AI Article Synopsis
- A new mass spectrometry method was developed to analyze N-glycan structures in serum proteins to identify fucosylated glycans as potential pancreatic cancer markers.
- This method was tested on haptoglobin from serum samples of 16 pancreatic cancer patients and 15 benign condition individuals, utilizing only a small volume of serum for extraction and analysis.
- The study found significant differences in fucosylation patterns between pancreatic cancer patients and those with benign conditions, indicating that this assay could be a promising tool for diagnosing pancreatic cancer.
Article Abstract
A mass spectrometric method was developed to elucidate the N-glycan structures of serum glycoproteins and utilize fucosylated glycans as potential markers for pancreatic cancer. This assay was applied to haptoglobin in human serum where N-glycans derived from the serum of 16 pancreatic cancer patients were compared with those from 15 individuals with benign conditions (5 normals, 5 chronic pancreatitis, and 5 type II diabetes). This assay used only 10 μL of serum where haptoglobin was extracted using a monoclonal antibody and quantitative permethylation was performed on desialylated N-glycans followed by MALDI-QIT-TOF MS analysis. Eight desialylated N-glycan structures of haptoglobin were identified where a bifucosylated triantennary structure was reported for the first time in pancreatic cancer samples. Both core and antennary fucosylation were elevated in pancreatic cancer samples compared to samples from benign conditions. Fucosylation degree indices were calculated and show a significant difference between pancreatic cancer patients of all stages and the benign conditions analyzed. This study demonstrates that a serum assay based on haptoglobin fucosylation patterns using mass spectrometric analysis may serve as a novel method for the diagnosis of pancreatic cancer.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3090531 | PMC |
| http://dx.doi.org/10.1021/pr200102h | DOI Listing |
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