Evidence map›Paper›PMID 20876197›Full record

ArticleThe Journal of physiology2010

Stromatoxin-sensitive, heteromultimeric Kv2.1/Kv9.3 channels contribute to myogenic control of cerebral arterial diameter.

Xi Zoë Zhong, Khaled S Abd-Elrahman, Chiu-Hsiang Liao, Ahmed F El-Yazbi, Emma J Walsh, Michael P Walsh, William C Cole

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

42 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Vascular Function and Ion Channels in Alzheimer's Disease.Microcirculation (New York, N.Y. : 1994) · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Mechanism of use-dependent Kv2 channel inhibition by RY785.The Journal of general physiology · 2022
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Kv2.1 channels play opposing roles in regulating membrane potential, CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. KMicrocirculation (New York, N.Y. : 1994) · 2018
    Review
  18. KMicrocirculation (New York, N.Y. : 1994) · 2018
    Review
  19. Review
  20. The yin and yang of KMicrocirculation (New York, N.Y. : 1994) · 2018
    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

7 authors at 1 institution in 1 country.

Xi Zoë ZhongThe Smooth Muscle Research Group, Department of Physiology and Pharmacology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive N.W., Calgary, Alberta, Canada T2N 4N1.
Khaled S Abd-Elrahman
Chiu-Hsiang Liao
Ahmed F El-Yazbi
Emma J Walsh
Michael P Walsh
William C Cole
University of Calgary · CA

Funding

Canadian Institutes of Health Research MOP-13505
6 · The paper itself

Abstract

Cerebral vascular smooth muscle contractility plays a crucial role in controlling arterial diameter and, thereby, blood flow regulation in the brain. A number of K(+) channels have been suggested to contribute to the regulation of diameter by controlling smooth muscle membrane potential (E(m)) and Ca(2+) influx. Previous studies indicate that stromatoxin (ScTx1)-sensitive, Kv2-containing channels contribute to the control of cerebral arterial diameter at 80 mmHg, but their precise role and molecular composition were not determined. Here, we tested if Kv2 subunits associate with 'silent' subunits from the Kv5, Kv6, Kv8 or Kv9 subfamilies to form heterotetrameric channels that contribute to control of diameter of rat middle cerebral arteries (RMCAs) over a range of intraluminal pressure from 10 to 100 mmHg. The predominant mRNAs expressed by RMCAs encode Kv2.1 and Kv9.3 subunits. Co-localization of Kv2.1 and Kv9.3 proteins at the plasma membrane of dissociated single RMCA myocytes was detected by proximity ligation assay. ScTx1-sensitive native current of RMCA myocytes and Kv2.1/Kv9.3 currents exhibited functional identity based on the similarity of their deactivation kinetics and voltage dependence of activation that were distinct from those of homomultimeric Kv2.1 channels. ScTx1 treatment enhanced the myogenic response of pressurized RMCAs between 40 and 100 mmHg, but this toxin also caused constriction between 10 and 40 mmHg that was not previously observed following inhibition of large conductance Ca(2+)-activated K(+) (BK(Ca)) and Kv1 channels. Taken together, this study defines the molecular basis of Kv2-containing channels and contributes to our understanding of the functional significance of their expression in cerebral vasculature. Specifically, our findings provide the first evidence of heteromultimeric Kv2.1/Kv9.3 channel expression in RMCA myocytes and their distinct contribution to control of cerebral arterial diameter over a wider range of E(m) and transmural pressure than Kv1 or BK(Ca) channels owing to their negative range of voltage-dependent activation.

Indexed as

AnimalsCerebral ArteriesHEK293 CellsHumansKCNQ3 Potassium ChannelMalePeptidesProtein MultimerizationProtein SubunitsRatsRats, Sprague-DawleyShab Potassium ChannelsSpider VenomsVasoconstrictionKcnb1 protein, ratKCNQ3 Potassium ChannelKcnq3 protein, ratPeptidesProtein SubunitsShab Potassium ChannelsSpider Venomsstromatoxin protein, Stromatopelma calceata

Identifiers

PMID20876197
PMCPMC3008855
OpenAlexW2110868985

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.