Evidence map›Paper›PMID 10944173›Full record

ArticleThe Journal of physiology2000

Leptin activation of ATP-sensitive K+ (KATP) channels in rat CRI-G1 insulinoma cells involves disruption of the actin cytoskeleton.

J Harvey, S C Hardy, A J Irving, M L Ashford

Abstract read
In one paragraph

Article in The Journal of physiology, 2000. 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
–field-weighted citation impact
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.

  1. Ion channels and actin: A tale of two friends.Histology and histopathology · 2025
    Review
  2. Mechanisms and Functions of Sweet Reception in Oral and Extraoral Organs.International journal of molecular sciences · 2024
    Review
  3. Review
  4. Review
  5. Subcellular trafficking and endocytic recycling of KAmerican journal of physiology. Cell physiology · 2022
    Review
  6. Article
  7. Review
  8. Leptin-induced Trafficking of KInternational journal of molecular sciences · 2019
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Human K(ATP) channelopathies: diseases of metabolic homeostasis.Pflugers Archiv : European journal of physiology · 2010
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

J HarveyDepartment of Biomedical Sciences, Institute of Medical Sciences, Aberdeen Centre for Energy Regulation and Obesity, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK.
S C Hardy
A J Irving
M L Ashford

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. The role of the cytoskeleton in leptin-induced activation of ATP-sensitive K+ (KATP) channels was examined in rat CRI-G1 insulin-secreting cells using patch clamp and fluorescence imaging techniques. 2. In whole cell recordings, dialysis with the actin filament stabiliser phalloidin (10 microM) prevented KATP channel activation by leptin. 3. Application of the actin filament destabilising agents deoxyribonuclease type 1 (DNase 1; 50 microg ml-1) or cytochalasin B (10 microM) to intact cells or inside-out membrane patches also increased KATP channel activity in a phalloidin-dependent manner. 4. The anti-microtubule agents nocodazole (10 microM) and colchicine (100 microM) had no effect on KATP channel activity. 5. Fluorescence staining of the cells with rhodamine-conjugated phalloidin revealed rapid disassembly of actin filaments by cytochalasin B and leptin, the latter action being prevented by the phosphoinositide 3 (PI 3)-kinase inhibitor LY 294002. 6. Activation of KATP channels by the PI 3-kinase product phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) was also prevented by phalloidin. This is consistent with the notion that leptin activates KATP channels in these cells by an increase in PtdIns(3,4,5)P3 or a similar 3-phosphorylated phosphoinositol lipid, resulting in actin filament disruption.

Indexed as

ActinsAdenosine TriphosphateAnimalsCell LineCytochalasin BCytoskeletonDeoxyribonuclease IInsulinomaLeptinMicroscopy, FluorescencePatch-Clamp TechniquesPhalloidinePhosphatidylinositol PhosphatesPhosphoinositide-3 Kinase InhibitorsPotassiumPotassium ChannelsActinsAdenosine TriphosphateCytochalasin BDeoxyribonuclease ILeptinPhalloidinephosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol PhosphatesPhosphoinositide-3 Kinase InhibitorsPotassiumPotassium Channels

Identifiers

PMID10944173
PMCPMC2270061

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.