Evidence map›Paper›PMID 30628647›Full record

ArticleInternational journal of molecular medicine2019

Human ether‑à‑go‑go‑related gene mutation L539fs/47‑hERG leads to cell apoptosis through the endoplasmic reticulum stress pathway.

Shuting Ma, Yun Zhao, Miaomiao Cao, Chaofeng Sun

Expression of concernOpen access · hybridAbstract read
In one paragraph

Article in International journal of molecular medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Shuting MaDepartment of Cardiovascular Medicine, First Affiliated Hospital of Xi'an Jiaotong University, Institute of Cardiovascular Channelopathy, Key Laboratory of Molecular Cardiology, Xi'an, Shaanxi 710061, P.R. China.
Yun ZhaoDepartment of Cardiovascular Medicine, First Affiliated Hospital of Xi'an Jiaotong University, Institute of Cardiovascular Channelopathy, Key Laboratory of Molecular Cardiology, Xi'an, Shaanxi 710061, P.R. China.
Miaomiao CaoDepartment of Cardiovascular Medicine, First Affiliated Hospital of Xi'an Jiaotong University, Institute of Cardiovascular Channelopathy, Key Laboratory of Molecular Cardiology, Xi'an, Shaanxi 710061, P.R. China.
Chaofeng SunDepartment of Cardiovascular Medicine, First Affiliated Hospital of Xi'an Jiaotong University, Institute of Cardiovascular Channelopathy, Key Laboratory of Molecular Cardiology, Xi'an, Shaanxi 710061, P.R. China.
First Affiliated Hospital of Xi'an Jiaotong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Congenital long QT syndrome (LQTS) is a cardiac channelopathy that often results in fatal arrhythmias. LQTS mutations not only lead to abnormal myocardial electrical activities but are associated with heart contraction abnormalities, cardiomyopathy and congenital heart defects. In vivo and in vitro studies have found that LQTS mutations are associated with cardiomyocyte apoptosis, cardiac developmental disorders and even embryonic mortality. Cardiac delayed rectifier potassium channel dysfunction due to the human ether‑à‑go‑go‑related gene (hERG) mutation causes congenital LQTS type 2. The majority of LQTS 2 mutations are characterized by mutant protein accumulation in the endoplasmic reticulum (ER). Unfolded or misfolded protein retention in the ER causes an unfolded protein reaction, which is characteristic of ER stress (ERS). Therefore, the present study hypothesized that LQTS mutations can cause cardiac structural abnormalities via ERS‑mediated cardiomyocyte apoptosis. To test this hypothesis, 293 cells were transiently transfected with an L539fs/47‑hERG plasmid to generate an LQTS 2 model. L539fs/47‑hERG is an LQTS 2 mutation, which consists of a 19‑bp deletion at 1619‑1637 and a point mutation at 1692. Using confocal laser scanning microscopy analysis, it was verified that the L539fs/47‑hERG protein was retained in the ER. Hoechst 33342 apoptosis staining indicated that apoptosis was increased in the L539fs/47‑hERG‑transfected cells, and this be reversed by treatment with 4‑phenyl butyric acid. Western blot analysis revealed increased expression levels of the ERS chaperone glucose regulated protein 78 and pro‑apoptotic ERS‑induced factors, including protein kinase R‑like endoplasmic reticulum kinase, eukaryotic translation‑initiation factor‑2α and C/EBP homologous protein, in the L539fs/47‑hERG‑transfected cells. The B‑cell lymphoma (Bcl‑2)‑associated X protein/Bcl‑2 ratio and caspase‑12 were also increased in the mutated cells. These results demonstrate that L539fs/47‑hERG induces cell apoptosis and the potential molecular mechanism involves the activation of ERS and ERS‑mediated cell apoptosis.

Indexed as

MutationAmino Acid SubstitutionApoptosisBase SequenceEndoplasmic ReticulumEndoplasmic Reticulum StressHEK293 CellsHumansLong QT SyndromeModels, BiologicalSequence Analysis, DNATranscriptional Regulator ERGUnfolded Protein ResponseERG protein, humanTranscriptional Regulator ERG

Identifiers

PMID30628647
PMCPMC6365044
OpenAlexW2907162817

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.