Duchenne muscular dystrophy (DMD) is an X-linked neuromuscular disease characterized by the absence of the cytoskeletal protein dystrophin (Dp427). Short isoforms, such as Dp116 in myelinating Schwann cells (SCs), exist in specific cell types. In SCs, Dp116 binds to the dystrophin-associated glycoprotein complex (DGC), which crucially contributes to myelin integrity and fiber conduction properties. Our prior research on the sciatic nerve (SN) of wild-type and mdx mice, a DMD animal model lacking Dp427, revealed a significant decrease in all myelin protein levels, indicating compromised myelin integrity. Given Dp116-DGC's crucial role in SCs, we analyzed levels, localization and immunofluorescence intensity of Dp116 and of three core DGC proteins: alpha- and beta-dystroglycan (DG), and beta-dystrobrevin. In mdx mouse SN, all parameters exhibited significant reductions compared to wild-type, except for Dp116. We therefore hypothesized that extracellular matrix metalloproteinases (MMPs) 2 and 9, which target beta-DG and are activated by muscle inflammation, could retrogradely impact DGC stability in the SN as well, compromising myelin integrity. Western immunoblot confirmed MMP-2 and MMP-9 activation. In addition, electrophysiological evidence by Compound Action Potential recording of sural nerve demonstrated reduced excitability of sensory Aβ-mechanoreceptors fibers, indicating potential muscle proprioception impairment. Finally, as cholinergic signaling significantly impacts axon-SCs communication and myelination, we also analyzed levels of M2 metabotropic and alpha-7 ionotropic ACh receptors, revealing a significant reduction of both in mdx mouse SN compared to wild-type. These findings collectively underscore DMD's substantial impact on peripheral nerves, potentially resulting in peripheral neuropathies and impaired muscular control.