Mammalian O-mannosyl glycans: Biochemistry and glycopathology

• Published in: Proceedings of the Japan Academy, Series B Vol. 95; no. 1; pp. 39 - 51
• Main Author: ENDO, Tamao
• Format: Journal Article
• Language: English
• Published: Japan The Japan Academy 01.01.2019
• Subjects: Animals; Biochemistry; Brain; congenital muscular dystrophy; Disease; dystroglycan; Enzymes; Glycan; Glycoproteins; Glycosylation; Gram-positive bacteria; Humans; Mammals; Mannose - chemistry; Muscles; Muscular dystrophy; Musculoskeletal system; Mutation; N-glycans; O-mannosylation; Peptides; Phosphorylation; Polysaccharides; Polysaccharides - biosynthesis; Polysaccharides - chemistry; Polysaccharides - metabolism; Proteins; Researchers; Review; ribitol-5-phosphate; O-mannosylation; congenital muscular dystrophy; dystroglycan; ribitol-5-phosphate
• ISSN: 0386-2208; 1349-2896; 1349-2896
• DOI: 10.2183/pjab.95.004

Glycosylation is an important posttranslational modification in mammals. The glycans of glycoproteins are classified into two groups, namely, N-glycans and O-glycans, according to their glycan-peptide linkage regions. Recently, O-mannosyl glycan, an O-glycan, has been shown to be important in muscle and brain development. A clear relationship between O-mannosyl glycans and the pathomechanisms of some congenital muscular dystrophies has been established in humans. Ribitol-5-phosphate is a newly identified glycan component in mammals, and its biosynthetic pathway has been elucidated. The discovery of new glycan structures and the identification of highly regulated mechanisms of glycan processing will help researchers to understand glycan functions and develop therapeutic strategies.