Evidence map›Paper›PMID 29777134›Full record

ArticleScientific reports2018

Zebrafish VCAP1X2 regulates cardiac contractility and proliferation of cardiomyocytes and epicardial cells.

Fang-Chi Hsieh, Yu-Fen Lu, Ian Liau, Chien-Chang Chen, Chao-Min Cheng, Chung-Der Hsiao, Sheng-Ping L Hwang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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 43% 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, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Thyroid Hormone Receptor α Mutations Cause Heart Defects in Zebrafish.Thyroid : official journal of the American Thyroid Association · 2021
    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

7 authors at 6 institutions in 1 country.

Fang-Chi HsiehGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, 11490, Taiwan.
Yu-Fen LuInstitute of Cellular and Organismic Biology, Academia Sinica, Taipei, 11529, Taiwan.
Ian LiauDepartment of Applied Chemistry and Institute of Molecular Science, National Chiao Tung University, Hsinchu, 30010, Taiwan.
Chien-Chang ChenInstitue of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Chao-Min ChengInstitute of Nanoengineering and Microsystems, National Tsing Hua University, Hsinchu, 30013, Taiwan.
Chung-Der HsiaoDepartment of Bioscience Technology, Chung Yuan Christian University, Taoyuan, 32023, Taiwan.
Sheng-Ping L HwangGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, 11490, Taiwan. zoslh@gate.sinica.edu.tw.ORCID 0000-0003-2554-3821
Institute of Cellular and Organismic Biology, Academia Sinica · TWChung Yuan Christian University · TWInstitute of Biomedical Sciences, Academia Sinica · TWNational Defense Medical Center · TWNational Tsing Hua University · TWNational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sarcomeric signaling complexes are important to sustain proper sarcomere structure and function, however, the mechanisms underlying these processes are not fully elucidated. In a gene trap experiment, we found that vascular cell adhesion protein 1 isoform X2 (VCAP1X2) mutant embryos displayed a dilated cardiomyopathy phenotype, including reduced cardiac contractility, enlarged ventricular chamber and thinned ventricular compact layer. Cardiomyocyte and epicardial cell proliferation was decreased in the mutant heart ventricle, as was the expression of pAKT and pERK. Contractile dysfunction in the mutant was caused by sarcomeric disorganization, including sparse myofilament, blurred Z-disc, and decreased gene expression for sarcomere modulators (smyd1b, mypn and fhl2a), sarcomeric proteins (myh6, myh7, vmhcl and tnnt2a) and calcium regulators (ryr2b and slc8a1a). Treatment of PI3K activator restored Z-disc alignment while injection of smyd1b mRNA restored Z-disc alignment, contractile function and cardiomyocyte proliferation in ventricles of VCAP1X2 mutant embryos. Furthermore, injection of VCAP1X2 variant mRNA rescued all phenotypes, so long as two cytosolic tyrosines were left intact. Our results reveal two tyrosine residues located in the VCAP1X2 cytoplasmic domain are essential to regulate cardiac contractility and the proliferation of ventricular cardiomyocytes and epicardial cells through modulating pAKT and pERK expression levels.

Indexed as

AnimalsCalciumCell ProliferationExtracellular Signal-Regulated MAP KinasesHeart VentriclesMutagenesisMyocardial ContractionMyocytes, CardiacMyofibrilsMyosin Heavy ChainsPhosphorylationProtein IsoformsProto-Oncogene Proteins c-aktSarcomeresSodium-Calcium ExchangerVascular Cell Adhesion Molecule-1CalciumExtracellular Signal-Regulated MAP KinasesMyosin Heavy ChainsProtein IsoformsProto-Oncogene Proteins c-aktSodium-Calcium Exchangersodium-calcium exchanger 1Vascular Cell Adhesion Molecule-1Zebrafish Proteins

Identifiers

PMID29777134
PMCPMC5959901
OpenAlexW2804248830

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.