Evidence map›Paper›PMID 24297175›Full record

ArticleThe Journal of biological chemistry2014

Differential protein kinase C-dependent modulation of Kv7.4 and Kv7.5 subunits of vascular Kv7 channels.

Lioubov I Brueggemann, Alexander R Mackie, Leanne L Cribbs, Jessica Freda, Abhishek Tripathi, Matthias Majetschak, Kenneth L Byron

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Review
  2. Article
  3. The machinery of healthy vasoconstriction: an overview.Pflugers Archiv : European journal of physiology · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. KCNQ5 activation by tannins mediates vasorelaxant effects of barks used in Native American botanical medicine.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

7 authors.

Lioubov I BrueggemannFrom the Departments of Molecular Pharmacology and Therapeutics.
Alexander R Mackie
Leanne L Cribbs
Jessica Freda
Abhishek Tripathi
Matthias Majetschak
Kenneth L Byron

Funding

KCNQ Channels and Vasoconstrictor Signal TransductionR01HL089564 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI BYRON, KENNETH L · 2009 to 2013
$1.9M
NHLBI NIH HHS R01 HL089564
6 · The paper itself

Abstract

The Kv7 family (Kv7.1-7.5) of voltage-activated potassium channels contributes to the maintenance of resting membrane potential in excitable cells. Previously, we provided pharmacological and electrophysiological evidence that Kv7.4 and Kv7.5 form predominantly heteromeric channels and that Kv7 activity is regulated by protein kinase C (PKC) in response to vasoconstrictors in vascular smooth muscle cells. Direct evidence for Kv7.4/7.5 heteromer formation, however, is lacking. Furthermore, it remains to be determined whether both subunits are regulated by PKC. Utilizing proximity ligation assays to visualize single molecule interactions, we now show that Kv7.4/Kv.7.5 heteromers are endogenously expressed in vascular smooth muscle cells. Introduction of dominant-negative Kv7.4 and Kv7.5 subunits in mesenteric artery myocytes reduced endogenous Kv7 currents by 84 and 76%, respectively. Expression of an inducible protein kinase Cα (PKCα) translocation system revealed that PKCα activation is sufficient to suppress endogenous Kv7 currents in A7r5 rat aortic and mesenteric artery smooth muscle cells. Arginine vasopressin (100 and 500 pm) and the PKC activator phorbol 12-myristate 13-acetate (1 nm) each inhibited human (h) Kv7.5 and hKv7.4/7.5, but not hKv7.4 channels expressed in A7r5 cells. A decrease in hKv7.5 and hKv7.4/7.5 current densities was associated with an increase in PKC-dependent phosphorylation of the channel proteins. These findings provide further evidence for a differential regulation of Kv7.4 and Kv7.5 channel subunits by PKC-dependent phosphorylation and new mechanistic insights into the role of heteromeric subunit assembly for regulation of vascular Kv7 channels.

Indexed as

AnimalsAortaArginine VasopressinCarcinogensCell LineHumansKCNQ Potassium ChannelsMaleMesenteric ArteriesMutation, MissenseMyocytes, Smooth MuscleProtein Kinase C-alphaRatsRats, Sprague-DawleyTetradecanoylphorbol AcetateVasoconstrictor AgentsArginine VasopressinCarcinogensKCNQ4 protein, humanKcnq4 protein, ratKCNQ5 protein, humanKcnq5 protein, ratKCNQ Potassium ChannelsPRKCA protein, humanProtein Kinase C-alphaTetradecanoylphorbol AcetateVasoconstrictor AgentsKCNQ ChannelMesenteric ArteryPatch Clamp ElectrophysiologyPotassium ChannelsProtein PhosphorylationSignal TransductionVascular Smooth Muscle CellsVasopressin

Identifiers

PMID24297175
PMCPMC3900957

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.