Evidence map›Paper›PMID 10864944›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000

Coexpression of rat P2X2 and P2X6 subunits in Xenopus oocytes.

B F King, A Townsend-Nicholson, S S Wildman, T Thomas, K M Spyer, G Burnstock

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

49 citing papers in PubMed, 155 citations in OpenAlex.

  1. Review
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  5. Review
  6. Article
  7. Article
  8. Review
  9. Structural and molecular modeling features of P2X receptors.International journal of molecular sciences · 2014
    Review
  10. Article
  11. Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014
    Review
  12. Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
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 2 institutions in 1 country.

B F KingAutonomic Neuroscience Institute, Royal Free and University College Medical School, Royal Free Campus, Hampstead, London NW3 2PF, United Kingdom. b.king@ucl.ac.uk
A Townsend-Nicholson
S S Wildman
T Thomas
K M Spyer
G Burnstock
The Royal Free Hospital · GBUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcripts for P2X(2) and P2X(6) subunits are present in rat CNS and frequently colocalize in the same brainstem nuclei. When rat P2X(2) (rP2X(2)) and rat P2X(6) (rP2X(6)) receptors were expressed individually in Xenopus oocytes and studied under voltage-clamp conditions, only homomeric rP2X(2) receptors were fully functional and gave rise to large inward currents (2-3 microA) to extracellular ATP. Coexpression of rP2X(2) and rP2X(6) subunits in Xenopus oocytes resulted in a heteromeric rP2X(2/6) receptor, which showed a significantly different phenotype from the wild-type rP2X(2) receptor. Differences included reduction in agonist potencies and, in some cases (e.g., Ap(4)A), significant loss of agonist activity. ATP-evoked inward currents were biphasic at the heteromeric rP2X(2/6) receptor, particularly when Zn(2+) ions were present or extracellular pH was lowered. The pH range was narrower for H(+) enhancement of ATP responses at the heteromeric rP2X(2/6) receptor. Also, H(+) ions inhibited ATP responses at low pH levels (<pH 6.3). The pH-dependent blocking activity of suramin was changed at this heteromeric receptor, although the potentiating effect of Zn(2+) on ATP responses was unchanged. Thus, the rP2X(2/6) receptor is a functionally modified P2X(2)-like receptor with a distinct pattern of pH modulation of ATP activation and suramin blockade. Although homomeric P2X(6) receptors function poorly, the P2X(6) subunit can contribute to functional heteromeric P2X channels and may influence the phenotype of native P2X receptors in those cells in which it is expressed.

Indexed as

Adenosine TriphosphateAnimalsBrain StemFemaleHydrogen-Ion ConcentrationMembrane PotentialsOocytesRatsReceptors, Purinergic P2Receptors, Purinergic P2X2Recombinant ProteinsSuraminTranscription, GeneticXenopus laevisAdenosine TriphosphateP2rx2 protein, ratpurinoceptor P2X6Receptors, Purinergic P2Receptors, Purinergic P2X2Recombinant ProteinsSuramin

Identifiers

PMID10864944
PMCPMC6772291
OpenAlexW1546894681

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.