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Analysis of dystrophic muscle by two dimensional differential in‐gel electrophoresis
Author(s) -
Dixon Jenna,
GardanSalmon Delphine,
Lonergan Steven,
Selsby Joshua T
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.989.2
Subject(s) - proteome , dystrophin , duchenne muscular dystrophy , mdx mouse , gene isoform , biology , difference gel electrophoresis , two dimensional gel electrophoresis , muscular dystrophy , gel electrophoresis , microbiology and biotechnology , proteomics , gene , genetics
Duchenne muscular dystrophy (DMD), the most common, fatal, X‐linked disease, is caused by a defect in the dystrophin gene. While dystrophin deficiency is the causative factor in this disease, changes in the expression of other proteins may also contribute to disease pathology. The objective of this investigation was to determine the extent to which dystrophin deficiency impacts the muscle proteome. We performed two dimensional differential in‐gel electrophoresis (2D‐DIGE) (pH 4‐7) on gastrocnemii taken from 6 week old male mice (n=6 mdx; n=6 C57). Of a total of 2200 spots detected, 41 spots (representing unique isoforms or modified proteins) were found to be differentially expressed (p<0.1; 24 spots with p<0.05). Of these, 30 spots were increased and 11 were decreased in mdx compared to control. Using mass spectroscopy and MALDI‐TOF, the identity of the proteins represented was confirmed in 36 spots. These proteins represent a variety of cell functions including apoptosis, mitochondrial function, and cell growth and differentiation. Further analysis of these proteins may allow for the identification of novel pathways and lead to the development of innovative strategies to minimize disease progression.