Evidence map›Paper›PMID 18723823›Full record

ArticleMolecular pharmacology2008

Coassembly of different sulfonylurea receptor subtypes extends the phenotypic diversity of ATP-sensitive potassium (KATP) channels.

Adam Wheeler, Chuan Wang, Ke Yang, Kun Fang, Kevin Davis, Amanda M Styer, Uyenlinh Mirshahi, Christophe Moreau, Jean Revilloud, Michel Vivaudou and 3 more

Open access · greenAbstract read
In one paragraph

Article in Molecular pharmacology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Trial
  2. Article
  3. Targeting ATP-Sensitive KAmerican journal of respiratory cell and molecular biology · 2022
    Article
  4. Article
  5. Pulmonary Hypertension and ATP-Sensitive Potassium Channels.Hypertension (Dallas, Tex. : 1979) · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Da-bu-yin-wan and qian-zheng-san to neuroprotect the mouse model of Parkinson's disease.Evidence-based complementary and alternative medicine : eCAM · 2014
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

13 authors at 2 institutions in 1 country.

Adam WheelerDepartment of Physiology and Biophysics, Case Western Reserve University, School of Medicine, Cleveland, Ohio, USA.
Chuan Wang
Ke Yang
Kun Fang
Kevin Davis
Amanda M Styer
Uyenlinh Mirshahi
Christophe Moreau
Jean Revilloud
Michel Vivaudou
Shunhe Liu
Tooraj Mirshahi
Kim W Chan
Case Western Reserve University · USUniversity School · US

Funding

SUR Transmembrane Domain in K(ATP) Channel FunctionR01DK060104 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI HARVEY, ROBERT D · 2002 to 2006
$1.2M
Intramural NIH HHS Z01 DK060104NIDDK NIH HHS DK60104NIDDK NIH HHS R01 DK060104
6 · The paper itself

Abstract

K(ATP) channels are metabolic sensors and targets of potassium channel openers (KCO; e.g., diazoxide and pinacidil). They comprise four sulfonylurea receptors (SUR) and four potassium channel subunits (Kir6) and are critical in regulating insulin secretion. Different SUR subtypes (SUR1, SUR2A, SUR2B) largely determine the metabolic sensitivities and the pharmacological profiles of K(ATP) channels. SUR1- but not SUR2-containing channels are highly sensitive to metabolic inhibition and diazoxide, whereas SUR2 channels are sensitive to pinacidil. It is generally believed that SUR1 and SUR2 are incompatible in channel coassembly. We used triple tandems, T1 and T2, each containing one SUR (SUR1 or SUR2A) and two Kir6.2Delta26 (last 26 residues are deleted) to examine the coassembly of different SUR. When T1 or T2 was expressed in Xenopus laevis oocytes, small whole-cell currents were activated by metabolic inhibition (induced by azide) plus a KCO (diazoxide for T1, pinacidil for T2). When coexpressed with any SUR subtype, the activated-currents were increased by 2- to 13-fold, indicating that different SUR can coassemble. Consistent with this, heteromeric SUR1+SUR2A channels were sensitive to azide, diazoxide, and pinacidil, and their single-channel burst duration was 2-fold longer than that of the T1 channels. Furthermore, SUR2A was coprecipitated with SUR1. Using whole-cell recording and immunostaining, heteromeric channels could also be detected when T1 and SUR2A were coexpressed in mammalian cells. Finally, the response of the SUR1+SUR2A channels to azide was found to be intermediate to those of the homomeric channels. Therefore, different SUR subtypes can coassemble into K(ATP) channels with distinct metabolic sensitivities and pharmacological profiles.

Indexed as

AnimalsATP-Binding Cassette TransportersBlotting, WesternCell LineChlorocebus aethiopsHumansImmunohistochemistryImmunoprecipitationKcnj11 ChannelPatch-Clamp TechniquesPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea ReceptorsXenopus laevisABCC8 protein, humanABCC9 protein, humanATP-Binding Cassette TransportersKcnj11 ChannelPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea Receptors

Identifiers

PMID18723823
PMCPMC2574914
OpenAlexW2031632335

What OpenQuestion holds

Textmetadata
LicenceTDM
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.