Evidence map›Paper›PMID 25592660›Full record

ArticlePflugers Archiv : European journal of physiology2015

Homodimeric anoctamin-1, but not homodimeric anoctamin-6, is activated by calcium increases mediated by the P2Y1 and P2X7 receptors.

Michaela Stolz, Manuela Klapperstück, Thomas Kendzierski, Silvia Detro-Dassen, Anna Panning, Günther Schmalzing, Fritz Markwardt

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2015. 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
2.8field-weighted citation impact, top 11% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Purinergic P2X7R as a potential target for pancreatic cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
    Review
  4. Untangling Macropore Formation and Current Facilitation in P2X7.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. The diverse roles of TMEM16A CaJournal of advanced research · 2021
    Review
  9. Article
  10. Article
  11. Dissection of P2X4 and P2X7 Receptor Current Components in BV-2 Microglia.International journal of molecular sciences · 2020
    Article
  12. Article
  13. Article
  14. P2X7 Interactions and Signaling - Making Head or Tail of It.Frontiers in molecular neuroscience · 2019
    Review
  15. Loss-of-function of Nav1.8/D1639N linked to human pain can be rescued by lidocaine.Pflugers Archiv : European journal of physiology · 2018
    Article
  16. Article
  17. Article
  18. Localization of the gate and selectivity filter of the full-length P2X7 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

7 authors at 2 institutions in 1 country.

Michaela StolzMolecular Pharmacology, RWTH Aachen University, Wendlingweg 2, D-52074, Aachen, Germany.
Manuela KlapperstückJulius-Bernstein-Institute for Physiology, Martin-Luther-University Halle-Wittenberg, Magdeburger Str. 6, D-06097, Halle/Saale, Germany.
Thomas KendzierskiJulius-Bernstein-Institute for Physiology, Martin-Luther-University Halle-Wittenberg, Magdeburger Str. 6, D-06097, Halle/Saale, Germany.
Silvia Detro-DassenMolecular Pharmacology, RWTH Aachen University, Wendlingweg 2, D-52074, Aachen, Germany.
Anna PanningMolecular Pharmacology, RWTH Aachen University, Wendlingweg 2, D-52074, Aachen, Germany.
Günther SchmalzingMolecular Pharmacology, RWTH Aachen University, Wendlingweg 2, D-52074, Aachen, Germany.
Fritz MarkwardtJulius-Bernstein-Institute for Physiology, Martin-Luther-University Halle-Wittenberg, Magdeburger Str. 6, D-06097, Halle/Saale, Germany. fritz.markwardt@medizin.uni-halle.de.
RWTH Aachen University · DEMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The P2X7 receptor (P2X7R) is a ligand-gated ion channel that conducts Na(+), K(+), and Ca(2+) when activated by extracellular ATP. In various cell types, such as secretory epithelia, the P2X7R is co-expressed with Ca(2+)-dependent Cl(-) channels of the TMEM16/anoctamin family. Here, we studied whether the P2X7R and TMEM16A/anoctamin-1 (Ano1) or TMEM16F/anoctamin-6 (Ano6) interact functionally and physically, using oocytes of Xenopus laevis and Ambystoma mexicanum (Axolotl) for heterologous expression. As a control, we co-expressed anoctamin-1 with the P2Y1 receptor (P2Y1R), which induces the release of Ca(2+) from intracellular stores via activating phospholipase C through coupling to Gαq. We found that co-expression of anoctamin-1 with the P2Y1R resulted in a small transient increase in Cl(-) conductance in response to ATP. Co-expression of anoctamin-1 with the P2X7R resulted in a large sustained increase in Cl(-) conductance via Ca(2+) influx through the ATP-opened P2X7R in Xenopus and in Axolotl oocytes, which lack endogenous Ca(2+)-dependent Cl(-) channels. P2Y1R- or P2X7R-mediated stimulation of Ano1 was primarily functional, as demonstrated by the absence of a physically stable interaction between Ano1 and the P2X7R. In the pancreatic cell line AsPC-1, we found the same functional Ca(2+)-dependent interaction of P2X7R and Ano1. The P2X7R-mediated sustained activation of Ano1 may be physiologically relevant to the time course of stimulus-secretion coupling in secretory epithelia. No such increase in Cl(-) conductance could be elicited by activating the P2X7 receptor in either Xenopus oocytes or Axolotl oocytes co-expressing Ano6. The lack of function of Ano6 can, at least in part, be explained by its poor cell-surface expression, resulting from a relatively inefficient exit of the homodimeric Ano6 from the endoplasmic reticulum.

Indexed as

Calcium SignalingAction PotentialsAmbystoma mexicanumAnimalsAnoctamin-1AnoctaminsCell Line, TumorChloride ChannelsHumansMicePhospholipid Transfer ProteinsReceptors, Purinergic P2X7Receptors, Purinergic P2Y1XenopusANO1 protein, mouseANO6 protein, mouseAnoctamin-1AnoctaminsChloride ChannelsPhospholipid Transfer ProteinsReceptors, Purinergic P2X7Receptors, Purinergic P2Y1Anoctamin-1Anoctamin-6Intracellular Ca2+P2X7 receptorQuaternary structure

Identifiers

PMID25592660
OpenAlexW2152575235

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.