Evidence map›Paper›PMID 12015420›Full record

ArticleThe Journal of physiology2002

Protein kinase C modulation of recombinant ATP-sensitive K(+) channels composed of Kir6.1 and/or Kir6.2 expressed with SUR2B.

Kevin S Thorneloe, Yoshiaki Maruyama, A Todd Malcolm, Peter E Light, Michael P Walsh, William C Cole

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Sexual dimorphism in vascular ATP-sensitive KThe Journal of physiology · 2021
    Article
  3. Review
  4. Article
  5. Review
  6. Risk factors and global cognitive status related to brain arteriolosclerosis in elderly individuals.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2017
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  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

6 authors at 2 institutions in 1 country.

Kevin S ThorneloeSmooth Muscle Research Group and Canadian Institutes of Health Research Group in Regulation of Vascular Contractility, University of Calgary, Calgary, Alberta, Canada.
Yoshiaki Maruyama
A Todd Malcolm
Peter E Light
Michael P Walsh
William C Cole
Canadian Institutes of Health Research · CAUniversity of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular identity of smooth muscle ATP-sensitive K(+) channels (K(ATP)) is not established with certainty. Patch clamp methods were employed to determine if recombinant K(ATP) channels composed of Kir6.1 and SUR2B subunits expressed by human embryonic kidney (HEK293) cells share an identical modulation by protein kinase C (PKC) with the vascular K(NDP) subtype of K(ATP) channel. The open probability of Kir6.1/SUR2B channels was determined before and after sequential exposure to pinacidil (50 microM) and the combination of pinacidil and phorbol 12,13-dibutyrate (PdBu; 50 nM). Treatment with PdBu caused a decline in channel activity, but this was not seen with an inactive phorbol ester, 4 alpha-phorbol 12,13-didecanoate (PdDe; 50 nM). Angiotensin II (0.1 microM) induced a similar inhibition of Kir6.1/SUR2B channels in cells expressing angiotensin AT(1) receptors. The effects of PdBu and angiotensin II were blocked by the PKC inhibitor, chelerythrine (3 microM). Purified PKC inhibited Kir6.1/SUR2B activity (in 0.5 mM ATP/ 0.5 mM ADP), and the inhibition was blocked by a specific peptide inhibitor of PKC, PKC(19-31). In contrast, PdBu increased the activity of recombinant K(ATP) channels composed of Kir6.2 and SUR2B, or the combination of Kir6.1, Kir6.2 and SUR2B subunits. The results indicate that the modulation by PKC of Kir6.1/SUR2B, but not Kir6.2/SUR2B or Kir6.1-Kir6.2/SUR2B channel gating mimics that of native vascular K(NDP) channels. Physiological inhibition of vascular K(ATP) current by vasoconstrictors which utilize intracellular signalling cascades involving PKC is concluded to involve the modulation of K(NDP) channel complexes composed of four Kir6.1 and their associated SUR2B subunits.

Indexed as

ATP-Binding Cassette TransportersAlgorithmsAngiotensin IICell LineElectrophysiologyEnzyme InhibitorsHumansKATP ChannelsKineticsMembrane PotentialsPatch-Clamp TechniquesPhorbol EstersPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein Kinase CReceptors, DrugAngiotensin IIATP-Binding Cassette TransportersEnzyme InhibitorsKATP ChannelsPhorbol EstersPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein Kinase CReceptors, DrugRecombinant ProteinsSulfonylurea ReceptorsuK-ATP-1 potassium channel

Identifiers

PMID12015420
PMCPMC2290299
OpenAlexW2075207354

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.