Evidence map›Paper›PMID 24213304›Full record

ArticleIslets

Leptin-stimulated KATP channel trafficking: a new paradigm for β-cell stimulus-secretion coupling?

George G Holz, Oleg G Chepurny, Colin A Leech

Open access · hybridAbstract readComment
In one paragraph

Article in Islets. 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
1.2field-weighted citation impact, top 20% 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, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. The endocrinology of the brain.Endocrine connections · 2018
    Review
  4. Regulation of KDiabetes · 2018
    Article
  5. Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

George G HolzDepartment of Medicine; State University of New York (SUNY); Upstate Medical University; Syracuse, NY USA; Department of Pharmacology; State University of New York (SUNY); Upstate Medical University; Syracuse, NY USA.
Oleg G ChepurnyDepartment of Medicine; State University of New York (SUNY); Upstate Medical University; Syracuse, NY USA.
Colin A LeechDepartment of Medicine; State University of New York (SUNY); Upstate Medical University; Syracuse, NY USA.
State University of New York · USSUNY Upstate Medical University · USSyracuse University · US

Funding

Molecular Basis of Antidiabetogenic Hormone ActionR01DK069575 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI HOLZ, GEORGE G · 2007 to 2017
$2.9M
NIDDK NIH HHS R01 DK069575
6 · The paper itself

Abstract

Insulin secretion from pancreatic β-cells is initiated by the closure of ATP-sensitive K+ channels (KATP) in response to high concentrations of glucose, and this action of glucose is counteracted by the hormone leptin, an adipokine that signals through the Ob-Rb receptor to increase KATP channel activity. Despite intensive investigations, the molecular basis for KATP channel regulation remains uncertain, particularly from the standpoint of whether fluctuations in plasma membrane KATP channel content underlie alterations of KATP channel activity in response to glucose or leptin. Surprisingly, newly published findings reveal that leptin stimulates AMP-activated protein kinase (AMPK) in order to promote trafficking of KATP channels from cytosolic vesicles to the plasma membrane of β-cells. This action of leptin is mimicked by low concentrations of glucose that also activate AMPK and that inhibit insulin secretion. Thus, a new paradigm for β-cell stimulus-secretion coupling is suggested in which leptin exerts a tonic inhibitory effect on β-cell excitability by virtue of its ability to increase plasma membrane KATP channel density and whole-cell KATP channel current. One important issue that remains unresolved is whether high concentrations of glucose suppress AMPK activity in order to shift the balance of membrane cycling so that KATP channel endocytosis predominates over vesicular KATP channel insertion into the plasma membrane. If so, high concentrations of glucose might transiently reduce KATP channel density/current, thereby favoring β-cell depolarization and insulin secretion. Such an AMPK-dependent action of glucose would complement its established ability to generate an increase of ATP/ADP concentration ratio that directly closes KATP channels in the plasma membrane.

Indexed as

AMP-Activated Protein KinasesAnimalsInsulin-Secreting CellsLeptinMembrane PotentialsSignal TransductionSodium-Potassium-Exchanging ATPaseAMP-Activated Protein KinasesLeptinSodium-Potassium-Exchanging ATPaseAMPKF-actinglucoseion channel translocationKATP channelleptin

Identifiers

PMID24213304
PMCPMC4010576
OpenAlexW2064814537

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.