Type

Journal Article

Authors

Kay Ohlendieck
Dieter Swandulla
Paula Meleady
Michael Henry
Maren Raucamp
Margit Zweyer
Sandra Murphy

Subjects

Biochemistry

Topics
phenotype protein expression membrane protein muscle skeletal mass muscular dystrophy duchenne protein isoforms extracellular matrix

Proteomic profiling of the mouse diaphragm and refined mass spectrometric analysis of the dystrophic phenotype. (2018)

Abstract The diaphragm is a crucial muscle involved in active inspiration and whole body homeostasis. Previous biochemical, immunochemical and cell biological investigations have established the distribution and fibre type-specific expression of key diaphragm proteins. Building on these findings, it was of interest to establish the entire experimentally assessable diaphragm proteome and verify the presence of specific protein isoforms within this specialized subtype of skeletal muscle. A highly sensitive Orbitrap Fusion Tribrid mass spectrometer was used for the systematic identification of the mouse diaphragm-associated protein population. Proteomics established 2925 proteins by high confidence peptide identification. Bioinformatics was used to determine the distribution of the main protein classes, biological processes and subcellular localization within the diaphragm proteome. Following the establishment of the respiratory muscle proteome with special emphasis on protein isoform expression in the contractile apparatus, the extra-sarcomeric cytoskeleton, the extracellular matrix and the excitation-contraction coupling apparatus, the mass spectrometric analysis of the diaphragm was extended to the refined identification of proteome-wide changes in X-linked muscular dystrophy. The comparative mass spectrometric profiling of the dystrophin-deficient diaphragm from the mdx-4cv mouse model of Duchenne muscular dystrophy identified 289 decreased and 468 increased protein species. Bioinformatics was employed to analyse the clustering of changes in protein classes and potential alterations in interaction patterns of proteins involved in metabolism, the contractile apparatus, proteostasis and the extracellular matrix. The detailed pathoproteomic profiling of the mdx-4cv diaphragm suggests highly complex alterations in a variety of crucial cellular processes due to deficiency in the membrane cytoskeletal protein dystrophin.
Collections Ireland -> Dublin City University -> PubMed

Full list of authors on original publication

Kay Ohlendieck, Dieter Swandulla, Paula Meleady, Michael Henry, Maren Raucamp, Margit Zweyer, Sandra Murphy

Experts in our system

1
Kay Ohlendieck
Maynooth University
Total Publications: 131
 
2
Dieter Swandulla
Maynooth University
Total Publications: 26
 
3
Paula Meleady
Dublin City University
Total Publications: 115
 
4
Michael Henry
Dublin City University
Total Publications: 99
 
5
Margit Zweyer
Maynooth University
Total Publications: 24
 
6
Sandra Murphy
Maynooth University
Total Publications: 32