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Why are Glycoproteins Modified by Poly-N-Acetyllactosamine Glycoconjugates?

[ Vol. 4 , Issue. 1 ]

Author(s):

Dapeng Zhou   Pages 1 - 9 ( 9 )

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-Nacetyllactosamine chains in N-glycans have been found to promote tumor progression and metastasis. Poly-N-acetyllactosamine chains are synthesized by repeated alternating additions of Nacetylglucosamine and galactose, catalyzed by β-1,3-N-acetylglucosaminyltransferases (poly-N-acetyllactosamine synthase) and β-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.

Keywords:

poly-n-acetyllactosamine, 3-n-acetylglucosaminyltransferase, 4-galactosyltransferase

Affiliation:

Department of Pathology, University of Chicago, 5841 S. Maryland Avenue, MC 1089 Chicago, IL 60637, USA



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