Ovarian cancer is a major cause of cancer mortality among women, largely
due to late diagnosis of advanced metastatic disease. More extensive molecular
analysis of metastatic ovarian cancer is needed to identify post-translational
modifications of proteins, especially glycosylation that is particularly
associated with metastatic disease to better understand the metastatic process
and identify potential therapeutic targets. Glycoproteins in ascites fluid were
enriched by affinity binding to lectins (ConA or WGA) and other affinity
matrices. Separate glycomic, proteomic, and glycopeptide analyses were
performed. Relative abundances of different N-glycan groups and proteins were
identified from ascites fluids and a serum control. Levels of biomarkers CA125,
MUC1, and fibronectin were also monitored in OC ascites samples by Western blot
analysis. N-Glycan analysis of ascites fluids showed the presence of large,
highly fucosylated and sialylated complex and hybrid glycans, some of which were
not observed in normal serum. OC ascites glycoproteins, haptoglobin,
fibronectin, lumican, fibulin, hemopexin, ceruloplasmin, alpha-1-antitrypsin,
and alpha-1-antichymotrypsin were more abundant in OC ascites or not present in
serum control samples. Further glycopeptide analysis of OC ascites identified
N-and O-glycans in clusterin, hemopexin, and fibulin glycopeptides, some of
which are unusual and may be important in OC metastasis.