Why are glycoproteins modified by poly-N-acetyllactosamine glyco-conjugates?

Abstract

Poly-N-acetyllactosamine structures occur in mammalian glycoproteins in both N- and O-linked glycans. They represent a backbone for additional modifications by fucosyltransferases, sialyltransferases and sulfotransferases. These glycans have been suggested to be involved in biospecific interactions with selectins and other glycan-binding proteins. Moreover, the poly-N-acetyllactosamine chains in N-glycans have been found to promote tumor progression and metastasis. Poly-N-acetyllactosamine chains are synthesized by repeated alternating additions of N-acetylglucosamine and galactose, catalyzed by beta-1,3-N-acetylglucosaminyltransferases (poly-N-acetyllactosamine synthase) and beta-1,4-galactosyltransferases. This review describes the poly-N-acetyllactosamine assembling machinery and focuses on recent advances in the molecular cloning and characterization of poly-N-acetyllactosamine synthase gene families. Recent progress in revealing the biological functions of poly-N-acetyllactosamine structures by various approaches in vitro and in vivo using different model systems has also been summarized.

• Authors: Dapeng Zhou
• Journal: Current protein & peptide science (Curr Protein Pept Sci) Vol. 4 Issue 1 Pg. 1-9 (Feb 2003) ISSN: 1389-2037 [Print] United Arab Emirates
• PMID: 12570780 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Glycoconjugates
• Glycoproteins
• Polysaccharides
• poly-N-acetyllactosamine
• Galactosyltransferases

Topics

• Animals
• Galactosyltransferases (metabolism)
• Glycoconjugates (metabolism)
• Glycoproteins (metabolism)
• Humans
• Polysaccharides (metabolism)
• Structure-Activity Relationship
• Substrate Specificity