Protein Glycosylation in Cancer.

While the first observations of glycosylation changes in cancerous tissues now date back several decades, the field of medical glycobiology has been largely hindered by: (a) lack of sufficient knowledge of the glycan biosynthesis (non-template coded) in complex cellular systems; (b) structural complexity of carbohydrates; and (c) lack of structural and quantitative tools to observe pertinent glycosylation changes. During the last several years, glycomics and glycoproteomics have joined the other “omics” technologies in their potential of elucidating the processes pertaining to disease biomarker detection. We have developed highly sensitive techniques based on mass spectrometry to profile the glycans derived from blood serum glycoproteins. The comparisons between control individuals and patients suffering from different types of cancer yielded statistically significant differences in glycomic profiles. While a search for diagnostically and prognostically useful profiling procedures continues, our laboratory has characterized several glycoproteins of interest to pancreatic, esophageal, ovarian, and lung cancers.