Evidence map›Paper›PMID 16120774›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005

Regulation of human recombinant P2X3 receptors by ecto-protein kinase C.

Kerstin Wirkner, Doychin Stanchev, Laszlo Köles, Markus Klebingat, Hassan Dihazi, Gesine Flehmig, Catherine Vial, Richard J Evans, Susanna Fürst, Peter P Mager and 2 more

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Overexpressed NaFrontiers in cellular neuroscience · 2021
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. The P2Y2 receptor sensitizes mouse bladder sensory neurons and facilitates purinergic currents.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  12. Article
  13. Article
  14. Interaction of P2 purinergic receptors with cellular macromolecules.Naunyn-Schmiedeberg's archives of pharmacology · 2008
    Review
  15. Article
  16. Article
  17. Neutralization of nerve growth factor induces plasticity of ATP-sensitive P2X3 receptors of nociceptive trigeminal ganglion neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  18. Article
  19. Article
  20. Molecular properties of P2X receptors.Pflugers Archiv : European journal of physiology · 2006
    Review
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

12 authors at 3 institutions in 3 countries.

Kerstin WirknerRudolf-Boehm-Institute of Pharmacology and Toxicology, University of Leipzig, D-04107 Leipzig, Germany.
Doychin Stanchev
Laszlo Köles
Markus Klebingat
Hassan Dihazi
Gesine Flehmig
Catherine Vial
Richard J Evans
Susanna Fürst
Peter P Mager
Klaus Eschrich
Peter Illes
Leipzig University · DESemmelweis University · HUUniversity of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The whole-cell patch-clamp technique was used to record current responses to nucleotides and nucleosides in human embryonic kidney HEK293 cells transfected with the human purinergic P2X3 receptor. When guanosine 5'-O-(3-thiodiphosphate) was included into the pipette solution, UTP at concentrations that did not alter the holding current facilitated the alpha,beta-methylene ATP (alpha,beta-meATP)-induced current. ATP and GTP, but not UDP or uridine, had an effect similar to that of UTP. Compounds known to activate protein kinase C (PKC) acted like the nucleoside triphosphates investigated, whereas various PKC inhibitors invariably reduced the effects of both PKC activators and UTP. The substitution by Ala of Ser/Thr residues situated within PKC consensus sites of the P2X3 receptor ectodomain either abolished (PKC2 and PKC3; T134A, S178A) or did not alter (PKC4 and PKC6; T196A, S269A) the UTP-induced potentiation of the alpha,beta-meATP current. Both the blockade of ecto-protein kinase C activity and the substitution of Thr-134 or Ser-178 by Ala depressed the maximum of the concentration-response curve for alpha,beta-meATP without altering the EC50 values. Molecular simulation of the P2X3 receptor structure indicated no overlap between assumed nucleotide binding domains and the relevant phosphorylation sites PKC2 and PKC3. alpha,beta-meATP-induced currents through native homomeric P2X3 receptors of rat dorsal root ganglia were also facilitated by UTP. In conclusion, it is suggested that low concentrations of endogenous nucleotides in the extracellular space may prime the sensitivity of P2X3 receptors toward the effect of subsequently applied (released) higher agonistic concentrations. The priming effect of nucleotides might be attributable to a phosphorylation of PKC sites at the ectodomain of P2X3 receptors.

Indexed as

AnimalsCell LineCells, CulturedDose-Response Relationship, DrugHumansProtein Kinase CProtein Kinase InhibitorsProtein KinasesPurinergic P2 Receptor AgonistsRatsRats, WistarReceptors, Purinergic P2Receptors, Purinergic P2X3Recombinant ProteinsUridine Triphosphateectoprotein kinaseP2RX3 protein, humanP2rx3 protein, ratProtein Kinase CProtein Kinase InhibitorsProtein KinasesPurinergic P2 Receptor AgonistsReceptors, Purinergic P2Receptors, Purinergic P2X3Recombinant ProteinsUridine Triphosphate

Identifiers

PMID16120774
PMCPMC6725260
OpenAlexW2113466780

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.