Evidence map›Paper›PMID 19833877›Full record

ArticleDiabetes2010

Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes.

Hyonson Hwang, Benjamin P Bowen, Natalie Lefort, Charles R Flynn, Elena A De Filippis, Christine Roberts, Christopher C Smoke, Christian Meyer, Kurt Højlund, Zhengping Yi and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Diabetes, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed, 2 pooled it
6.7field-weighted citation impact, top 3% 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

142 citing papers in PubMed, 2 syntheses or guidelines pooled it, 257 citations in OpenAlex.

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  16. SERCA blockade as a treatment strategy for obesity.European journal of applied physiology · 2025
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82 more citing papers are in PubMed but not listed here.

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

11 authors at 1 institution in 2 countries.

Hyonson HwangCenter for Metabolic Biology, Arizona State University, Tempe, Arizona, USA.
Benjamin P Bowen
Natalie Lefort
Charles R Flynn
Elena A De Filippis
Christine Roberts
Christopher C Smoke
Christian Meyer
Kurt Højlund
Zhengping Yi
Lawrence J Mandarino
Arizona State University · US

Funding

MOLECULAR REGULATION OF MUSCLE GLUCOSE METABOLISM IN MANR01DK047936 · NIDDK · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI MANDARINO, LAWRENCE J · 1994 to 2022
$10.7M
PGC-1 & Muscle Mitochondrial Dysfunction in DiabetesR01DK066483 · NIDDK · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI MANDARINO, LAWRENCE J · 2004 to 2018
$6.7M
Human Skeletal Muscle Proteome and Phosphoproteome in Obesity and Type 2 DiabetesR01DK081750 · NIDDK · WAYNE STATE UNIVERSITY · PI YI, ZHENGPING · 2009 to 2017
$3.0M
NIDDK NIH HHS R01 DK047936NIDDK NIH HHS R01 DK066483NIDDK NIH HHS R01 DK081750NIDDK NIH HHS R01DK081750NIDDK NIH HHS R01DK47936NIDDK NIH HHS R01DK66483
6 · The paper itself

Abstract

objectiveInsulin resistance in skeletal muscle is an early phenomenon in the pathogenesis of type 2 diabetes. Studies of insulin resistance usually are highly focused. However, approaches that give a more global picture of abnormalities in insulin resistance are useful in pointing out new directions for research. In previous studies, gene expression analyses show a coordinated pattern of reduction in nuclear-encoded mitochondrial gene expression in insulin resistance. However, changes in mRNA levels may not predict changes in protein abundance. An approach to identify global protein abundance changes involving the use of proteomics was used here. RESEARCH DESIGN AND

methodsMuscle biopsies were obtained basally from lean, obese, and type 2 diabetic volunteers (n = 8 each); glucose clamps were used to assess insulin sensitivity. Muscle protein was subjected to mass spectrometry-based quantification using normalized spectral abundance factors.

resultsOf 1,218 proteins assigned, 400 were present in at least half of all subjects. Of these, 92 were altered by a factor of 2 in insulin resistance, and of those, 15 were significantly increased or decreased by ANOVA (P < 0.05). Analysis of protein sets revealed patterns of decreased abundance in mitochondrial proteins and altered abundance of proteins involved with cytoskeletal structure (desmin and alpha actinin-2 both decreased), chaperone function (TCP-1 subunits increased), and proteasome subunits (increased).

conclusionsThe results confirm the reduction in mitochondrial proteins in insulin-resistant muscle and suggest that changes in muscle structure, protein degradation, and folding also characterize insulin resistance.

Indexed as

AdultBiopsyBody Mass IndexChaperonin Containing TCP-1ChaperoninsCytoskeletal ProteinsDiabetes Mellitus, Type 2FemaleGene Expression ProfilingGlucose Clamp TechniqueHumansMaleMass SpectrometryMiddle AgedMitochondria, MuscleMuscle, SkeletalChaperonin Containing TCP-1ChaperoninsCytoskeletal ProteinsPeptide HydrolasesTCP1 protein, human

Identifiers

PMID19833877
PMCPMC2797941
OpenAlexW2160330411

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.