ArticleBiology2015
Simultaneous Pathoproteomic Evaluation of the Dystrophin-Glycoprotein Complex and Secondary Changes in the mdx-4cv Mouse Model of Duchenne Muscular Dystrophy.
Article in Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- A 3D skeletal muscle system for disease modelling and secretome profiling of Duchenne muscular dystrophy.Skeletal muscle · 2026Article
- Label-free proteomic analysis of Duchenne and Becker muscular dystrophy showed decreased sarcomere proteins and increased ubiquitination-related proteins.Scientific reports · 2025Article
- Improvement in the sensitivity of LA-ICP-MS bioimaging by addition of nitrogen to the argon carrier gas.Journal of analytical atomic spectrometry · 2024Article
- How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?Proteomes · 2024Article
- Proteomic profiling of impaired excitation-contraction coupling and abnormal calcium handling in muscular dystrophy.Proteomics · 2022Review
- Proteomic Identification of Markers of Membrane Repair, Regeneration and Fibrosis in the Aged and Dystrophic Diaphragm.Life (Basel, Switzerland) · 2022Article
- Histopathology of Duchenne muscular dystrophy in correlation with changes in proteomic biomarkers.Histology and histopathology · 2022Review
- Review
- Quantitative immuno-mass spectrometry imaging of skeletal muscle dystrophin.Scientific reports · 2021Article
- Proteomic profiling of the mouse diaphragm and refined mass spectrometric analysis of the dystrophic phenotype.Journal of muscle research and cell motility · 2019Article
- Dataset on the comparative proteomic profiling of mouse saliva and serum from wild type versus the dystrophicData in brief · 2018Article
- Comparative gel-based proteomic analysis of chemically crosslinked complexes in dystrophic skeletal muscle.Electrophoresis · 2018Article
- Subproteomic profiling of sarcolemma from dystrophicData in brief · 2018Article
- Proteomic profiling of liver tissue from theClinical proteomics · 2018Article
- Chemical crosslinking analysis of β-dystroglycan in dystrophin-deficient skeletal muscle.HRB open research · 2018Article
- Mass spectrometric identification of dystrophin, the protein product of the Duchenne muscular dystrophy gene, in distinct muscle surface membranes.International journal of molecular medicine · 2017Article
- Proteomic profiling of mdx-4cv serum reveals highly elevated levels of the inflammation-induced plasma marker haptoglobin in muscular dystrophy.International journal of molecular medicine · 2017Article
- 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.Journal of muscle research and cell motility · 2017Article
- [Molecular pathogenesis of Duchenne muscular dystrophy-related fibrosis].Der Pathologe · 2017Article
- Absence of Dystrophin Disrupts Skeletal Muscle Signaling: Roles of Ca2+, Reactive Oxygen Species, and Nitric Oxide in the Development of Muscular Dystrophy.Physiological reviews · 2016Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In skeletal muscle, the dystrophin-glycoprotein complex forms a membrane-associated assembly of relatively low abundance, making its detailed proteomic characterization in normal versus dystrophic tissues technically challenging. To overcome this analytical problem, we have enriched the muscle membrane fraction by a minimal differential centrifugation step followed by the comprehensive label-free mass spectrometric analysis of microsomal membrane preparations. This organelle proteomic approach successfully identified dystrophin and its binding partners in normal versus dystrophic hind limb muscles. The introduction of a simple pre-fractionation step enabled the simultaneous proteomic comparison of the reduction in the dystrophin-glycoprotein complex and secondary changes in the mdx-4cv mouse model of dystrophinopathy in a single analytical run. The proteomic screening of the microsomal fraction from dystrophic hind limb muscle identified the full-length dystrophin isoform Dp427 as the most drastically reduced protein in dystrophinopathy, demonstrating the remarkable analytical power of comparative muscle proteomics. Secondary pathoproteomic expression patterns were established for 281 proteins, including dystrophin-associated proteins and components involved in metabolism, signalling, contraction, ion-regulation, protein folding, the extracellular matrix and the cytoskeleton. Key findings were verified by immunoblotting. Increased levels of the sarcolemmal Na+/K+-ATPase in dystrophic leg muscles were also confirmed by immunofluorescence microscopy. Thus, the reduction of sample complexity in organelle-focused proteomics can be advantageous for the profiling of supramolecular protein complexes in highly intricate systems, such as skeletal muscle tissue.
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