Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1573, Issue 3, Pages 363-368Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0304-4165(02)00404-X
Keywords
N-acetylglucosaminyltransferase; GlcNAc-TIII; bisecting GlcNAc; tumor progression; growth control
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Funding
- PHS HHS [R01 30645] Funding Source: Medline
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N-acetylglucosaminyltransferase III (GlcNAc-TIII), a product of the human MGAT3 gene, was discovered as a glycosyltransferase activity in hen oviduct. GlcNAc-TIII transfers GlcNAc in beta4-linkage to the core Man of complex or hybrid N-glycans, and thereby alters not only the composition, but also the conformation of the N-glycan. The dramatic consequences of the addition of this bisecting GIcNAc residue are reflected in the altered binding of lectins that recognize Gal residues on N-glycans. Changes in GIcNAc-TIII expression correlate with hepatoma and leukemia in rodents and humans, and the bisecting GlcNAc on Asn 297 of human IgG antibodies enhances their effector functions. Overexpression of a cDNA encoding GIcNAc-TIII alters growth control and cell-cell interactions in cultured cells, and in transgenic mice. While mice lacking GlcNAc-TIII are viable and fertile, they exhibit retarded progression of diethylnitrosamine (DEN)induced liver tumors. Further biological functions of GlcNAc-TIII are expected to be uncovered as mice with a null mutation in the Mgat3 gene are challenged. (C) 2002 Elsevier Science B.V. All rights reserved.
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