Evidence map›Paper›PMID 24202214›Full record

ArticleThe Journal of biological chemistry2013

Caveolin-1 facilitates the direct coupling between large conductance Ca2+-activated K+ (BKCa) and Cav1.2 Ca2+ channels and their clustering to regulate membrane excitability in vascular myocytes.

Yoshiaki Suzuki, Hisao Yamamura, Susumu Ohya, Yuji Imaizumi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. CaInflammation and regeneration · 2025
    Review
  5. Review
  6. Insulin resistance, CaFrontiers in physiology · 2025
    Review
  7. Review
  8. CaInflammation and regeneration · 2024
    Review
  9. Piezo1, the new actor in cell volume regulation.Pflugers Archiv : European journal of physiology · 2024
    Review
  10. Article
  11. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  12. Review
  13. CaInternational journal of molecular sciences · 2023
    Review
  14. A molecular complex of CaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Functional tuning of Vascular L-type CaFrontiers in physiology · 2022
    Review
  17. Review
  18. Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Yoshiaki SuzukiFrom the Department of Molecular and Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan and.
Hisao Yamamura
Susumu Ohya
Yuji Imaizumi
Nagoya City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-type voltage-dependent Ca(2+) channels (LVDCC) and large conductance Ca(2+)-activated K(+) channels (BKCa) are the major factors defining membrane excitability in vascular smooth muscle cells (VSMCs). The Ca(2+) release from sarcoplasmic reticulum through ryanodine receptor significantly contributes to BKCa activation in VSMCs. In this study direct coupling between LVDCC (Cav1.2) and BKCa and the role of caveoline-1 on their interaction in mouse mesenteric artery SMCs were examined. The direct activation of BKCa by Ca(2+) influx through coupling LVDCC was demonstrated by patch clamp recordings in freshly isolated VSMCs. Using total internal reflection fluorescence microscopy, it was found that a large part of yellow fluorescent protein-tagged BKCa co-localized with the cyan fluorescent protein-tagged Cav1.2 expressed in the plasma membrane of primary cultured mouse VSMCs and that the two molecules often exhibited FRET. It is notable that each BKα subunit of a tetramer in BKCa can directly interact with Cav1.2 and promotes Cav1.2 cluster in the molecular complex. Furthermore, caveolin-1 deficiency in knock-out (KO) mice significantly reduced not only the direct coupling between BKCa and Cav1.2 but also the functional coupling between BKCa and ryanodine receptor in VSMCs. The measurement of single cell shortening by 40 mm K(+) revealed enhanced contractility in VSMCs from KO mice than wild type. Taken together, caveolin-1 facilitates the accumulation/clustering of BKCa-LVDCC complex in caveolae, which effectively regulates spatiotemporal Ca(2+) dynamics including the negative feedback, to control the arterial excitability and contractility.

Indexed as

Action PotentialsAnimalsCalciumCalcium Channels, L-TypeCaveolin 1HEK293 CellsHumansLarge-Conductance Calcium-Activated Potassium ChannelsMiceMice, Inbred C57BLMice, KnockoutMuscle ContractionMuscle, Smooth, VascularMyocytes, Smooth MuscleProtein BindingProtein SubunitsCalciumCalcium Channels, L-TypeCav1 protein, mouseCaveolin 1Large-Conductance Calcium-Activated Potassium ChannelsL-type calcium channel alpha(1C)Protein SubunitsRyanodine Receptor Calcium Release ChannelCalcium SignalingCaveolinFluorescence Resonance Energy Transfer (FRET)ImagingLarge Conductance Calcium-activated Potassium ChannelL-type Voltage-dependent Calcium ChannelSingle Molecule BiophysicsTotal Internal Reflection Fluorescent MicroscopyVascular Smooth Muscle Cells

Identifiers

PMID24202214
PMCPMC3868784
OpenAlexW2010115785

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.