Evidence map›Paper›PMID 30419068›Full record

ArticlePloS one2018

Lack of modulatory effect of the SCN5A R1193Q polymorphism on cardiac fast Na+ current at body temperature.

Masayoshi Abe, Koshi Kinoshita, Kenta Matsuoka, Takahito Nakada, Kimiaki Miura, Yukiko Hata, Naoki Nishida, Toshihide Tabata

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 1 institution in 1 country.

Masayoshi AbeLaboratory for Biological Information Processing, Graduate School of Science and Engineering, University of Toyama, Toyama City, Toyama, Japan.
Koshi KinoshitaDepartment of Legal Medicine, Graduate School of Medical and Pharmaceutical Sciences, University of Toyama, Toyama City, Toyama, Japan.
Kenta MatsuokaLaboratory for Biological Information Processing, Graduate School of Science and Engineering, University of Toyama, Toyama City, Toyama, Japan.
Takahito NakadaLaboratory for Biological Information Processing, Graduate School of Science and Engineering, University of Toyama, Toyama City, Toyama, Japan.
Kimiaki MiuraLaboratory for Biological Information Processing, Graduate School of Science and Engineering, University of Toyama, Toyama City, Toyama, Japan.
Yukiko HataDepartment of Legal Medicine, Graduate School of Medical and Pharmaceutical Sciences, University of Toyama, Toyama City, Toyama, Japan.
Naoki NishidaDepartment of Legal Medicine, Graduate School of Medical and Pharmaceutical Sciences, University of Toyama, Toyama City, Toyama, Japan.
Toshihide TabataLaboratory for Biological Information Processing, Graduate School of Science and Engineering, University of Toyama, Toyama City, Toyama, Japan.
University of Toyama · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SCN5A encodes the main subunit of the NaV1.5 channel, which mediates the fast Na+ current responsible for generating cardiac action potentials. The single nucleotide polymorphism SCN5A(R1193Q), which results in an amino acid replacement in the subunit, is common in East Asia. SCN5A(R1193Q) is often identified in patients with type 3 long QT syndrome and Brugada syndrome. However, its linkage to arrhythmic disorders is under debate. Previous electrophysiological studies performed at room temperature inconsistently reported the gain- or loss-of-function effect of SCN5A(R1193Q) on the NaV1.5 channel. More recently, it was theoretically predicted that SCN5A(R1193Q) would exert a loss-of-function effect at body temperature. Here, we experimentally assessed whether SCN5A(R1193Q) modulates the NaV1.5 channel at various temperatures including normal and febrile body temperatures. We compared voltage-gated Na+ currents in SCN5A(R1193Q)-transfected and wild-type SCN5A-transfected HEK293T cells using a whole-cell voltage-clamp technique. First, we made comparisons at constant temperatures of 25°C, 36.5°C, and 38°C, and found no difference in the conductance density, voltage dependence of gating, or time dependence of gating. This suggested that SCN5A(R1193Q) does not modulate the NaV1.5 channel regardless of temperature. Second, we made comparisons while varying the temperature from 38°C to 26°C in 3 min, and again observed no difference in the time course of the amplitude or time dependence of gating during the temperature change. This also indicated that SCN5A(R1193Q) does not modulate the NaV1.5 channel in response to an acute body temperature change. Therefore, SCN5A(R1193Q) may not be a monogenic factor that triggers arrhythmic disorders.

Indexed as

Body TemperatureMembrane PotentialsMutation, MissenseNAV1.5 Voltage-Gated Sodium ChannelPolymorphism, GeneticAmino Acid SubstitutionArrhythmias, CardiacHEK293 CellsHumansMyocardiumSodiumNAV1.5 Voltage-Gated Sodium ChannelSCN5A protein, humanSodium

Identifiers

PMID30419068
PMCPMC6231685
OpenAlexW2901552935

What OpenQuestion holds

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Registered trials

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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.