Dystrophin or utrophin are associated with integral and peripheral membrane proteins that can be classified as the dystroglycan complex (DGC): a multimeric protein assembly that links the extracellular matrix (ECM) to the actin cytoskeleton. The DGC mediates three major functions: structural stability of the plasma membrane, ion homeostasis, and transmembrane signaling. The DGC is critical for integrity of muscle fibers by linking the actin cytoskeleton to the ECM, and has been studied in the context of muscle dystrophies and cardiomyopathies for this[1]. In patients suffering from Duchenne muscular dystrophy (DMD), the gene encoding the dystrophin protein shows mutations, resulting in the absence or very low levels of this protein. Utrophin shows sequence and structural similarity to dystrophin and can functionally compensate for the lack of dystrophin under these conditions. However, utrophin does not anchor nNOS to the sarcolemma, which is a requirement to regulate blood flow to the muscle and to ensure that all of its metabolic needs are met[2].