Evidence map›Paper›PMID 26010327›Full record

ArticleObesity (Silver Spring, Md.)2015

Skeletal muscle myotubes in severe obesity exhibit altered ubiquitin-proteasome and autophagic/lysosomal proteolytic flux.

Lance M Bollinger, Jonathan J S Powell, Joseph A Houmard, Carol A Witczak, Jeffrey J Brault

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Obesity (Silver Spring, Md.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

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  20. Mitochondrial Function in Muscle Stem Cell Fates.Frontiers in cell and developmental biology · 2020
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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

5 authors at 1 institution in 1 country.

Lance M BollingerDepartment of Kinesiology, Human Performance Lab, College of Health and Human Performance, East Carolina University, Greenville, North Carolina, USA.
Jonathan J S PowellDepartment of Kinesiology, Human Performance Lab, College of Health and Human Performance, East Carolina University, Greenville, North Carolina, USA.
Joseph A HoumardDepartment of Kinesiology, Human Performance Lab, College of Health and Human Performance, East Carolina University, Greenville, North Carolina, USA.
Carol A WitczakDepartment of Kinesiology, Human Performance Lab, College of Health and Human Performance, East Carolina University, Greenville, North Carolina, USA.
Jeffrey J BraultDepartment of Kinesiology, Human Performance Lab, College of Health and Human Performance, East Carolina University, Greenville, North Carolina, USA.
East Carolina University · US

Funding

LIPID METABOLISM IN OBESITY, WEIGHT LOSS AND EXERCISER01DK056112 · NIDDK · EAST CAROLINA UNIVERSITY · PI HOUMARD, JOSEPH A · 2000 to 2016
$4.5M
Role of Ca2+/calmodulin kinases in skeletal muscle glucose transport and growth.R00AR056298 · NIAMS · EAST CAROLINA UNIVERSITY · PI WITCZAK, CAROL ANN · 2011 to 2013
$735k
NIAMS NIH HHS R00-AR05629NIAMS NIH HHS R00 AR056298NIDDK NIH HHS R01 DK056112NIDDK NIH HHS R01-DK56112
6 · The paper itself

Abstract

objectiveWhole-body protein metabolism is dysregulated with obesity. The goal of the study was to determine whether activity and expression of major protein degradation pathways are compromised specifically in human skeletal muscle with obesity.

methodsPrimary human skeletal muscle (HSkM) cell cultures were utilized since cellular mechanisms can be studied absent of hormones and contractile activity that could independently influence metabolism. HSkM from 10 lean women (BMI ≤ 26.0 kg/m(2) ) and 8 women with severe obesity (BMI ≥ 39.0) were examined basally and when stimulated to atrophy (serum and amino acid starvation).

resultsHSkM from obese donors had a lower proportion of type I myosin heavy chain and slower flux through the autophagic/lysosomal pathway. During starvation, flux through the ubiquitin-proteasome system diverged according to obesity status, with a decrease in lean subjects and an increase in HSkM from subjects with obesity. HSkM in obesity also displayed elevated proteasome activity despite no difference in proteasome content. Atrophy-related gene expression and myotube area were similar in myotubes derived from individuals with and without obesity under basal and starved conditions.

conclusionsOur data indicate that muscle cells in lean individuals and in those with severe obesity have innate differences in management of protein degradation, which may explain their metabolic differences.

Indexed as

AutophagyAdultCell Culture TechniquesFemaleGene ExpressionHumansLysosomesMuscle Fibers, SkeletalMuscle, SkeletalObesity, MorbidProteasome Endopeptidase ComplexReal-Time Polymerase Chain ReactionUbiquitinYoung AdultProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID26010327
PMCPMC4445474
OpenAlexW1905520651

What OpenQuestion holds

Textmetadata
LicenceTDM
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.