Evidence map›Paper›PMID 17704905›Full record

ArticleDiabetologia2007

An adenylate kinase is involved in KATP channel regulation of mouse pancreatic beta cells.

D U Schulze, M Düfer, B Wieringa, P Krippeit-Drews, G Drews

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Diabetologia, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. The role of the adenylate kinase 5 gene in various diseases and cancer.Journal of clinical and translational science · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Oxidative stress and beta-cell dysfunction.Pflugers Archiv : European journal of physiology · 2010
    Review
  10. K(ATP) channelopathies in the pancreas.Pflugers Archiv : European journal of physiology · 2010
    Review
  11. Review
  12. Article
  13. Article
  14. Neonatal diabetes mellitus.Endocrine reviews · 2008
    Review
  15. Cytosolic adenylate kinases regulate K-ATP channel activity in human beta-cells.Biochemical and biophysical research communications · 2008
    Article
  16. 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

5 authors at 2 institutions in 2 countries.

D U SchulzeInstitute of Pharmacy, Department of Pharmacology, University of Tübingen, Auf der Morgenstelle 8, 72076, Tübingen, Germany.
M Düfer
B Wieringa
P Krippeit-Drews
G Drews
University of Tübingen · DERadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aims/hypothesisIn a previous study, we demonstrated that a creatine kinase (CK) modulates K(ATP) channel activity in pancreatic beta cells. To explore phosphotransfer signalling pathways in more detail, we examined whether K(ATP) channel regulation in beta cells is determined by a metabolic interaction between adenylate kinase (AK) and CK.

methodsSingle channel activity was measured with the patch-clamp technique in the inside-out (i/o) and open-cell attached (oca) configuration.

resultsThe ATP sensitivity of K(ATP) channels was higher in i/o patches than in permeabilised beta cells (oca). One reason for this observation could be that the local ATP:ADP ratio in the proximity of the channels is determined by factors not active in i/o patches. AMP (0.1 mmol/l) clearly increased open channel probability in the presence of ATP (0.125 mmol/l) in permeabilised cells but not in excised patches. This suggests that AK-catalysed ADP production in the vicinity of the channels is involved in K(ATP) channel regulation. The observation that the stimulatory effect of AMP on K(ATP) channels was prevented by the AK inhibitor P (1),P (5)-di(adenosine-5')pentaphosphate (Ap(5)A; 20 micromol/l) and abolished in the presence of the non-metabolisable ATP analogue adenosine 5'-(beta,gamma-imido)triphosphate tetralithium salt (AMP-PNP; 0.12 mmol/l) strengthens this idea. In beta cells from AK1 knockout mice, the effect of AMP was less pronounced, though not completely suppressed. The increase in K(ATP) channel activity induced by AMP in the presence of ATP was outweighed by phosphocreatine (1 mmol/l). We suggest that this is due to an elevation of the ATP concentration by CK. CONCLUSIONS/

interpretationWe propose that phosphotransfer events mediated by AK and CK play an important role in determining the effective concentrations of ATP and ADP in the microenvironment of pancreatic beta cell K(ATP) channels. Thus, these enzymes determine the open probability of K(ATP) channels and eventually the actual rate of insulin secretion.

Indexed as

Adenosine MonophosphateAdenosine TriphosphateAdenylate KinaseAnimalsElectrophysiologyInsulin-Secreting CellsKATP ChannelsMaleMiceMice, Inbred C57BLModels, BiologicalPatch-Clamp TechniquesAdenosine MonophosphateAdenosine TriphosphateAdenylate KinaseKATP Channels

Identifiers

PMID17704905
OpenAlexW1965420509

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.