Disorders in a unique type of posttranslational modification of a-dystroglycan lay at a background of a group of congenital muscular dystrophies, called dystroglycanopathies. To bind laminin in a basal membrane the protein has to be glycosylated in a special way, with mannose linked with O-glycosidic bond to serine or threonine in a mucin-like region. The nascent glycan is then elongated with N-acetylglucosamine, galactose, sialic acid and optionally fucose. It is also suggested that proper function of dystroglycan depends on mannose phosphorylation.

Muscular cell integrity is assured by a number of proteins of different structure, function and localization. Their defective synthesis of genetic background results in muscular dystrophies. In these diseases progressive damage of skeletal muscle leads to disability, and in some cases affection of respiratory muscles may be a cause of early death. There is no doubt now that proper muscle function demands undisturbed collaboration of a great number of proteins, located inside the cell as well as in sarcolemma and extracellular matrix.