Altered glycans have long been associated with cancer and are displayed on such cancer protein markers as CA-125, CA19-9, a fetoprotein, MUC 1, PSA, etc  but have never been fully exploited as indicators of cancer in their own right or as an adjunct to other biomarkers.

We now have the mass spectrometric technology to detect the glycosylation changes on proteins and lipids and to accurately assign glycan structures including sequence and linkage in both cell lines and tissue samples¹.  We can also now correlate these changes with the genes and epigenetic changes responsible for the aberrant glycans observed. Furthermore, we have shown that specific glycan masses can be used to precisely image the localisation of different tissue types in formalin fixed paraffin embedded tissue sections ².

Ovarian cancer is a cancer which is not only difficult to detect at early stage but is also controversial in regard to its tissue origin and metastatic progression. We show that there are significant changes in glycosylation in proteins and lipids between ovarian cancer cell lines that are reflected by changes in expression of the glycosylation pathway genes. We also show that glycan structures can differentiate between patient tissues of ovarian, peritoneal and tubal origin subtypes. Furthermore we demonstrate that specific single glycan structures can localise tissue types in formalin fixed paraffin embedded tissue sections of ovarian cancer samples.