Evidence map›Paper›PMID 28803268›Full record

ArticleJournal of muscle research and cell motility2017

Proteomic profiling of the dystrophin complex and membrane fraction from dystrophic mdx muscle reveals decreases in the cytolinker desmoglein and increases in the extracellular matrix stabilizers biglycan and fibronectin.

Sandra Murphy, Heinrich Brinkmeier, Mirjam Krautwald, Michael Henry, Paula Meleady, Kay Ohlendieck

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In one paragraph

Article in Journal of muscle research and cell motility, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Serum protein biomarker signature of Duchenne muscular dystrophy.European journal of translational myology · 2025
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  8. Identification of Subproteomic Markers for Skeletal Muscle Profiling.Methods in molecular biology (Clifton, N.J.) · 2023
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  9. Review
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  17. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  18. Article
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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

6 authors at 3 institutions in 2 countries.

Sandra MurphyDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, County Kildare, Ireland.
Heinrich BrinkmeierInstitute of Pathophysiology, University Medicine Greifswald, 17495, Karlsburg, Germany.
Mirjam KrautwaldInstitute of Pathophysiology, University Medicine Greifswald, 17495, Karlsburg, Germany.
Michael HenryNational Institute for Cellular Biotechnology, Dublin City University, Dublin 9, Ireland.
Paula MeleadyNational Institute for Cellular Biotechnology, Dublin City University, Dublin 9, Ireland.
Kay OhlendieckDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, County Kildare, Ireland. kay.ohlendieck@mu.ie.ORCID 0000-0002-6266-4510
Dublin City University · IENational University of Ireland, Maynooth · IEUniversitätsmedizin Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The almost complete loss of the membrane cytoskeletal protein dystrophin and concomitant drastic reduction in dystrophin-associated glycoproteins are the underlying mechanisms of the highly progressive neuromuscular disorder Duchenne muscular dystrophy. In order to identify new potential binding partners of dystrophin or proteins in close proximity to the sarcolemmal dystrophin complex, proteomic profiling of the isolated dystrophin-glycoprotein complex was carried out. Subcellular membrane fractionation and detergent solubilisation, in combination with ion exchange, lectin chromatography and density gradient ultracentrifugation, was performed to isolate a dystrophin complex-enriched fraction. Following gradient gel electrophoresis and on-membrane digestion, the protein constituents of the dystrophin fraction were determined by peptide mass spectrometry. This proteomic strategy resulted in the novel identification of desmoglein and desmoplakin, which act as cytolinker proteins and possibly exist in close proximity to the dystrophin complex in the sarcolemma membrane. Interestingly, comparative immunoblotting showed a significant reduction in desmoglein in dystrophin-deficient mdx skeletal muscles, reminiscent of the pathobiochemical fate of the dystrophin-associated core proteins in muscular dystrophy. Comparative membrane proteomics was used to correlate this novel finding to large-scale changes in the dystrophic phenotype. A drastic increase in the extracellular stabilizers biglycan and fibronectin was shown by both mass spectrometric analysis and immunoblotting. The reduced expression of desmoglein in dystrophin-deficient skeletal muscles, and simultaneous increase in components of the extracellular matrix, suggest that muscular dystrophy is associated with plasmalemmal disintegration, loss of cellular linkage and reactive myofibrosis.

Indexed as

AnimalsBiglycanChromatography, LiquidDesmogleinsDystrophinFibronectinsMass SpectrometryMiceProteomicsBiglycanDesmogleinsDystrophinFibronectinsBiglycanDesmogleinDesmoplakinDystrophinDystrophinopathyFibronectin

Identifiers

PMID28803268
OpenAlexW2744859841

What OpenQuestion holds

Textmetadata
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.