Evidence map›Paper›PMID 19764811›Full record

ArticleJournal of proteome research2009

In vivo phosphoproteome of human skeletal muscle revealed by phosphopeptide enrichment and HPLC-ESI-MS/MS.

Kurt Højlund, Benjamin P Bowen, Hyonson Hwang, Charles R Flynn, Lohith Madireddy, Thangiah Geetha, Paul Langlais, Christian Meyer, Lawrence J Mandarino, Zhengping Yi

Abstract read
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 81 citations in OpenAlex.

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  14. Serine-47 phosphorylation of cytochromeFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
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  17. Tissue-specific regulation of cytochrome c by post-translational modifications: respiration, the mitochondrial membrane potential, ROS, and apoptosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Review
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  20. Non-alcoholic fatty liver disease phosphoproteomics: A functional piece of the precision puzzle.Hepatology research : the official journal of the Japan Society of Hepatology · 2017
    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

10 authors at 3 institutions in 2 countries.

Kurt HøjlundCenter for Metabolic Biology, Arizona State University, Tempe, Arizona 85287-3704, USA.
Benjamin P Bowen
Hyonson Hwang
Charles R Flynn
Lohith Madireddy
Thangiah Geetha
Paul Langlais
Christian Meyer
Lawrence J Mandarino
Zhengping Yi
Arizona State University · USOdense University Hospital · DKUniversity of Southern Denmark · DK

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 R01DK66483
6 · The paper itself

Abstract

Protein phosphorylation plays an essential role in signal transduction pathways that regulate substrate and energy metabolism, contractile function, and muscle mass in human skeletal muscle. Abnormal phosphorylation of signaling enzymes has been identified in insulin-resistant muscle using phosphoepitope-specific antibodies, but its role in other skeletal muscle disorders remains largely unknown. This may be in part due to insufficient knowledge of relevant targets. Here, we therefore present the first large-scale in vivo phosphoproteomic study of human skeletal muscle from 3 lean, healthy volunteers. Trypsin digestion of 3-5 mg human skeletal muscle protein was followed by phosphopeptide enrichment using SCX and TiO(2). The resulting phosphopeptides were analyzed by HPLC-ESI-MS/MS. Using this unbiased approach, we identified 306 distinct in vivo phosphorylation sites in 127 proteins, including 240 phosphoserines, 53 phosphothreonines, and 13 phosphotyrosines in at least 2 out of 3 subjects. In addition, 61 ambiguous phosphorylation sites were identified in at least 2 out of 3 subjects. The majority of phosphoproteins detected are involved in sarcomeric function, excitation-contraction coupling (the Ca(2+)-cycle), glycolysis, and glycogen metabolism. Of particular interest, we identified multiple novel phosphorylation sites on several sarcomeric Z-disk proteins known to be involved in signaling and muscle disorders. These results provide numerous new targets for the investigation of human skeletal muscle phosphoproteins in health and disease and demonstrate feasibility of phosphoproteomics research of human skeletal muscle in vivo.

Indexed as

AdultAmino Acid SequenceChromatography, High Pressure LiquidComputational BiologyHumansMaleMiddle AgedMolecular Sequence DataMuscle ProteinsMuscle, SkeletalPhosphopeptidesPhosphorylationProteomeProteomicsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryMuscle ProteinsPhosphopeptidesProteome

Identifiers

PMID19764811
PMCPMC2783959
OpenAlexW2025702673

What Socratic 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 Socratic graph.