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.

journal_name

Curr Protein Pept Sci

authors

Zhou D

doi

10.2174/1389203033380304

keywords:

subject

Has Abstract

pub_date

2003-02-01 00:00:00

pages

1-9

issue

1

eissn

1389-2037

issn

1875-5550

journal_volume

4

pub_type

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