Evidence map›Paper›PMID 17052768›Full record

ArticleBiochimica et biophysica acta2007

Protein kinase C regulation of P2X3 receptors is unlikely to involve direct receptor phosphorylation.

David A Brown, David I Yule

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Regulation of P2X1 receptors by modulators of the cAMP effectors PKA and EPAC.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  2. Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Biochemical and biophysical research communications · 2020
    Article
  3. Article
  4. Article
  5. CBNeurochemical research · 2018
    Article
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  7. Article
  8. Review
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  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Interaction of P2 purinergic receptors with cellular macromolecules.Naunyn-Schmiedeberg's archives of pharmacology · 2008
    Review
  17. Article
  18. Article
  19. 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
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

2 authors.

David A BrownDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester Medical Center, 601 Elmwood Avenue, Rochester, NY 14642, USA.
David I Yule

Funding

[Ca2+]i and Secretory Dynamics in Parotid Acinar CellsR01DE014756 · NIDCR · UNIVERSITY OF ROCHESTER · PI David I Yule · 2002 to 2026
$9.9M
TRAINING PROGRAM IN ORAL SCIENCET32DE007202 · NIDCR · UNIVERSITY OF ROCHESTER · PI QUIVEY, ROBERT G · 1990 to 2010
$5.5M
PANCREATIC SECRETION--G PROTEIN MEDIATED CA++ SIGNALINGR01DK054568 · NIDDK · UNIVERSITY OF ROCHESTER · PI YULE, DAVID I · 1998 to 2012
$3.1M
NIDCR NIH HHS R01 DE014756NIDCR NIH HHS R01-DE014756NIDCR NIH HHS T32 DE007202NIDCR NIH HHS T32-DE07202NIDDK NIH HHS R01 DK054568NIDDK NIH HHS R01-DK-054568
6 · The paper itself

Abstract

P2X receptors (P2XR) act as ligand-gated, cation-selective ion channels. A common characteristic of all seven P2X family members is a conserved consensus sequence for protein kinase C (PKC)-mediated phosphorylation in the intracellular N-terminus of the receptor. Activation of PKC has been shown to enhance currents through P2X(3)R, however the molecular mechanism of this potentiation has not been elucidated. In the present study we show that activation of PKC can enhance adenosine triphosphate (ATP)-mediated Ca(2+) signals approximately 2.5-fold in a DT-40 3KO cell culture system (P2 receptor null) transiently overexpressing P2X(3)R. ATP-activated cation currents were also directly studied using whole cell patch clamp techniques in HEK-293 cells, a null background for ionotropic P2XR. PKC activation resulted in a approximately 8.5-fold enhancement of ATP-activated current in HEK-293 cells transfected with P2X(3)R cDNA, but had no effect on currents through either P2X(4)R- or P2X(7)R-transfected cells. P2X(3)R-transfected HEK-293 cells were metabolically labeled with (32)PO(4)(-) and following treatment with phorbol-12-myristate-13-acetate (PMA) and subsequent immunoprecipitation, there was no incorporation of (32)PO(4)(-) in bands corresponding to P2X(3)R. Similarly, in vitro phosphorylation experiments, utilizing purified PKC catalytic subunits failed to establish phosphorylation of either P2X(3)R or P2X(3)R-EGFP. These data indicate that PKC activation can enhance both the Ca(2+) signal as well as the cation current through P2X(3)R, however it appears that the regulation is unlikely to be a result of direct phosphorylation of the receptor.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsCalcium SignalingChickensEnzyme ActivationHumansImmunoblottingImmunoprecipitationInositol 1,4,5-Trisphosphate ReceptorsIon Channel GatingMolecular Sequence DataPhosphorylationProtein Kinase CRatsReceptors, Purinergic P2Adenosine TriphosphateInositol 1,4,5-Trisphosphate ReceptorsP2RX3 protein, humanP2RX4 protein, humanP2RX7 protein, humanProtein Kinase CReceptors, Purinergic P2Receptors, Purinergic P2X3Receptors, Purinergic P2X4Receptors, Purinergic P2X7Tetradecanoylphorbol Acetate

Identifiers

PMID17052768
PMCPMC1861828

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.