Evidence map›Paper›PMID 12815176›Full record

ArticleThe Journal of physiology2003

G protein-independent inhibition of GIRK current by adenosine in rat atrial myocytes overexpressing A1 receptors after adenovirus-mediated gene transfer.

Leif I Bösche, Marie-Cécile Wellner-Kienitz, Kirsten Bender, Lutz Pott

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Adenosine A1 receptors (A1Rs) play a critical role in osteoclast formation and function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  4. Article
  5. 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

4 authors at 1 institution in 1 country.

Leif I BöscheDepartment of Physiology, Ruhr-University Bochum, D-4480 Bochum, Germany.
Marie-Cécile Wellner-Kienitz
Kirsten Bender
Lutz Pott
Ruhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-activated inwardly rectifying K+ (GIRK) channels, important regulators of membrane excitability in the heart and central nervous system, are activated by interaction with betagamma subunits from heterotrimeric G proteins upon receptor stimulation. In atrial myocytes various endogenous receptors couple to GIRK channels, including the canonical muscarinic M2 receptor (M2AChR) and the A1 adenosine receptor (A1AdoR). Saturating stimulation of A1AdoR in atrial myocytes activates only a fraction of the GIRK current that is activated via M2AChR, which reflects a lower density of A1AdoR. In the present study A1AdoR were overexpressed by means of adenovirus-mediated gene transfer using green fluorescent protein (GFP) as the reporter. Confirmatory to a previous study, this resulted in an increased sensitivity of macroscopic GIRK current (ACh-activated K+ current (IK(ACh))) to stimulation by Ado. However, in the majority of GFP-positive myocytes, exposure to Ado at concentrations > or =1 microM resulted in activation of IK(ACh) followed by a rapid inhibition. In those cells a rebound activation of current was recorded upon washout of Ado. The inhibitory component could be recorded in isolation when IK(ACh) was activated by M2AChR-stimulation and brief pulses of Ado were superimposed. In myocytes loaded with GTP-gamma-S, IK(ACh), irreversibly activated by brief exposure to agonist, was still reversibly inhibited by Ado, suggesting that inhibition is independent of G protein cycling. In myocytes co-transfected with adenoviral vectors encoding A1AdoR and GIRK4 subunit, no inhibition of GIRK current by Ado was observed. As acute desensitization of atrial GIRK current, which is reminiscent of the inhibition described here, has been shown to be absent in myocytes overexpressing GIRK4, this suggests that acute desensitization and the novel inhibition might share a common pathway whose target is the GIRK channel complex or its GIRK1 subunit.

Indexed as

Potassium Channels, Inwardly RectifyingAcetylcholineAdenosineAdenoviridaeAnimalsDNA PrimersElectrophysiologyGene Transfer TechniquesG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding ProteinsHeart AtriaIn Vitro TechniquesMembrane PotentialsMuscle CellsPatch-Clamp TechniquesPotassium Channel BlockersAcetylcholineAdenosineDNA PrimersG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding ProteinsPotassium Channel BlockersPotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, Purinergic P1

Identifiers

PMID12815176
PMCPMC2343091
OpenAlexW2079615819

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.