| Title | Synthesis and glycan priming activity of acetylated disaccharides. | | Author(s) | Sarkar AK, Brown JR, Esko JD | | Institution | Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093, USA. | | Source | Carbohydr Res 2000 Nov 3; 329(2):287-300. | | MeSH | Acetylation
Acetylgalactosamine
Acetylglucosamine
Carbohydrate Conformation
Carbohydrate Sequence
Cell Adhesion
Cells, Cultured
Comparative Study
Disaccharides
E-Selectin
Endothelium, Vascular
Gene Expression Regulation, Neoplastic
Glycosylation
Humans
Magnetic Resonance Spectroscopy
Membrane Glycoproteins
Molecular Sequence Data
Neoplasm Proteins
Oligosaccharides
Polysaccharides
Protein Processing, Post-Translational
Research Support, U.S. Gov't, P.H.S.
Structure-Activity Relationship
U937 Cells
| | Abstract | Five disaccharides related in structure to the glycans of vertebrate mucins have been chemically synthesized using orthogonal blocking, coupling and deblocking techniques. These include 2-naphthylmethyl 3,4,6-tetra-O-acetyl-beta-D-galactopyranosyl-( 1 --> 4)-2-acetamido-3,6-di-O-acetyl-2-deoxy-beta-D-glucopyranoside (6), 2-naphthylmethyl 2-aceta-mido-3,4,6-tri-O-acetyl-2-deoxy-beta-D-glucopyranosyl-(1 --> 3)-2,4,6-tri-O-acetyl-beta-D-galactopyranoside (14), 2-naph-thylmethyl2,3,4,6-tetra-O-acetyl-beta-D-galactopyranosyl-(1 --> 3)-2-acetamido-4,6-di- O-acetyl-2-deoxy-alpha-D-galactopyranoside (20), 2-naphthylmethyl 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-beta-D-glucopyranosyl-(1 --> 3)-2-acetamido-4,6-di-O-acetyl-2-deoxy-alpha-D-galactopyranoside (23) and 2-naphthylmethyl 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-beta-D-glu-copyranosyl-(1 --> 6)-2-acetamido-3,4-di-O-acetyl-2-deoxy-alpha-D-galactopyranoside (27). These per-O-acetylated compounds were fed to U-937 cells to test their ability to prime oligosaccharide synthesis, inhibit glycoprotein biosynthesis and alter adhesion to E-selectin expressed on endothelial cells. The results show that 6, 14, and 20 served as substrates for oligosaccharide synthesis. The generation of glycoside-primed glycans altered the formation of glycoproteins on the cell surface and inhibited cell adhesion dependent on E-selectin. | | Language | eng | | Pub Type(s) | Journal Article
| | PubMed ID | 11117312 |
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