Mapping Tissue Carbohydrates Using Mass Spectrometry

March 21, 2022


This GEN Protocols Mixer will be relevant for all interested in methods used in glycoproteomics research that aims to understand the pivotal role of carbohydrate motifs that modify the proteome.

Glycoproteomics, a dynamic area of frontier research, provides a systems biology approach to understanding the biological attributes and functions of glycosylation in biological processes as diverse as immune response, development, differentiation, adhesion, and host-pathogen interactions. Over half of all human proteins bear N-linked glycosylations with vital roles in protein folding, molecular trafficking, signal transduction, cell-cell interactions, and other processes. Changes in glycosylation have been found in diseases ranging from cancer and cystic fibrosis to Parkinson's disease and arthritis. In addition to deciphering disease etiology, glycoproteins are ideal biomarkers as they are assessable in minimally invasive serum samples. Despite its importance in biology, glycoproteomic analyses remain analytically challenging, partly because glycosylation mechanisms are complex and heterogeneous. Imaging mass spectrometry (IMS) is a powerful tool to detect changes in N-linked glycosylation to bolster histopathologic insights from standard formalin-fixed paraffin-embedded tissue samples.


Prof. Richard Drake, Ph.D., Professor and Endowed Chair in Proteomics, Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, USA


For Research Use Only. Not for use in clinical diagnostic procedures.