Evidence map›Paper›PMID 22752717›Full record

ArticleThe Journal of membrane biology2012

Neurons and β-cells of the pancreas express connexin36, forming gap junction channels that exhibit strong cationic selectivity.

Feliksas F Bukauskas

Open access · greenAbstract read
In one paragraph

Article in The Journal of membrane biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Defining the electrical synapse.Nature reviews. Neuroscience · 2026
    Review
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  13. Two functionally distinct networks of gap junction-coupled inhibitory neurons in the thalamic reticular nucleus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  14. Article
  15. Connexins and steroidogenesis in mouse Leydig cells.Canadian journal of physiology and pharmacology · 2013
    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

1 author at 1 institution in 1 country.

Feliksas F BukauskasDominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. feliksas.bukauskas@einstein.yu.edu
Albert Einstein College of Medicine · US

Funding

Connexins and Heart FunctionR01HL084464 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2007 to 2010
$1.7M
Gating of Connexin-Based Gap Junction Channels and HemichannelsR01NS072238 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2010 to 2013
$1.4M
NHLBI NIH HHS HL084464NHLBI NIH HHS R01 HL084464NINDS NIH HHS NS072238NINDS NIH HHS R01 NS072238
6 · The paper itself

Abstract

We examined the permeability of connexin36 (Cx36) homotypic gap junction (GJ) channels, expressed in neurons and β-cells of the pancreas, to dyes differing in molecular mass and net charge. Experiments were performed in HeLa cells stably expressing Cx36 tagged with EGFP by combining a dual whole-cell voltage clamp and fluorescence imaging. To assess the permeability of the single GJ channel (P(γ)), we used a dual-mode excitation of fluorescent dyes that allowed us to measure cell-to-cell dye transfer at levels not resolvable using whole-field excitation solely. We demonstrate that P(γ) of Cx36 for cationic dyes (EAM-1⁺ and EAM-2⁺) is ~10-fold higher than that for an anionic dye of the same net charge and similar molecular mass, Alexa fluor-350 (AFl-350⁻). In addition, P(γ) for Lucifer yellow (LY²⁻) is approximately fourfold smaller than that for AFl-350⁻, which suggests that the higher negativity of LY²⁻ significantly reduces permeability. The P(γ) of Cx36 for AFl-350 is approximately 358, 138, 23 and four times smaller than the P(γ)s of Cx43, Cx40, Cx45, and Cx57, respectively. In contrast, it is 6.5-fold higher than the P(γ) of mCx30.2, which exhibits a smaller single-channel conductance. Thus, Cx36 GJs are highly cation-selective and should exhibit relatively low permeability to numerous vital negatively charged metabolites and high permeability to K⁺, a major charge carrier in cell-cell communication.

Indexed as

CationsConnexinsElectrophysiologyGap Junction delta-2 ProteinGap JunctionsHeLa CellsHumansIon Channel GatingIon ChannelsCationsConnexinsGap Junction delta-2 ProteinIon Channels

Identifiers

PMID22752717
PMCPMC3626077
OpenAlexW2027448639

What OpenQuestion holds

Textmetadata
LicenceTDM
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.