Evidence map›Paper›PMID 34727990›Full record

ArticleSkeletal muscle2021

Protein profile of fiber types in human skeletal muscle: a single-fiber proteomics study.

Marta Murgia, Leonardo Nogara, Martina Baraldo, Carlo Reggiani, Matthias Mann, Stefano Schiaffino

Open access · goldAbstract read
In one paragraph

Article in Skeletal muscle, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 1 pooled it
9.7field-weighted citation impact, top 1% 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

103 citing papers in PubMed, 1 synthesis or guideline pooled it, 165 citations in OpenAlex.

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43 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

6 authors at 3 institutions in 4 countries.

Marta Murgia *Department of Biomedical Science, University of Padova, 35121, Padova, Italy. mmurgia@biochem.mpg.de.
Leonardo Nogara *Department of Biomedical Science, University of Padova, 35121, Padova, Italy.
Martina BaraldoDepartment of Biomedical Science, University of Padova, 35121, Padova, Italy.
Carlo ReggianiDepartment of Biomedical Science, University of Padova, 35121, Padova, Italy.
Matthias MannDepartment of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Martinsried, Germany.
Stefano SchiaffinoVenetian Institute of Molecular Medicine (VIMM), 35121, Padova, Italy. stefano.schiaffino@unipd.it.ORCID 0000-0002-5607-6421
University of Padua · ITUniversity of Copenhagen · DKVeneto Institute of Molecular Medicine · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHuman skeletal muscle is composed of three major fiber types, referred to as type 1, 2A, and 2X fibers. This heterogeneous cellular composition complicates the interpretation of studies based on whole skeletal muscle lysate. A single-fiber proteomics approach is required to obtain a fiber-type resolved quantitative information on skeletal muscle pathophysiology.

methodsSingle fibers were dissected from vastus lateralis muscle biopsies of young adult males and processed for mass spectrometry-based single-fiber proteomics. We provide and analyze a resource dataset based on relatively pure fibers, containing at least 80% of either MYH7 (marker of slow type 1 fibers), MYH2 (marker of fast 2A fibers), or MYH1 (marker of fast 2X fibers).

resultsIn a dataset of more than 3800 proteins detected by single-fiber proteomics, we selected 404 proteins showing a statistically significant difference among fiber types. We identified numerous type 1 or 2X fiber type-specific protein markers, defined as proteins present at 3-fold or higher levels in these compared to other fiber types. In contrast, we could detect only two 2A-specific protein markers in addition to MYH2. We observed three other major patterns: proteins showing a differential distribution according to the sequence 1 > 2A > 2X or 2X > 2A > 1 and type 2-specific proteins expressed in 2A and 2X fibers at levels 3 times greater than in type 1 fibers. In addition to precisely quantifying known fiber type-specific protein patterns, our study revealed several novel features of fiber type specificity, including the selective enrichment of components of the dystrophin and integrin complexes, as well as microtubular proteins, in type 2X fibers. The fiber type-specific distribution of some selected proteins revealed by proteomics was validated by immunofluorescence analyses with specific antibodies.

conclusionWe here show that numerous muscle proteins, including proteins whose function is unknown, are selectively enriched in specific fiber types, pointing to potential implications in muscle pathophysiology. This reinforces the notion that single-fiber proteomics, together with recently developed approaches to single-cell proteomics, will be instrumental to explore and quantify muscle cell heterogeneity.

Indexed as

Muscle, SkeletalProteomicsHumansMaleMuscle Fibers, SkeletalMuscle ProteinsMuscle ProteinsHuman skeletal muscleMass spectrometryMuscle fiber typesSingle-fiber proteomics

Identifiers

PMID34727990
PMCPMC8561870
OpenAlexW3210336483

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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.