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
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. N-glycopeptide, , -, -, N-glycopeptide
- 10. N-glycosylation, , -, -, sites
- 10. glycoprotein, , glycoprotein, -, -
- 10. one, , -, -, sites
- 11. N-glycopeptides, , -, -, N-glycopeptides
- 11. sialylated, , -, -, N-glycopeptides
- 3. glycoprotein, , glycoprotein, -, -
- 4. N-glycopeptides, , -, -, N-glycopeptides
- 4. sialylated, , -, -, N-glycopeptides
- 6. N-glycopeptides, , -, -, N-glycopeptides
- 7. N-glycosylation, , -, -, sites
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):