Evidence map›Paper›PMID 35113304›Full record

ArticleMolecular biology reports2022

Lysine demethylase 3A is a positive regulator of cardiac myofibroblast transdifferentiation that increases Smad3 phosphorylation following transforming growth factor beta1 stimulation.

Xiaopei Liu, Jining Zhou, Bofang Zhang, Gen Liu, Qi Hu, Jing Chen

Abstract read
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In one paragraph

Article in Molecular biology reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

6 authors at 1 institution in 1 country.

Xiaopei Liu *Department of Cardiology, Renmin Hospital of Wuhan University; Cardiovascular Research Institute, Wuhan University, Hubei Key Laboratory of Cardiology, Wuhan, 430000, Hubei, People's Republic of China.
Jining Zhou *Department of Cardiology, Renmin Hospital of Wuhan University; Cardiovascular Research Institute, Wuhan University, Hubei Key Laboratory of Cardiology, Wuhan, 430000, Hubei, People's Republic of China.
Bofang ZhangDepartment of Cardiology, Renmin Hospital of Wuhan University; Cardiovascular Research Institute, Wuhan University, Hubei Key Laboratory of Cardiology, Wuhan, 430000, Hubei, People's Republic of China.
Gen LiuDepartment of Cardiology, Renmin Hospital of Wuhan University; Cardiovascular Research Institute, Wuhan University, Hubei Key Laboratory of Cardiology, Wuhan, 430000, Hubei, People's Republic of China.
Qi HuDepartment of Cardiology, Renmin Hospital of Wuhan University; Cardiovascular Research Institute, Wuhan University, Hubei Key Laboratory of Cardiology, Wuhan, 430000, Hubei, People's Republic of China.
Jing ChenDepartment of Cardiology, Renmin Hospital of Wuhan University; Cardiovascular Research Institute, Wuhan University, Hubei Key Laboratory of Cardiology, Wuhan, 430000, Hubei, People's Republic of China. chenjing1982@whu.edu.cn.ORCID http://orcid.org/0000-0002-4037-7158
Wuhan University · CN

Funding

National Natural Science Foundation of China 81570331Natural Science Foundation of Hubei Province 2018CFB240Natural Science Foundation of Hubei Province 2021CFB334
6 · The paper itself

Abstract

backgroundThe epigenetic modifier molecule lysine demethylase 3A (KDM3A) has been shown to help ameliorate cardiovascular diseases, but its effect on cardiac fibroblasts (CFs) remains unclear. METHODS AND

resultsWe designed gain- and loss-of-function experiments to investigate the biological functions of KDM3A in CFs. Moreover, we used SIS3-HCl (a specific inhibitor of p-Smad3) to explore the underlying mechanism. Cell viability and migration were verified by CCK-8 and cell migration experiments, respectively, and the degree of fibrosis was measured by Western blot analysis. Our data revealed that KDM3A enhanced the proliferation and migration of CFs and increased the fibroblast-to-myofibroblast transition while enabling the Smad3 phosphorylation response to transforming growth factor beta1 (TGFβ1) stimulation. However, these effects were abolished by SIS3-HCl. Furthermore, KDM3A inhibition obviously protected against cardiac myofibroblast transdifferentiation under TGFβ1 stimulation.

conclusionsKDM3A may act as a novel regulator of cardiac myofibroblast transdifferentiation through its ability to modulate the phosphorylation of Smad3 following TGFβ1 stimulation.

Indexed as

MyofibroblastsTransforming Growth Factor beta1Cell TransdifferentiationFibroblastsLysinePhosphorylationSmad3 ProteinTransforming Growth Factor betaLysineSmad3 ProteinTransforming Growth Factor betaTransforming Growth Factor beta1Cardiac fibrosisFibroblast-to-myofibroblast transitionKDM3ASmad3

Identifiers

PMID35113304
OpenAlexW4210721234

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.