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Saturday, September 22 • 2:00pm - 5:00pm
EuroGlycoScience Forum

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Participants need to register for The EMBO Meeting 2012 to attend this special interest symposium.


Protein glycosylation in human disease

The majority of human proteins are posttranslationally modified by the addition of complex oligosaccharides (glycans). Glycans are integral part of glycoproteins and as such significantly participate in structural and functional roles of these proteins in disease mechanisms. Due to structural complexity of glycans and the absence of genetic template for their synthesis, glycan parts of glycoproteins were nearly completely ignored in the past, but recent technological advances enabled analysis of their importance in numerous disease mechanisms. Among other functions, protein glycosylation was shown to be an essential regulator of effector functions of IgG, membrane half-life of various receptors and pharmacodynamic properties of biological therapeutics. Changes in glycosylation were implicated in the progression and/or predisposition of numerous diseases including cancer, diabetes, autoimmune and infectious diseases. Recent population studies of the human glycome indicated very large variability in glycome composition between individuals which derived from both genetic background and environmental influence. Genome wide association studies of the glycome identified proteins that were previously implicated in mechanisms of several major diseases as major regulators of protein glycosylation. Glycosylation changes regulated by these genes were also previously implicated in disease mechanisms (e.g. decreased galactosylation in rheumatoid arthritis), indicating that at least part of disease relevance of these genes derives from their role in protein glycosylation. Human glycome is estimated to be several orders of magnitude more complex than the proteome, thus numerous studies will be needed to reveal the role of glycans in specific molecular processes, but even the current level of knowledge strongly supports their importance in many diseases.


To view the full programme, please click here.


For further information, please contact the organizers: Sabine Flitsch and Gordan Lauc.


Stuart Haslam

Imperial College London
Saturday September 22, 2012 14:40 - 15:10 @ Rhodes 6    The glycobiology of infection and immunity Abstract: Glycans, in the form of polysaccharides or glycoconjugates (bound to proteins and lipids), are found on the surface of every cell in nature. Glycans engage with receptors (called lectins or glycan binding proteins) to mediate cell-cell recognition in numerous biological processes including pathogen/host... Read More →

Gordan Lauc

Faculty of Pharmacy and Biochemistry, University of Zagreb
Saturday September 22, 2012 14:00 - 14:40 @ Rhodes 6    The ubiquitous importance of protein glycosylation Abstract: | The majority of all proteins are glycosylated and their glycan parts have numerous structural, functional and regulatory roles. However, due to their structural complexity, the absence of a direct genetic template and technological limitations, the knowledge about glycans is lagging significantly behind the... Read More →

Falk Nimmerjahn

University of Erlangen-Nürnberg
Saturday September 22, 2012 15:10 - 15:40 @ Rhodes 6    Modulation of IgG function by Fc glycosylation Abstract: IgG antibodies are the primary mediators of protective humoral immunity against pathogens and have been used therapeutically for over a century. They were first used as antitoxins for the treatment of infectious diseases in the pre-antibiotic era. Today, hyperimmune sera from human donors recovering from infection... Read More →

Pauline M. Rudd

Glycobiology Group, National Institute for Bioprocessing Research and Training
Saturday September 22, 2012 16:30 - 17:00 @ Rhodes 6    Glycans as biomarkers of disease Pauline M Rudd, Jane Telford, Jennifer C. Byrne, Barbara Adamcyzk, Radka Saldova Abstract: Over half of all proteins are glycosylated, and alterations in glycosylation are common in both physiological and pathological processes. Glycan processing is, in the first instance, determined by genes (1) that code for 600 or so... Read More →

Uli Scherer

Department of Rheumatology, Leiden University Medical Center
Saturday September 22, 2012 16:00 - 16:30 @ Rhodes 6   Glycosylation Changes in Autoimmune Diseases Abstract: In many autoimmune diseases, including rheumatoid arthritis (RA), antibodies against self-antigens are believed to be the causative agent that drives disease pathogenesis. Antibodies are glycoproteins, with glycans attached to both constant and variable regions of the molecule. These glycans strongly influence... Read More →

Saturday September 22, 2012 2:00pm - 5:00pm
Rhodes 6

Attendees (3)