Functional Analysis of the Glucuronyltransferases GlcAT-P and GlcAT-S of Drosophila melanogaster: Distinct Activities towards the O-linked T-antigen
Copyright policy )Functional Analysis of the Glucuronyltransferases GlcAT-P and GlcAT-S of Drosophila melanogaster: Distinct Activities towards the O-linked T-antigen
The Drosophila melanogaster glucuronyltransferases dGlcAT-S and dGlcAT-P were reported to be expressed ubiquitously and results of in vitro activity assays indicate a functional redundancy. We analyzed both transferases in vivo and in vitro and could show significant differences in their activity towards N-and O-glycoproteins in vivo. While GlcAT-P is able to use N-linked N-acetyllactosamine chains and the O-linked T-antigen as a substrate to form non-sulfated HNK1- (GlcAβ1-3Galβ1-4GlcNAcβ1-) and glucuronyl-T-antigens in vivo, GlcAT-S adds glucuronic acid only to N-linked chains, thereby synthesizing only the non-sulfated HNK1-antigen.
- University of Melbourne Australia
- University of Cologne Germany
- Universtity of Cologne Germany
570, N-glycans, Amino Sugars, glucuronyltransferases, In Vitro Techniques, 540, Microbiology, QR1-502, Article, glycomics, Cell Line, Drosophila melanogaster, Glucuronic Acid, glucuronyltransferases; <i>Drosophila melanogaster</i>; <i>N</i>-glycans; <i>O</i>-glycans; mass spectrometry; glycomics, Animals, Drosophila Proteins, O-glycans, Glucuronosyltransferase, Antigens, Viral, Tumor, mass spectrometry
570, N-glycans, Amino Sugars, glucuronyltransferases, In Vitro Techniques, 540, Microbiology, QR1-502, Article, glycomics, Cell Line, Drosophila melanogaster, Glucuronic Acid, glucuronyltransferases; <i>Drosophila melanogaster</i>; <i>N</i>-glycans; <i>O</i>-glycans; mass spectrometry; glycomics, Animals, Drosophila Proteins, O-glycans, Glucuronosyltransferase, Antigens, Viral, Tumor, mass spectrometry
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