Evidence map›Paper›PMID 9736638›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

Central P2X4 and P2X6 channel subunits coassemble into a novel heteromeric ATP receptor.

K T Lê, K Babinski, P Séguéla

Abstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
–field-weighted citation impact
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

84 citing papers in PubMed.

  1. Review
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  8. Article
  9. Article
  10. Review
  11. Review
  12. ATP evokes CaJournal of neurochemistry · 2017
    Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Structural and molecular modeling features of P2X receptors.International journal of molecular sciences · 2014
    Review
  19. Ligand-gated purinergic receptors regulate HIV-1 Tat and morphine related neurotoxicity in primary mouse striatal neuron-glia co-cultures.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2014
    Article
  20. Article

24 more citing papers are in PubMed but not listed here.

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

3 authors.

K T LêCell Biology of Excitable Tissue Group, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada H3A 2B4.
K Babinski
P Séguéla

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ionotropic ATP receptors are widely expressed in mammalian CNS. Despite extensive functional characterization of neuronal homomeric P2X receptors in heterologous expression systems, the subunit composition of native central P2X ATP-gated channels remains to be elucidated. P2X4 and P2X6 are major central subunits with highly overlapping mRNA distribution at both regional and cellular levels. When expressed alone in Xenopus oocytes, P2X6 subunits do not assemble into surface receptors responsive to ATP applications. On the other hand, P2X4 subunits assemble into bona fide ATP-gated channels, slowly desensitizing and weakly sensitive to the partial agonist alpha,beta-methylene ATP and to noncompetitive antagonists suramin and pyridoxal-5-phosphate-6-azophenyl-2',4'-disulfonic acid. We demonstrate here that the coexpression of P2X4 and P2X6 subunits in Xenopus oocytes leads to the generation of a novel pharmacological phenotype of ionotropic ATP receptors. Heteromeric P2X4+6 receptors are activated by low-micromolar alpha, beta-methylene ATP (EC50 = 12 microM) and are blocked by suramin and by Reactive Blue 2, which has the property, at low concentrations, to potentiate homomeric P2X4 receptors. The assembly of P2X4 with P2X6 subunits results from subunit-dependent interactions, as shown by their specific copurification from HEK-293 cells transiently transfected with various epitope-tagged P2X channel subunits. Our data strongly suggest that the numerous cases of neuronal colocalizations of P2X4 and P2X6 subunits observed in mammalian CNS reflect the native expression of heteromeric P2X4+6 channels with unique functional properties.

Indexed as

Adenosine TriphosphateAnimalsAntineoplastic AgentsCationsCells, CulturedElectrophysiologyEnzyme InhibitorsHumansIon Channel GatingKidneyNeuropeptidesOocytesPlatelet Aggregation InhibitorsProtonsPyridoxal PhosphateReceptors, Purinergic P2Adenosine Triphosphatealpha,beta-methyleneadenosine 5'-triphosphateAntineoplastic AgentsCationsCibacron Blue F 3GAEnzyme InhibitorsNeuropeptidesP2RX4 protein, humanPlatelet Aggregation InhibitorsProtonspurinoceptor P2X6Pyridoxal Phosphatepyridoxal phosphate-6-azophenyl-2',4'-disulfonic acidReceptors, Purinergic P2Receptors, Purinergic P2X4SuraminTriazinesZinc

Identifiers

PMID9736638
PMCPMC6793241

What OpenQuestion holds

Textmetadata
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.