Mass spectrometry-based N-linked glycomic profiling as a means for tracking pancreatic cancer metastasis

• Total N-glycans are identified via quantitative mass spectrometric approaches.
• The relative quantity of high-mannose glycans is higher on Capan-1 cancer cells.
• The highly-branched sialyted N-glycans is up-regulated on Panc-1 and MIA PaCa-2.
• N-glycosylation on pancreatic cancer cells depend on the site of tumor metastasis.

The aberrant glycosylation profile on the surface of cancer cells has been recognized for its potential diagnostic value towards assessing tumor progression. In this study, we initially investigate N-glycan profiles on the surface of normal (HPDE) and cancerous (Capan-1, Panc-1, and MIA PaCa-2) pancreatic cell lines, which are from different sites of pancreatic tumor. The enzymatically deglycosylated total N-glycans are permethylated via a quantitative solid-phase method and then analyzed by using MALDI-TOF MS and MALDI-QIT-TOF MS. We demonstrate that the level of high-mannose type glycans is higher among Capan-1 cells—pancreatic cancer cells that have metastasized to the liver—than that observed among Panc-1 and MIA PaCa-2 cells—pancreatic cancer cells from the pancreas duct head and tail regions, respectively. Furthermore, the relative abundance of highly-branched sialyted N-glycans is significantly up-regulated on Panc-1 and MIA PaCa-2 pancreatic cancer cells compared to that of normal HPDE pancreas cells. Taken together, these results indicate that specific N-glycosylation profile changes in pancreatic cancer cells can be used to not only distinguish between normal and cancerous cells but also provide more information on their location and metastatic potential.

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