Title : Comparison of sialylated
N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls
Abstract :
- Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases
- Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis
- Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers
- We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS
- Relative quantitation was done using the spectrum processing software MZmine
- Identification was performed on the web-based tool GlycopeptideID , developed for in silico analysis of intact N-glycopeptides
- Seventeen high-abundance serum proteins , mainly acute-phase proteins , and immunoglobulins, with total 27 N-glycosylation sites , and 62 glycoforms, were identified
- Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05)
- In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold
- Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein
- In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins , and immunoglobulins, and that changes are site specific