Speaker: Joseph Zaia, Boston University School of Medicine

Topic: Proteomics, glycomics, and glycoproteomics of matrisome molecules

Date: Monday, September 16th, 2019

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instruments, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Meghan Burke (meghan.burke@nist.gov) by Friday, September 16th if you will be attending the dinner.

Abstract: The most straightforward applications of proteomics database searching involve intracellular proteins. While intracellular gene products number in the thousands, their well-defined post-translational modifications (PTMs) makes database searching practical. By contrast, cell surface and extracellular matrisome proteins pass through the secretory pathway where many become glycosylated, modulating their physicochemical properties, adhesive interactions, and diversifying their functions. While matrisome proteins number only a few hundred, their high degree of complex glycosylation multiplies the number of theoretical proteoforms by orders of magnitude. Given that extracellular networks that mediate cell-cell and cell-pathogen interactions in physiology depend on glycosylation, it is important to characterize the proteomes, glycomes and glycoproteomes of matrisome molecules that exist in a given biological context. In this presentation, I will summarize proteomics approaches for characterizing matrisome molecules, with an emphasis on applications to brain diseases.