GBMSDG Meeting Archives
January 15, 2009
Professor Catherine E. Costello
Boston University School of Medicine
Revolutions in Mass Spectrometry-Based
Shire Human Genetic Therapies
Glycoproteins play multiple roles in biological systems and are remodeled throughout the life of the organism to modify or optimize their functions. The task of determining structures and structure/function relationships is made difficult by the occurrence of the glycans as mixtures of closely related structures, with complex branching patterns and labile bonds. Nevertheless, modern mass spectrometry techniques, coupled with improvements in sample preparation and separation methods, are enabling this task to be accomplished at sensitivity levels that approach those for proteins and peptides. Through the Human Glycoproteomics Initiative, worldwide cooperation among laboratories that are engaged in glycomic studies has recently been directed at the evaluation of methods for the characterization of glycoproteins with N- and O-linked glycans. Current efforts are now aiming at whole cell studies and the assembly of databases and software for glycan structural interpretation that are both compatible with one another and user-friendly. As these tools become increasingly available to the community, more laboratories should be equipped to undertake the profiling and structural studies of glycans. This overview of progress in glycoprotein characterization will include some local milestones, current developments and their applications to the analysis of glycans from model systems and human diseases.
This research is supported by NIH Grants P41 RR10888, S10 RR15942, S10 RR020946 and P01 HL68705 and Contract No. N01 HV28178.
Dinner hosted at Shire