Evidence map›Paper›PMID 16418402›Full record

ArticleThe Journal of general physiology2006

Membrane-delimited inhibition of maxi-K channel activity by the intermediate conductance Ca2+-activated K channel.

Jill Thompson, Ted Begenisich

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Functional Potassium Channels in Macrophages.The Journal of membrane biology · 2023
    Review
  3. KCells · 2020
    Review
  4. New saliva secretion model based on the expression of NaPflugers Archiv : European journal of physiology · 2018
    Article
  5. Article
  6. Review
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  8. Article
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  14. A dynamic model of saliva secretion.Journal of theoretical biology · 2010
    Article
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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

2 authors at 1 institution in 1 country.

Jill ThompsonDepartment of Pharmacology, University of Rochester Medical Center, Rochester, NY 14642, USA.
Ted Begenisich
University of Rochester Medical Center · US

Funding

Salivary gland hypofunction: genetic defects in signalP01DE013539 · NIDCR · UNIVERSITY OF ROCHESTER · PI MELVIN, JAMES E · 2000 to 2004
$4.7M
NIDCR NIH HHS DE-13539NIDCR NIH HHS P01 DE013539
6 · The paper itself

Abstract

The complexity of mammalian physiology requires a diverse array of ion channel proteins. This diversity extends even to a single family of channels. For example, the family of Ca2+-activated K channels contains three structural subfamilies characterized by small, intermediate, and large single channel conductances. Many cells and tissues, including neurons, vascular smooth muscle, endothelial cells, macrophages, and salivary glands express more than a single class of these channels, raising questions about their specific physiological roles. We demonstrate here a novel interaction between two types of Ca2+-activated K channels: maxi-K channels, encoded by the KCa1.1 gene, and IK1 channels (KCa3.1). In both native parotid acinar cells and in a heterologous expression system, activation of IK1 channels inhibits maxi-K activity. This interaction was independent of the mode of activation of the IK1 channels: direct application of Ca2+, muscarinic receptor stimulation, or by direct chemical activation of the IK1 channels. The IK1-induced inhibition of maxi-K activity occurred in small, cell-free membrane patches and was due to a reduction in the maxi-K channel open probability and not to a change in the single channel current level. These data suggest that IK1 channels inhibit maxi-K channel activity via a direct, membrane-delimited interaction between the channel proteins. A quantitative analysis indicates that each maxi-K channel may be surrounded by four IK1 channels and will be inhibited if any one of these IK1 channels opens. This novel, regulated inhibition of maxi-K channels by activation of IK1 adds to the complexity of the properties of these Ca2+-activated K channels and likely contributes to the diversity of their functional roles.

Indexed as

AnimalsCalciumCell MembraneChloride ChannelsGene ExpressionIntermediate-Conductance Calcium-Activated Potassium ChannelsLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMiceMice, Inbred StrainsModels, BiologicalParotid GlandPatch-Clamp TechniquesReceptors, MuscarinicCalciumChloride ChannelsIntermediate-Conductance Calcium-Activated Potassium ChannelsLarge-Conductance Calcium-Activated Potassium ChannelsReceptors, Muscarinic

Identifiers

PMID16418402
PMCPMC2151496
OpenAlexW1986941387

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.