Evidence map›Paper›PMID 15024061›Full record

ArticleMolecular and cellular biology2004

ATP-sensitive K(+) channels regulate the concentrative adenosine transporter CNT2 following activation by A(1) adenosine receptors.

Sylvie Duflot, Bárbara Riera, Sonia Fernández-Veledo, Vicent Casadó, Robert I Norman, F Javier Casado, Carme Lluís, Rafael Franco, Marçal Pastor-Anglada

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Who Is Who in Adenosine Transport.Frontiers in pharmacology · 2018
    Review
  6. Emerging Roles of Nucleoside Transporters.Frontiers in pharmacology · 2018
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Opioid receptor-independent protection of ischemic rat hepatocytes by morphine.Biochemical and biophysical research communications · 2006
    Article
  15. 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

9 authors at 2 institutions in 2 countries.

Sylvie DuflotDepartament de Bioquímica i Biologia Molecular, Universitat de Barcelona, E-08071 Barcelona, Spain.
Bárbara Riera
Sonia Fernández-Veledo
Vicent Casadó
Robert I Norman
F Javier Casado
Carme Lluís
Rafael Franco
Marçal Pastor-Anglada
Universitat de Barcelona · ESUniversity of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study describes a novel mechanism of regulation of the high-affinity Na(+)-dependent adenosine transporter (CNT2) via the activation of A(1) adenosine receptors (A(1)R). This regulation is mediated by the activation of ATP-sensitive K(+) (K(ATP)) channels. The high-affinity Na(+)-dependent adenosine transporter CNT2 and A(1)R are coexpressed in the basolateral domain of the rat hepatocyte plasma membrane and are colocalized in the rat hepatoma cell line FAO. The transient increase in CNT2-mediated transport activity triggered by (-)-N(6)-(2-phenylisopropyl)adenosine is fully inhibited by K(ATP) channel blockers and mimicked by a K(ATP) channel opener. A(1)R agonist activation of CNT2 occurs in both hepatocytes and FAO cells, which express Kir6.1, Kir6.2, SUR1, SUR2A, and SUR2B mRNA channel subunits. With the available antibodies against Kir6.X, SUR2A, and SUR2B, it is shown that all of these proteins colocalize with CNT2 and A(1)R in defined plasma membrane domains of FAO cells. The extent of the purinergic modulation of CNT2 is affected by the glucose concentration, a finding which indicates that glycemia and glucose metabolism may affect this cross-regulation among A(1)R, CNT2, and K(ATP) channels. These results also suggest that the activation of K(ATP) channels under metabolic stress can be mediated by the activation of A(1)R. Cell protection under these circumstances may be achieved by potentiation of the uptake of adenosine and its further metabolization to ATP. Mediation of purinergic responses and a connection between the intracellular energy status and the need for an exogenous adenosine supply are novel roles for K(ATP) channels.

Indexed as

AdenosineAnimalsCarcinoma, HepatocellularCell Line, TumorCell MembraneGlucoseHepatocytesLiver NeoplasmsMaleMembrane Transport ProteinsPotassium Channel BlockersPotassium Channels, Inwardly RectifyingProtein IsoformsProtein SubunitsPurine NucleosidesRatsAdenosinecif nucleoside transporterGlucoseMembrane Transport ProteinsN-(1-methyl-2-phenylethyl)adenosinePotassium Channel BlockersPotassium Channels, Inwardly RectifyingProtein IsoformsProtein SubunitsPurine NucleosidesReceptor, Adenosine A1

Identifiers

PMID15024061
PMCPMC371120
OpenAlexW2140006576

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.