Emerging Opportunities for Incorporation of Proteomics and Glycoproteomics into Clinical Analyses

Catherine E. Costello
Boston University School of Medicine, Boston, MA

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Catherine Costello (Presenter) Boston University School of Medicine

Presenter Bio: Catherine E. Costello is a William Fairfield Warren Distinguished Professor in the Depts. of Biochemistry, Biophysics, and Chemistry at Boston University. She was a postdoctoral fellow and Senior Research Scientist at MIT for more than 20 years. She founded the BU School of Medicine Center for Biomedical Mass Spectrometry in 1994. Her research centers on development of mass spectrometry-based methods for biopolymers and their application to study glycobiology, protein post-translational modifications, protein misfolding disorders, cardiovascular and infectious diseases, and bioactive lipids. She has authored about 400 scientific papers. She has served as President of the International Mass Spectrometry Foundation, HUPO and ASMS, and multiple editorial and advisory boards. She has received several major awards in mass spectrometry, proteomics and chemistry and is a fellow of ACS and AAAS.

Relevant Financial Disclosures (within past 24 months) Honorarium/Expenses MSACL, Agilent Grant/Research Support Natl Inst of Health, Nutricia, Eisai Committee/Board/Advisory Board Malta Foundatiion for Research & Education in the Middle East Discussing Products? YES, presenter will present educational content related to products/services of one or more ineligible company(ies) listed above. Conflict mitigation IN PROCESS.

Determination of the relationship between changes in tissue and circulating levels of proteins and their derivative peptides and the development of disease- or age-related physiological changes poses major challenges because of the broad dynamic range of the biologically active species, the structural complexity and diversity of co- and post-translational modifications, and the presence of numerous isomeric structures in biological samples. To minimize losses and avoid introduction of artifacts that are due to sample handling, to discriminate among similar components, and to make efficient use of instrument time, we are developing ion mobility and mass spectrometry-based methods that are compatible with on-line separations and increase the yield of detailed structural information. We are also exploring the suite of electron-based dissociation methods that preserve labile protein modifications while producing highly informative fragmentation. Illustrations will include results from recent and ongoing studies in which a variety of MS techniques are being applied to enable comprehensive proteomic and glycoproteomics analyses of clinical samples and model cell systems that are relevant to development of vaccines, cancer therapeutics, and tools for combating infectious diseases, and to increased understanding of the pathways underlying protein misfolding disorders.