Evidence map›Paper›PMID 24053798›Full record

ArticleBMC cell biology2013

Suppression of protein kinase C theta contributes to enhanced myogenesis in vitro via IRS1 and ERK1/2 phosphorylation.

Joseph S Marino, Terry D Hinds, Rachael A Potter, Eric Ondrus, Jeremy L Onion, Abigail Dowling, Thomas J McLoughlin, Edwin R Sanchez, Jennifer W Hill

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
1.3field-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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  5. Article
  6. Article
  7. Biliverdin reductase isozymes in metabolism.Trends in endocrinology and metabolism: TEM · 2015
    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

9 authors at 1 institution in 1 country.

Joseph S MarinoCenter for Diabetes and Endocrine Research, Department of Physiology and Pharmacology, University of Toledo College of Medicine, Toledo, OH 43614, USA. JenniferW.Hill@utoledo.edu.
Terry D Hinds
Rachael A Potter
Eric Ondrus
Jeremy L Onion
Abigail Dowling
Thomas J McLoughlin
Edwin R Sanchez
Jennifer W Hill
University of Toledo · US

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
TPR Proteins in Steroid Receptor Signaling &PhysiologyR01DK070127 · NIDDK · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI SANCHEZ, EDWIN RAMON · 2005 to 2009
$1.3M
NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK070127
6 · The paper itself

Abstract

backgroundDifferentiation and fusion of skeletal muscle myoblasts into multi-nucleated myotubes is required for neonatal development and regeneration in adult skeletal muscle. Herein, we report novel findings that protein kinase C theta (PKCθ) regulates myoblast differentiation via phosphorylation of insulin receptor substrate-1 and ERK1/2.

resultsIn this study, PKCθ knockdown (PKCθshRNA) myotubes had reduced inhibitory insulin receptor substrate-1 ser1095 phosphorylation, enhanced myoblast differentiation and cell fusion, and increased rates of protein synthesis as determined by [3H] phenylalanine incorporation. Phosphorylation of insulin receptor substrate-1 ser632/635 and extracellular signal-regulated kinase1/2 (ERK1/2) was increased in PKCθshRNA cells, with no change in ERK5 phosphorylation, highlighting a PKCθ-regulated myogenic pathway. Inhibition of PI3-kinase prevented cell differentiation and fusion in control cells, which was attenuated in PKCθshRNA cells. Thus, with reduced PKCθ, differentiation and fusion occur in the absence of PI3-kinase activity. Inhibition of the ERK kinase, MEK1/2, impaired differentiation and cell fusion in control cells. Differentiation was preserved in PKCθshRNA cells treated with a MEK1/2 inhibitor, although cell fusion was blunted, indicating PKCθ regulates differentiation via IRS1 and ERK1/2, and this occurs independently of MEK1/2 activation.

conclusionCellular signaling regulating the myogenic program and protein synthesis are complex and intertwined. These studies suggest that PKCθ regulates myogenic and protein synthetic signaling via the modulation of IRS1and ERK1/2 phosphorylation. Myotubes lacking PKCθ had increased rates of protein synthesis and enhanced myotube development despite reduced activation of the canonical anabolic-signaling pathway. Further investigation of PKCθ regulated signaling may reveal important interactions regulating skeletal muscle health in an insulin resistant state.

Indexed as

AnimalsCell DifferentiationCell FusionCells, CulturedGene Expression Regulation, DevelopmentalInsulin Receptor Substrate ProteinsIsoenzymesMAP Kinase Kinase 1MAP Kinase Kinase 2MiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Muscle DevelopmentMuscle Fibers, SkeletalMyoblastsPhosphatidylinositol 3-KinasesInsulin Receptor Substrate ProteinsIrs1 protein, mouseIsoenzymesMap2k1 protein, mouseMap2k2 protein, mouseMAP Kinase Kinase 1MAP Kinase Kinase 2Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Phosphatidylinositol 3-KinasesPrkcq protein, mouseProtein Kinase CProtein Kinase C-thetaProtein Kinase InhibitorsRNA, Small Interfering

Identifiers

PMID24053798
PMCPMC3848841
OpenAlexW2142542740

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.