Evidence map›Paper›PMID 25172946›Full record

ArticleThe Journal of physiology2014

Na+ current properties in islet α- and β-cells reflect cell-specific Scn3a and Scn9a expression.

Quan Zhang, Margarita V Chibalina, Martin Bengtsson, Lukas N Groschner, Reshma Ramracheya, Nils J G Rorsman, Veronika Leiss, Mohammed A Nassar, Andrea Welling, Fiona M Gribble and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 93 citations in OpenAlex.

  1. Trial
  2. Article
  3. Glycolytic activation of β-cell NaMolecular metabolism · 2026
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  15. GNature communications · 2022
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  19. Regulation of α-cell glucagon secretion: The role of second messengers.Chronic diseases and translational medicine · 2022
    Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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

15 authors at 7 institutions in 3 countries.

Quan ZhangOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK.
Margarita V ChibalinaOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK.
Martin BengtssonOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK.
Lukas N GroschnerOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK.
Reshma RamracheyaOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK.
Nils J G RorsmanOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK.
Veronika LeissInstitut für Pharmakologie und Toxikologie, TU München, Biedersteiner Str. 29, 80802, München, Germany Institut für Pharmakologie und Toxikologie, Eberhard-Karls Universität, Wilhelmstr. 56, 72074, Tübingen, Germany.
Mohammed A NassarMolecular Nociception Group, University College London (UCL), Gower Street, London, WC1E 6BT, UK Biomedical Science, University of Sheffield, Sheffield, S10 2TN, UK.
Andrea WellingInstitut für Pharmakologie und Toxikologie, TU München, Biedersteiner Str. 29, 80802, München, Germany.
Fiona M GribbleCambridge Institute for Medical Research, University of Cambridge School of Clinical Medicine, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Frank ReimannCambridge Institute for Medical Research, University of Cambridge School of Clinical Medicine, Wellcome Trust/MRC Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Franz HofmannInstitut für Pharmakologie und Toxikologie, TU München, Biedersteiner Str. 29, 80802, München, Germany FOR 923, Institut für Pharmakologie und Toxikologie, TU München, Biedersteiner Str. 29, 80802, München, Germany.
John N WoodMolecular Nociception Group, University College London (UCL), Gower Street, London, WC1E 6BT, UK.
Frances M AshcroftHenry Wellcome Centre for Gene Function, Department of Physiology, Anatomy and Genetics, University of Oxford, Parks Road, Oxford, OX1 3PT, UK.
Patrik RorsmanOxford Centre for Diabetes, Endocrinology and Metabolism, University of Oxford, Churchill Hospital, Oxford, OX3 7LJ, UK Department of Neuroscience and Physiology, Sahlgren's Academy, University of Göteborg, Box 430, SE40530, Göteborg, Sweden patrik.rorsman@ocdem.ox.ac.uk.
Churchill Hospital · GBUniversity of Oxford · GBUniversity of Cambridge · GBOxford Centre for Diabetes, Endocrinology and Metabolism · GBUniversity College London · GBUniversity of Sheffield · GBUniversity of Tübingen · DE

Funding

Biotechnology and Biological Sciences Research Council BB/F000227/1Medical Research Council G0801995Medical Research Council G0901905Medical Research Council MC_UU_12012/3Wellcome Trust 084655Wellcome Trust 088357Wellcome Trust 089795Wellcome Trust 095531Wellcome Trust 095531/Z/11/ZWellcome Trust 101054Wellcome Trust 884655
6 · The paper itself

Abstract

Mouse pancreatic β- and α-cells are equipped with voltage-gated Na(+) currents that inactivate over widely different membrane potentials (half-maximal inactivation (V0.5) at -100 mV and -50 mV in β- and α-cells, respectively). Single-cell PCR analyses show that both α- and β-cells have Nav1.3 (Scn3) and Nav1.7 (Scn9a) α subunits, but their relative proportions differ: β-cells principally express Nav1.7 and α-cells Nav1.3. In α-cells, genetically ablating Scn3a reduces the Na(+) current by 80%. In β-cells, knockout of Scn9a lowers the Na(+) current by >85%, unveiling a small Scn3a-dependent component. Glucagon and insulin secretion are inhibited in Scn3a(-/-) islets but unaffected in Scn9a-deficient islets. Thus, Nav1.3 is the functionally important Na(+) channel α subunit in both α- and β-cells because Nav1.7 is largely inactive at physiological membrane potentials due to its unusually negative voltage dependence of inactivation. Interestingly, the Nav1.7 sequence in brain and islets is identical and yet the V0.5 for inactivation is >30 mV more negative in β-cells. This may indicate the presence of an intracellular factor that modulates the voltage dependence of inactivation.

Indexed as

AnimalsGene Expression RegulationGlucagon-Secreting CellsGlucoseHEK293 CellsHumansInsulinInsulin-Secreting CellsInsulin SecretionMiceMice, Inbred C57BLMice, KnockoutNAV1.3 Voltage-Gated Sodium ChannelNAV1.7 Voltage-Gated Sodium ChannelNeurotoxinsProtein IsoformsGlucoseInsulinNAV1.3 Voltage-Gated Sodium ChannelNAV1.7 Voltage-Gated Sodium ChannelNeurotoxinsProtein IsoformsProtein SubunitsSodium

Identifiers

PMID25172946
PMCPMC4253470
OpenAlexW1608643486

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.