Duchenne muscular dystrophy is a rare and lethal neuromuscular disease caused by loss-of-function mutations in the dystrophin protein that provides structural integrity to striated muscle fibers. Mice with loss-of-function mutations for the Dmd gene encoding dystrophin (mdx-4cv) were treated with microdystrophin or split-intein AAV constructs to restore various-length dystrophin isoforms to the skeletal muscle compartment. The aim of this study was to compare protein expression profiles between healthy (WT), mdx-4cv, and AAV-treated mdx-4cv gastrocnemius skeletal muscle. We employed an isobaric labeling TMT multiplex discovery proteomics approach to describe and compare proteomic profiles across experimental groups.