Evidence map›Paper›PMID 23486946›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013

Intracellular magnesium-dependent modulation of gap junction channels formed by neuronal connexin36.

Nicolás Palacios-Prado, Gregory Hoge, Alina Marandykina, Lina Rimkute, Sandrine Chapuis, Nerijus Paulauskas, Vytenis A Skeberdis, John O'Brien, Alberto E Pereda, Michael V L Bennett and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Magnesium (MgCurrent pharmaceutical design · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Magnesium Is a Key Player in Neuronal Maturation and Neuropathology.International journal of molecular sciences · 2019
    Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Two Forms of Electrical Transmission Between Neurons.Frontiers in molecular neuroscience · 2018
    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

11 authors at 2 institutions in 2 countries.

Nicolás Palacios-PradoDominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Gregory Hoge
Alina Marandykina
Lina Rimkute
Sandrine Chapuis
Nerijus Paulauskas
Vytenis A Skeberdis
John O'Brien
Alberto E Pereda
Michael V L Bennett
Feliksas F Bukauskas
Albert Einstein College of Medicine · USLithuanian University of Health Sciences · LT

Funding

REGULATION OF RETINAL GAP JUNCTIONSR01EY012857 · NEI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JOHN O'BRIEN · 2000 to 2026
$8.3M
Plasticity of Electrical SynapsesR01DC011099 · NIDCD · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI Alberto E Pereda · 2010 to 2026
$7.0M
Connexins and Heart FunctionR01HL084464 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2007 to 2010
$1.7M
Cx43 Hemichannels: Gating, Modification and FunctionR01NS055363 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BENNETT, MICHAEL V L · 2007 to 2011
$1.6M
Gating of Connexin-Based Gap Junction Channels and HemichannelsR01NS072238 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI BUKAUSKAS, FELIKSAS · 2010 to 2013
$1.4M
Plasticity of Mammalian Electrical SynapsesR21NS055726 · NINDS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI PEREDA, ALBERTO E · 2007 to 2008
$399k
NEI NIH HHS EY 12857NEI NIH HHS R01 EY012857NHLBI NIH HHS R01 HL084464NHLBI NIH HHS R01HL 084464NIDCD NIH HHS DC 011099NIDCD NIH HHS R01 DC011099NINDS NIH HHS NS 55363NINDS NIH HHS R01 NS055363NINDS NIH HHS R01 NS072238NINDS NIH HHS R01NS 072238NINDS NIH HHS R21 NS055726NINDS NIH HHS R21NS055726
6 · The paper itself

Abstract

Gap junction (GJ) channels composed of Connexin36 (Cx36) are widely expressed in the mammalian CNS and form electrical synapses between neurons. Here we describe a novel modulatory mechanism of Cx36 GJ channels dependent on intracellular free magnesium ([Mg(2+)]i). We examined junctional conductance (gj) and its dependence on transjunctional voltage (Vj) at different [Mg(2+)]i in cultures of HeLa or N2A cells expressing Cx36. We found that Cx36 GJs are partially inhibited at resting [Mg(2+)]i. Thus, gj can be augmented or reduced by lowering or increasing [Mg(2+)]i, respectively. Similar changes in gj and Vj-gating were observed using MgATP or K2ATP in pipette solutions, which increases or decreases [Mg(2+)]i, respectively. Changes in phosphorylation of Cx36 or in intracellular free calcium concentration were not involved in the observed Mg(2+)-dependent modulation of gj. Magnesium ions permeate the channel and transjunctional asymmetry in [Mg(2+)]i resulted in asymmetric Vj-gating. The gj of GJs formed of Cx26, Cx32, Cx43, Cx45, and Cx47 was also reduced by increasing [Mg(2+)]i, but was not increased by lowering [Mg(2+)]i; single-channel conductance did not change. We showed that [Mg(2+)]i affects both open probability and the number of functional channels, likely through binding in the channel lumen. Finally, we showed that Cx36-containing electrical synapses between neurons of the trigeminal mesencephalic nucleus in rat brain slices are similarly affected by changes in [Mg(2+)]i. Thus, this novel modulatory mechanism could underlie changes in neuronal synchronization under conditions in which ATP levels, and consequently [Mg(2+)]i, are modified.

Indexed as

Adenosine TriphosphateAnimalsAnimals, NewbornBiophysical PhenomenaCations, DivalentCell Line, TumorChelating AgentsConnexin 26ConnexinsDose-Response Relationship, DrugEgtazic AcidFemaleGap Junction delta-2 ProteinGap JunctionsGreen Fluorescent ProteinsHumans1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acidAdenosine TriphosphateCations, DivalentChelating AgentsConnexin 26ConnexinsEgtazic AcidGap Junction delta-2 ProteinGJB2 protein, humanGreen Fluorescent ProteinsMagnesium

Identifiers

PMID23486946
PMCPMC3635812
OpenAlexW2006787260

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.