Article

Proteomic analysis of dystrophic muscle.

Department of Biology, National University of Ireland Maynooth, Maynooth, Co. Kildare, Ireland.
Methods in molecular biology (Clifton, N.J.) 01/2012; 798:357-69. DOI:10.1007/978-1-61779-343-1_20
Source: PubMed

ABSTRACT Mass spectrometry-based proteomics had a major impact on the global characterization of skeletal muscles and has decisively enhanced the field of neuromuscular pathology. Proteomic profiling of x-linked muscular dystrophy has identified a large number of new signature molecules involved in fiber degeneration. Here, we describe the difference in-gel electrophoretic analysis of the dystrophic diaphragm muscle from the MDX mouse model of Duchenne muscular dystrophy. This chapter summarizes the various experimental steps involved in muscle proteomics, such as sample preparation, fluorescence labeling, isoelectric focusing, second-dimension slab gel electrophoresis, image analysis, in-gel digestion and electrospray ionization mass spectrometry.

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Keywords

chapter summarizes
 
decisively
 
difference in-gel electrophoretic analysis
 
Duchenne muscular dystrophy
 
electrospray ionization mass spectrometry
 
fluorescence labeling
 
image analysis
 
in-gel digestion
 
Mass spectrometry-based proteomics
 
MDX mouse model
 
muscle proteomics
 
neuromuscular pathology
 
new signature molecules
 
Proteomic profiling
 
sample preparation
 
second-dimension slab gel electrophoresis
 
x-linked muscular dystrophy