ATP release; and (iii) ASN greatly decreases the activity of extracellular ecto-ATPase responsible for ATP degradation. Thus, it is concluded that purinergic receptors might be putative pharmacological targets in the molecular mechanism of extracellular ASN toxicity. Interference with P2X7 signaling seems to be a promising strategy for the prevention or therapy of PD and other neurodegenerative disorders.

Indexed as

Adenosine Triphosphatealpha-SynucleinAnimalsCalciumCell Line, TumorConnexinsExtracellular SpaceHumansMaleMicrogliaNerve Tissue ProteinsRats, WistarReceptors, Purinergic P2X7Adenosine Triphosphatealpha-SynucleinCalciumConnexinsNerve Tissue ProteinsPANX1 protein, humanReceptors, Purinergic P2X7Alpha-synucleinEcto-ATPaseExtracellular ATPP2X7 receptorPannexin 1Purinergic P2 receptors

Identifiers

PMID28516276
PMCPMC5563296
OpenAlexW2614544395

What OpenQuestion 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 OpenQuestion graph.