September 14, 2007 – September 18, 2007
Location: Ecole Normale Superieure, Paris, France
Organized by Ken Moya, Carlito Lebrilla and Steve Berry
Oligosaccharides, composed largely of the simpler elements carbon, oxygen and hydrogen, lend enormous complexity to biological molecules. The formation of sugars and their addition to lipids and proteins requires the regulated activity of specific enzymes. Due to the combinatorial possibilities of carbohydrate modifications of proteins, glycosylation adds a manifold complexity to the functional information in the genome. Oligosaccharide synthesis and protein glycosylation is evolutionarily old, existing in prokaryotes as wells as in eukaryotes. Glycoprotein oligosaccharide composition has typically been studied using metabolic labeling, lectins, and enzymatic removal of specific saccharides.
In addition, oligosaccharides can influence glycoprotein conformation and function due to their size and charge. With regard to these structural characteristics, oligosaccharides have not until recently readily lent themselves to analysis by approaches such as mass spectrometry. In terms of cell biology, oligosaccharides play a key role in important cellular processes such as recognition, adhesion and division. Within cells, glycosylation can influence glycoprotein trafficking and perhaps disease pathogenicity. At a systems level, carbohydrates are now recognized as having a role in immune recognition and for contributing to certain autoimmune diseases such as rheumatoid arthritis and multiple sclerosis. While in the nervous system, glycoproteins and their glycans play an active role in axon growth during brain development, synaptic plasticity underlying learning and in degenerative processes in diseases such as Alzheimer’s disease. The workshop will bring together experts in the field to discuss the glycosome from the physical structure of glycans to their role in disease.
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