Evidence map›Paper›PMID 15218066›Full record

ArticleThe Journal of physiology2004

Zinc is both an intracellular and extracellular regulator of KATP channel function.

Anne-Lise Prost, Alain Bloc, Nicolas Hussy, Renaud Derand, Michel Vivaudou

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.9field-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

32 citing papers in PubMed, 65 citations in OpenAlex.

  1. Zinc homeostasis and redox alterations in obesity.Frontiers in endocrinology · 2023
    Review
  2. Article
  3. Article
  4. Review
  5. Zinc and its regulators in pancreas.Inflammopharmacology · 2019
    Review
  6. Increased free ZnJournal of cellular and molecular medicine · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. The Critical Roles of Zinc: Beyond Impact on Myocardial Signaling.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2015
    Review
  14. Review
  15. Review
  16. Article
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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

5 authors at 3 institutions in 2 countries.

Anne-Lise ProstBiophysique Moléculaire & Cellulaire, CNRS UMR5090, CEA/DRDC, 17 rue des Martyrs, 38054 Grenoble, France.
Alain Bloc
Nicolas Hussy
Renaud Derand
Michel Vivaudou
Centre National de la Recherche Scientifique · FRCEA Grenoble · FRUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular Zn(2+) has been identified as an activator of pancreatic K(ATP) channels. We further examined the action of Zn(2+) on recombinant K(ATP) channels formed with the inward rectifier K(+) channel subunit Kir6.2 associated with either the pancreatic/neuronal sulphonylurea receptor 1 (SUR1) subunit or the cardiac SUR2A subunit. Zn(2+), applied at either the extracellular or intracellular side of the membrane appeared as a potent, reversible activator of K(ATP) channels. External Zn(2+), at micromolar concentrations, activated SUR1/Kir6.2 but induced a small inhibition of SUR2A/Kir6.2 channels. Cytosolic Zn(2+) dose-dependently stimulated both SUR1/Kir6.2 and SUR2A/Kir6.2 channels, with half-maximal effects at 1.8 and 60 microm, respectively, but it did not affect the Kir6.2 subunit expressed alone. These observations point to an action of both external and internal Zn(2+) on the SUR subunit. Effects of internal Zn(2+) were not due to Zn(2+) leaking out, since they were unaffected by the presence of a Zn(2+) chelator on the external side. Similarly, internal chelators did not affect activation by external Zn(2+). Therefore, Zn(2+) is an endogenous K(ATP) channel opener being active on both sides of the membrane, with potentially distinct sites of action located on the SUR subunit. These findings uncover a novel regulatory pathway targeting K(ATP) channels, and suggest a new role for Zn(2+) as an intracellular signalling molecule.

Indexed as

Adenosine TriphosphateAnimalsChlorocebus aethiopsCOS CellsCricetinaeExtracellular FluidFemaleIntracellular FluidKcnj11 ChannelMiceOocytesPotassium Channels, Inwardly RectifyingProtein SubunitsRatsXenopus laevisZincAdenosine TriphosphateKcnj11 ChannelPotassium Channels, Inwardly RectifyingProtein SubunitsZinc

Identifiers

PMID15218066
PMCPMC1665068
OpenAlexW1536892476

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.