Evidence map›Paper›PMID 25031892›Full record

ArticleEndocrinology and metabolism (Seoul, Korea)2014

A Novel Cytosolic Isoform of Mitochondrial Trans-2-Enoyl-CoA Reductase Enhances Peroxisome Proliferator-Activated Receptor α Activity.

Dong-Gyu Kim, Jae Cheal Yoo, Eunju Kim, Young-Sun Lee, Oleg V Yarishkin, Da Yong Lee, Kun Ho Lee, Seong-Geun Hong, Eun Mi Hwang, Jae-Yong Park

Open access · diamondAbstract read
In one paragraph

Article in Endocrinology and metabolism (Seoul, Korea), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  14. Exploration of targets regulated by miR-125b in porcine adipocytes.In vitro cellular & developmental biology. Animal · 2020
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  18. Articles in 'endocrinology and metabolism' in 2014.Endocrinology and metabolism (Seoul, Korea) · 2015
    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

10 authors at 1 institution in 1 country.

Dong-Gyu KimDepartment of Physiology, Institute of Health Science, Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine, Jinju, Korea.
Jae Cheal YooDepartment of Physiology, Institute of Health Science, Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine, Jinju, Korea.
Eunju KimCenter for Functional Connectomics, Korea Institute of Science and Technology, Seoul, Korea.
Young-Sun LeeDepartment of Physiology, Institute of Health Science, Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine, Jinju, Korea.
Oleg V YarishkinCenter for Functional Connectomics, Korea Institute of Science and Technology, Seoul, Korea.
Da Yong LeeCenter for Functional Connectomics, Korea Institute of Science and Technology, Seoul, Korea.
Kun Ho LeeDepartment of Marine Life Science, Chosun University College of Natural Sciences, Gwangju, Korea.
Seong-Geun HongDepartment of Physiology, Institute of Health Science, Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine, Jinju, Korea.
Eun Mi HwangCenter for Functional Connectomics, Korea Institute of Science and Technology, Seoul, Korea.
Jae-Yong ParkDepartment of Physiology, Institute of Health Science, Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine, Jinju, Korea. ; Center for Functional Connectomics, Korea Institute of Science and Technology, Seoul, Korea.
Korea Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMitochondrial trans-2-enoyl-CoA reductase (MECR) is involved in mitochondrial synthesis of fatty acids and is highly expressed in mitochondria. MECR is also known as nuclear receptor binding factor-1, which was originally reported with yeast two-hybrid screening as a binding protein of the nuclear hormone receptor peroxisome proliferator-activated receptor α (PPARα). However, MECR and PPARα are localized at different compartment, mitochondria, and the nucleus, respectively. Therefore, the presence of a cytosolic or nuclear isoform of MECR is necessary for functional interaction between MECR and PPARα.

methodsTo identify the expression pattern of MECR and the cytosolic form of MECR (cMECR), we performed reverse transcription polymerase chain reaction (RT-PCR) with various tissue samples from Sprague-Dawley rats. To confirm the interaction between cMECR and PPARα, we performed several binding assays such as yeast two-hybrid, coimmunoprecipitation, and bimolecular fluorescence complementation. To observe subcellular localization of these proteins, immunocytochemistry was performed. A luciferase assay was used to measure PPARα activity.

resultsWe provide evidence of an alternatively spliced variant of the rat MECR gene that yields cMECR. The cMECR lacks the N-terminal 76 amino acids of MECR and shows uniform distribution in the cytoplasm and nucleus of HeLa cells. cMECR directly bound PPARα in the nucleus and increased PPARα-dependent luciferase activity in HeLa cells.

conclusionWe found the cytosolic form of MECR (cMECR) was expressed in the cytosolic and/or nuclear region, directly binds with PPARα, and enhances PPARα activity.

Indexed as

Alternative splicingCytosolic mitochondrial trans-2-enoyl-CoA reductaseMitochondrial targeting sequencesPPAR alphaTrans-2-enoyl-CoA reductase (NADPH)

Identifiers

PMID25031892
PMCPMC4091492
OpenAlexW2158034689

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.