Evidence map›Paper›PMID 21984254›Full record

ArticleMolecular pharmacology2012

The LRRC26 protein selectively alters the efficacy of BK channel activators.

Janos Almassy, Ted Begenisich

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Molecular pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

31 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021
    Review
  7. Review
  8. Calcium-Activated KHandbook of experimental pharmacology · 2021
    Article
  9. Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance CaAmerican journal of physiology. Lung cellular and molecular physiology · 2020
    Article
  10. Review
  11. Review
  12. Knockout of the LRRC26 subunit reveals a primary role of LRRC26-containing BK channels in secretory epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. BK Channels in the Central Nervous System.International review of neurobiology · 2016
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Janos AlmassyDepartment of Pharmacology and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA.
Ted Begenisich
University of Rochester · US

Funding

An experimental/computational approach for understanding salivary fluid secretionR01DE019245 · NIDCR · UNIVERSITY OF ROCHESTER · PI David I Yule · 2008 to 2026
$9.7M
The Physiological Roles of K Channels in Fluid SecretionR01DE016960 · NIDCR · UNIVERSITY OF ROCHESTER · PI BEGENISICH, TED B · 2006 to 2010
$1.8M
NIDCR NIH HHS R01 DE016960NIDCR NIH HHS R01-DE016960NIDCR NIH HHS R01 DE019245NIDCR NIH HHS R01-DE019245
6 · The paper itself

Abstract

Large conductance, Ca(2+)-activated K channel proteins are involved in a wide range of physiological activities, so there is considerable interest in the pharmacology of large conductance calcium-activated K (BK) channels. One potent activator of BK channels is mallotoxin (MTX), which produces a very large hyperpolarizing shift of the voltage gating of heterologously expressed BK channels and causes a dramatic increase in the activity of BK channels in human smooth muscle cells. However, we found that MTX shifted the steady-state activation of BK channels in native parotid acinar cells by only 6 mV. This was not because the parotid BK isoform (parSlo) is inherently insensitive to MTX as MTX shifted the activation of heterologously expressed parSlo channels by 70 mV. Even though MTX had a minimal effect on steady-state activation of parotid BK channels, it produced an approximate 2-fold speeding of the channel-gating kinetics. The BK channels in parotid acinar cells have a much more hyperpolarized voltage activation range than BK channels in most other cell types. We found that this is probably attributable to an accessory protein, LRRC26, which is expressed in parotid glands: expressed parSlo + LRRC26 channels were resistant to the actions of MTX. Another class of BK activators is the benzimidazalones that includes 1,3-dihydro-1-(2-hydroxy-5-(trifluoromethyl)phenyl)-5-(trifluoromethyl)-2H-benzimidazol-2-one (NS-1619). Although the LRRC26 accessory protein strongly inhibited the ability of MTX to activate BK channels, we found that it had only a small effect on the action of NS-1619 on BK channels. Thus, the LRRC26 BK channel accessory protein selectively alters the pharmacology of BK channels.

Indexed as

Acinar CellsAnimalsBenzimidazolesCells, CulturedCHO CellsCricetinaeCricetulusHumansLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMiceNeoplasm ProteinsParotid GlandPatch-Clamp TechniquesPicrotoxinPotassium ChannelsBenzimidazoleshyenanchinLarge-Conductance Calcium-Activated Potassium ChannelsLRRC26 protein, humanNeoplasm ProteinsNS 1619PicrotoxinPotassium Channels

Identifiers

PMID21984254
PMCPMC3250112
OpenAlexW2153592673

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.