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ZFIN ID: ZDB-PUB-021017-46
Order out of chaos: Assembly of ligand binding sites in heparan sulfate
Esko, J.D. and Selleck, S.B.
Date: 2002
Source: Annual review of biochemistry 71: 435-471 (Review)
Registered Authors:
Keywords: glycosaminoglycans, proteoglycans, glycosylation, sulfation, model organisms
MeSH Terms:
  • Animals
  • Antithrombins/metabolism
  • Binding Sites
  • Body Patterning
  • Enzymes/genetics
  • Enzymes/metabolism
  • Fibroblast Growth Factor 2/metabolism
  • Heparitin Sulfate/chemistry*
  • Heparitin Sulfate/metabolism*
  • Humans
  • Ligands
  • Molecular Structure
  • Oligosaccharides/chemistry
  • Oligosaccharides/metabolism
  • Protein Binding
PubMed: 12045103 Full text @ Ann. Rev. Biochem.
ABSTRACT
Virtually every cell type in metazoan organisms produces heparan sulfate. These complex polysaccharides provide docking sites for numerous protein ligands and receptors involved in diverse biological processes, including growth control, signal transduction, cell adhesion, hemostasis, and lipid metabolism. The binding sites consist of relatively small tracts of variably sulfated glucosamine and uronic acid residues in specific arrangements. Their formation occurs in a tissue-specific fashion, generated by the action of a large family of enzymes involved in nucleotide sugar metabolism, polymer formation (glycosyltransferases), and chain processing (sulfotransferases and an epimerase). New insights into the specificity and organization of the biosynthetic apparatus have emerged from genetic studies of cultured cells, nematodes, fruit flies, zebrafish, rodents, and humans. This review covers recent developments in the field and provides a resource for investigators interested in the incredible diversity and specificity of this process.
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