Evidence map›Paper›PMID 29595878›Full record

ArticlePhysiological reports2018

AKT2 is the predominant AKT isoform expressed in human skeletal muscle.

Ronald W Matheny, Alyssa V Geddis, Mary N Abdalla, Luis A Leandry, Michael Ford, Holly L McClung, Stefan M Pasiakos

Open access · goldAbstract read
In one paragraph

Article in Physiological reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  11. The dose-response effects of arachidonic acid on primary human skeletal myoblasts and myotubes.Journal of the International Society of Sports Nutrition · 2023
    Article
  12. Review
  13. Insulin Signal Transduction Perturbations in Insulin Resistance.International journal of molecular sciences · 2021
    Review
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  17. Article
  18. Germline or inducible knockout of p300 or CBP in skeletal muscle does not alter insulin sensitivity.American journal of physiology. Endocrinology and metabolism · 2019
    Article
  19. Review
  20. 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

7 authors at 2 institutions in 1 country.

Ronald W MathenyMilitary Performance Division, US Army Research Institute of Environmental Medicine, Natick, Massachusetts.
Alyssa V GeddisMilitary Performance Division, US Army Research Institute of Environmental Medicine, Natick, Massachusetts.
Mary N AbdallaMilitary Performance Division, US Army Research Institute of Environmental Medicine, Natick, Massachusetts.
Luis A LeandryMilitary Performance Division, US Army Research Institute of Environmental Medicine, Natick, Massachusetts.
Michael FordMS Bioworks, Ann Arbor, Michigan.
Holly L McClungMilitary Nutrition Division, US Army Research Institute of Environmental Medicine, Natick, Massachusetts.
Stefan M PasiakosMilitary Nutrition Division, US Army Research Institute of Environmental Medicine, Natick, Massachusetts.
U.S. Army Research Institute of Environmental Medicine · USBioWorks (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skeletal muscle physiology and metabolism are regulated by complex networks of intracellular signaling pathways. Among many of these pathways, the protein kinase AKT plays a prominent role. While three AKT isoforms have been identified (AKT1, AKT2, and AKT3), surprisingly little is known regarding isoform-specific expression of AKT in human skeletal muscle. To address this, we examined the expressions of each AKT isoform in muscle biopsy samples collected from the vastus lateralis of healthy male adults at rest. In muscle, AKT2 was the most highly expressed AKT transcript, exhibiting a 15.4-fold increase over AKT1 and AKT3 transcripts. Next, the abundance of AKT protein isoforms was determined using antibody immunoprecipitation followed by Liquid Chromatography-Parallel Reaction Monitoring/Mass Spectrometry. Immunoprecipitation was performed using either mouse or rabbit pan AKT antibodies that were immunoreactive with all three AKT isoforms. We found that AKT2 was the most abundant AKT isoform in human skeletal muscle (4.2-fold greater than AKT1 using the rabbit antibody and 1.6-fold greater than AKT1 using the mouse antibody). AKT3 was virtually undetectable. Next, cultured primary human myoblasts were virally-transduced with cDNAs encoding either wild-type (WT) or kinase-inactive AKT1 (AKT1-K179M) or AKT2 (AKT2-K181M) and allowed to terminally differentiate. Myotubes expressing WT-AKT1 or WT-AKT2 showed enhanced fusion compared to control myotubes, while myotubes expressing AKT1-K179M showed a 14% reduction in fusion. Myotubes expressing AKT2-K181M displayed 63% decreased fusion compared to control. Together, these data identify AKT2 as the most highly-expressed AKT isoform in human skeletal muscle and as the principal AKT isoform regulating human myoblast differentiation.

Indexed as

AdultCell DifferentiationHumansIsoenzymesMaleMuscle, SkeletalMyoblasts, SkeletalProto-Oncogene Proteins c-aktAKT2 protein, humanIsoenzymesProto-Oncogene Proteins c-aktAKTdifferentiationmyoblastskeletal muscle

Identifiers

PMID29595878
PMCPMC5875533
OpenAlexW2795539580

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.