Evolution of Glycan Diversity

     Glycans are saccharides that can be attached to a wide variety of biological molecules through an enzymatic process called glycosylation to augment their function. Of the four fundamental building blocks of life, proteins, carbohydrates (glycans), lipids and nucleic acids, glycans have received the least attention from researchers. Glycans are found in archaea, bacteria and eukaryotes, and their diverse functions contribute to physical and structural integrity, extracellular matrix formation, signal transduction, protein folding and information exchange between cells (and pathogens). Glycans are the predominant molecule on the cell surface and serve as the first point of contact between a cell and other cells, the extracellular matrix and pathogens. The heightened evolutionary pressure of being at the front lines of cellular collaboration and conflict most likely led to the diversification of glycans. Glyco-epitope diversity enhances the role of glycans in the group of debilitating and life-shortening disorders known as congenital muscular dystrophy, or CMD. Both membrane proteins and the ECM are highly glycosylated, and O-glycans are essential for proper ECM function and communication between cells and the ECM. Several Glycoepitomics forms of CMD are known to result from dysfunctional O-glycosylation of membrane and ECM proteins; however, one-third of CMDs arise from an unknown genetic etiology.

Relevant Conferences:Glycobiology Conferences | Biochemistry Conferences

6th International Conference on Bioinformatics, March 29-30, 2016 Valencia, Spain; International Conference on Structural Biology, June 23-24, 2016 New Orleans, USA; World Congress on Amino Acids and Proteins, December 08-09, 2016 Baltimore, USA; International Conference on Nucleic Acids, August 04-06, 2016 Seattle, USA 7th International Conference and Expo on Proteomics, October 24-26, 2016 Rome, Italy; International Conference on Obesity & Chronic Diseases, July 25-27, 2016 Las Vegas USA; International Conference on New Therapeutics for Diabetes and Obesity, April 17-20, 2016 La Jolla, USA; Conference on Plasma Spectrochemistry, January 10-16, 2016 Tucson, USA; Euro Fed Lipid Congress, September 18-21, 2016 Gent, Belgium; Conference on Obesity and Adipose Tissue Biology, February 15-19, 2016 Banff, Canada

Carbohydrates are capable of generating structural diversity in multiple ways and are prominently displayed on the surfaces of cell membranes or on the exposed regions of macromolecules. Unlike proteins, which are connected solely by a peptide bond, carbohydrates utilize many possible glycosidic linkages so as to extensively diversify their structures. Glycosylation is a critical function of the biosynthetic-secretory pathway in the endoplasmic reticulum (ER) and Golgi apparatus. Glycosylation increases the diversity of the proteome to a level unmatched by any other post-translational modification. Glycosidases catalyze the hydrolysis of glycosidic bonds to remove sugars from proteins. These enzymes are critical for glycan processing in the ER and Golgi, and each enzyme shows specificity for removing a particular sugar (e.g., mannosidase).

• Glycoepitomics
• Glycan structural modelling
• Biochemical analysis of lipids & proteins
• Comparative Glycomics
• Synthesis systems of glycans
• Glyco-epitope Diversity

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