The role of protein glycosylation in muscle diseases

As a post-translational modification, glycosylation plays vital role in regulating the folding and function of proteins necessary for many biological processes. Unlike glycation, glycosylation is an enzymatic process; glycosyltransferases transfer sugars to proteins, forming glycosidic bonds with amino acid residues on proteins. Changes that interfere with the enzymatic reaction and result in abnormal glycosylation can spatio-temporally affect the balance of glycosylation, leading to disease states. Muscle diseases have been associated with dysfunctional protein glycosylation, and many studies have focused on the pathophysiology underlying this association. This review aims to summarize the research progress on protein glycosylation in the pathogenesis of muscle diseases and provides new insight into the muscle research field.

Literatures were reviewed comparatively and data were organized to find information about protein glycosylation and its role in muscle disease.

Protein glycosylation modification is closely related to the occurrence of muscle diseases. α-DG is a key protein in the study of inherited muscle diseases and has a wide range of glycosylation, including O-linked glycosylation and N-linked glycosylation. Besides, O-GlcNAc glycosylation is an important mechanism of protein glycosylation, helping maintaining the structure and function of skeletal muscle and participating in multiple biological processes. Protein glycosylation is also connected to muscle disease and neurodegenerative diseases, especially Alzheimer's disease.

Taken together, better understanding of protein glycosylation and its implication in muscle disease would help provide new perspectives in the prevention and treatment measures for human muscle diseases.