Evidence map›Paper›PMID 26468734›Full record

ArticleScientific reports2015

Co-activator binding protein PIMT mediates TNF-α induced insulin resistance in skeletal muscle via the transcriptional down-regulation of MEF2A and GLUT4.

Vasundhara Kain, Bandish Kapadia, Navin Viswakarma, Sriram Seshadri, Bhumika Prajapati, Prasant K Jena, Chandana Lakshmi Teja Meda, Maitreyi Subramanian, Sashidhara Kaimal Suraj, Sireesh T Kumar and 5 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  14. Environmental Enrichment Potently Prevents Microglia-Mediated Neuroinflammation by Human Amyloid β-Protein Oligomers.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
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  15. 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

15 authors at 4 institutions in 2 countries.

Vasundhara KainDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
Bandish KapadiaDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
Navin ViswakarmaDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
Sriram SeshadriInstitute of Science, Nirma University, Sarkhej-Gandhinagar Highway, Ahmedabad, Gujarat, India.
Bhumika PrajapatiInstitute of Science, Nirma University, Sarkhej-Gandhinagar Highway, Ahmedabad, Gujarat, India.
Prasant K JenaInstitute of Science, Nirma University, Sarkhej-Gandhinagar Highway, Ahmedabad, Gujarat, India.
Chandana Lakshmi Teja MedaDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
Maitreyi SubramanianDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
Sashidhara Kaimal SurajDepartment of Biotechnology, School of Life Sciences, University of Hyderabad, Hyderabad, Telangana, India.
Sireesh T KumarDepartment of Biotechnology, School of Life Sciences, University of Hyderabad, Hyderabad, Telangana, India.
Phanithi Prakash BabuDepartment of Biotechnology, School of Life Sciences, University of Hyderabad, Hyderabad, Telangana, India.
Bayar ThimmapayaDepartment of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, United States of America.
Janardan K ReddyDepartment of Pathology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, United States of America.
Kishore V L ParsaDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
Parimal MisraDepartment of Biology, Dr. Reddy's Institute of Life Sciences, University of Hyderabad Campus, Hyderabad, Telangana, India.
University of Hyderabad · INNirma University · INInstitute of Life Sciences · INNorthwestern University · US

Funding

Transcriptional Coactivators in Liver FunctionR01DK083163 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI REDDY, JANARDAN K. · 2009 to 2013
$1.7M
Med1 in Liver Metabolism, Regeneration and CancerR01DK097249 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI JIA, YUZHI, REDDY, JANARDAN K. · 2013 to 2017
$1.7M
NIDDK NIH HHS R01 DK083163NIDDK NIH HHS R01 DK097249
6 · The paper itself

Abstract

The mechanisms underlying inflammation induced insulin resistance are poorly understood. Here, we report that the expression of PIMT, a transcriptional co-activator binding protein, was up-regulated in the soleus muscle of high sucrose diet (HSD) induced insulin resistant rats and TNF-α exposed cultured myoblasts. Moreover, TNF-α induced phosphorylation of PIMT at the ERK1/2 target site Ser(298). Wild type (WT) PIMT or phospho-mimic Ser298Asp mutant but not phospho-deficient Ser298Ala PIMT mutant abrogated insulin stimulated glucose uptake by L6 myotubes and neonatal rat skeletal myoblasts. Whereas, PIMT knock down relieved TNF-α inhibited insulin signaling. Mechanistic analysis revealed that PIMT differentially regulated the expression of GLUT4, MEF2A, PGC-1α and HDAC5 in cultured cells and skeletal muscle of Wistar rats. Further characterization showed that PIMT was recruited to GLUT4, MEF2A and HDAC5 promoters and overexpression of PIMT abolished the activity of WT but not MEF2A binding defective mutant GLUT4 promoter. Collectively, we conclude that PIMT mediates TNF-α induced insulin resistance at the skeletal muscle via the transcriptional modulation of GLUT4, MEF2A, PGC-1α and HDAC5 genes.

Indexed as

AnimalsBlood GlucoseCells, CulturedDown-RegulationGlucose Transporter Type 4HEK293 CellsHistone DeacetylasesHumansInsulin ResistanceMaleMEF2 Transcription FactorsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Myoblasts, SkeletalPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPhosphorylationBlood GlucoseGlucose Transporter Type 4Hdac5 protein, ratHistone DeacetylasesMEF2A protein, ratMEF2 Transcription FactorsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaPpargc1a protein, ratProtein D-Aspartate-L-Isoaspartate MethyltransferaseTranscription FactorsTumor Necrosis Factor-alpha

Identifiers

PMID26468734
PMCPMC4606566
OpenAlexW2426939044

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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.