O-mannosyl glycans in mammals

Biochim Biophys Acta. 1999 Dec 6;1473(1):237-46. doi: 10.1016/s0304-4165(99)00182-8.

Abstract

Most proteins within living organisms contain glycans. Glycan structures can modulate the biological properties and functions of glycoproteins. The major glycans of glycoproteins can be classified into two groups, N-glycans and O-glycans, according to their glycan-peptide linkage regions. Developments in glycobiology have revealed a new type of glycosidic linkage to the peptide portion, the O-mannosyl linkage, in mammals, while so far it had been thought to be specific to yeast. This review will give an outline of the O-mannosyl glycans of mammalian glycoproteins. Since one of the most well known O-mannosyl-modified mammalian glycoproteins is dystroglycan, the functional aspects of the O-mannosyl glycan of dystroglycan will be described to help understand this new glycobiological field.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / metabolism
  • Dystroglycans
  • Glucosyltransferases
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism
  • Glycosylation
  • Humans
  • Mannose / chemistry*
  • Mannose / metabolism
  • Mannosyltransferases / metabolism*
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism
  • Models, Molecular
  • Polysaccharides / biosynthesis
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism
  • Ribonucleases / chemistry
  • Yeasts

Substances

  • Cytoskeletal Proteins
  • DAG1 protein, human
  • Glycoproteins
  • Membrane Glycoproteins
  • Polysaccharides
  • glycogenin
  • Dystroglycans
  • Glucosyltransferases
  • Mannosyltransferases
  • Ribonucleases
  • Mannose