title: Proteomic analysis of dystrophic muscle.
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.
authors: Department of Biology, National University of Ireland Maynooth, Maynooth, Co. Kildare, Ireland.
authors: Caroline
authors: C
authors: Lewis
authors: Philip
authors: P
authors: Doran
authors: Kay
authors: K
authors: Ohlendieck
mesh_terms: D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D005456:Fluorescent Dyes; D007525:Isoelectric Focusing; D013058:Mass Spectrometry; D051379:Mice; D018101:Mice, Inbred mdx; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000473:pathology; D020388:Muscular Dystrophy, Duchenne / Q000378:metabolism* / Q000473:pathology; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D013194:Staining and Labeling / Q000379:methods
chemical_list: D005456:Fluorescent Dyes; D011506:Proteins