Evidence map›Paper›PMID 26875982›Full record

ArticleInternational journal of molecular sciences2016

Overexpression of Glucocorticoid Receptor β Enhances Myogenesis and Reduces Catabolic Gene Expression.

Terry D Hinds, Bailey Peck, Evan Shek, Steven Stroup, Jennifer Hinson, Susan Arthur, Joseph S Marino

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

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  10. FKBP51 and the molecular chaperoning of metabolism.Trends in endocrinology and metabolism: TEM · 2021
    Review
  11. Review
  12. Glucocorticoid Receptor β (GRβ): Beyond Its Dominant-Negative Function.International journal of molecular sciences · 2021
    Review
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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 2 institutions in 1 country.

Terry D HindsCenter for Hypertension and Personalized Medicine, Department of Physiology and Pharmacology, University of Toledo College of Medicine, Toledo, OH 43614, USA. terry.hinds@utoledo.edu.
Bailey PeckLaboratory of Systems Physiology, Department of Kinesiology, University of North Carolina Charlotte, Charlotte, NC 28223, USA. bpeck3@uncc.edu.
Evan ShekLaboratory of Systems Physiology, Department of Kinesiology, University of North Carolina Charlotte, Charlotte, NC 28223, USA. eshek@uncc.edu.
Steven StroupLaboratory of Systems Physiology, Department of Kinesiology, University of North Carolina Charlotte, Charlotte, NC 28223, USA. sstroup4@uncc.edu.
Jennifer HinsonLaboratory of Systems Physiology, Department of Kinesiology, University of North Carolina Charlotte, Charlotte, NC 28223, USA. jhinso47@uncc.edu.
Susan ArthurLaboratory of Systems Physiology, Department of Kinesiology, University of North Carolina Charlotte, Charlotte, NC 28223, USA. sarthur8@uncc.edu.
Joseph S MarinoLaboratory of Systems Physiology, Department of Kinesiology, University of North Carolina Charlotte, Charlotte, NC 28223, USA. jmarin10@uncc.edu.
University of North Carolina at Charlotte · USUniversity of Toledo · US

Funding

Antioxidant-PPARalpha interaction and hypertensionK01HL125445 · NHLBI · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI HINDS, TERRY D · 2015 to 2019
$779k
NHLBI NIH HHS K01 HL125445NHLBI NIH HHS K01HL125445NIMHD NIH HHS L32 MD009154NIMHD NIH HHS L32MD009154PHS HHS L106365
6 · The paper itself

Abstract

Unlike the glucocorticoid receptor α (GRα), GR β (GRβ) has a truncated ligand-binding domain that prevents glucocorticoid binding, implicating GRα as the mediator of glucocorticoid-induced skeletal muscle loss. Because GRβ causes glucocorticoid resistance, targeting GRβ may be beneficial in impairing muscle loss as a result of GRα activity. The purpose of this study was to determine how the overexpression of GRβ affects myotube formation and dexamethasone (Dex) responsiveness. We measured GR isoform expression in C₂C12 muscle cells in response to Dex and insulin, and through four days of myotube formation. Next, lentiviral-mediated overexpression of GRβ in C₂C12 was performed, and these cells were characterized for cell fusion and myotube formation, as well as sensitivity to Dex via the expression of ubiquitin ligases. GRβ overexpression increased mRNA levels of muscle regulatory factors and enhanced proliferation in myoblasts. GRβ overexpressing myotubes had an increased fusion index. Myotubes overexpressing GRβ had lower forkhead box O3 (Foxo3a) mRNA levels and a blunted muscle atrophy F-box/Atrogen-1 (MAFbx) and muscle ring finger 1 (MuRF1) response to Dex. We showed that GRβ may serve as a pharmacological target for skeletal muscle growth and protection from glucocorticoid-induced catabolic signaling. Increasing GRβ levels in skeletal muscle may cause a state of glucocorticoid resistance, stabilizing muscle mass during exposure to high doses of glucocorticoids.

Indexed as

Gene ExpressionAnimalsCell DifferentiationCell LineDexamethasoneEnergy MetabolismGene Expression RegulationInsulinMiceMuscle DevelopmentMuscle Fibers, SkeletalMyoblastsProtein IsoformsReceptors, GlucocorticoidRNA, MessengerDexamethasoneglucocorticoid receptor betaInsulinProtein IsoformsReceptors, GlucocorticoidRNA, Messengeratrophy 6dexamethasone 9glucocorticoid receptor α 2glucocorticoid receptor β 3GRα 5GRβ 4MAFbx 7MuRF1 8myogenesis

Identifiers

PMID26875982
PMCPMC4783964
OpenAlexW2260590380

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.