Sialic Acid Analysis in Pancreatic Cancer

Sialic Acid Analysis in Pancreatic Cancer

Pancreatic cancer has the highest mortality rate among the common malignancies. The discovery of sialoglycoproteins in pancreatic cancer cells holds potential for the diagnosis of cancer or as cell surface therapeutic targets. CD BioGlyco has developed a complete solution to provide our clients with sialic acid analysis in pancreatic cancer.

Pancreatic Cancer

Pancreatic cancer is cancer that begins in the tissues of the pancreas-an organ in the abdomen that lies behind the lower part of your stomach. Pancreatic cancer is the fourth leading cause of cancer death in Europe and the USA. Pancreatic cancer has the highest mortality rate among the common malignancies. The two main features of this tumor are the presence of a strong desmoplastic stroma and a high metastatic potential. The poor prognosis of pancreatic cancer is due to the aggressiveness of this disease, rapid metastasis, and late diagnosis of the malignancy.

Aberrant Sialylation in Pancreatic Cancer

A key hallmark of cancer is a change in glycosylation during tumor progression including the length and branching of polylactosamine chains and/or the quantity and linkage of terminal sialic acids. The role of some of these tumor-associated antigens has been in some cases reported. For example, Sialyl Lewis x and Sialyl Lewis a determinants act as E-selectin ligands facilitating the tumor hematogenous metastasis. In pancreatic cancer cells, the increase of sialyl Lewis x surface expression shows that cells have higher E-selectin adhesion capability and metastatic potential.

Fig.1 Changes in glycosylation during cancer progression.Fig.1 Changes in glycosylation during cancer progression. (Munkley, 2019)

Pancreatic cancer cells present an increased sialylation that is recognized by Siglec-7 and Siglec-9 on myeloid cells and induce immunomodulatory properties via binding to Siglec receptors. Tumour-derived sialic acids dictate monocyte to macrophage differentiation via signaling through Siglec-7 and Siglec-9.

The glycoconjugates on the surface of tumor cells present sialic acids in different linkages concerning the underlying glycan (namely α2,3, α2,6, and α2,8), each of which is catalyzed by specific enzymes. Lectins have long been used for the purification and detection of glycans in many studies. Many lectins have overlapping affinity while some others have unique specificity, allowing for the efficient detection of differential expression of glycan structure. We could perform immunohistochemistry on biopsies from pancreatic cancer patients using the biotinylated plant lectins derived from Maackia amurensis (MAL-II) and Sambucus nigra (SNA). These lectins are used as probes to identify sialylated structures with the α2,3 or α2,6 configuration, respectively.

Sialoglycoproteins play an important role in tumor progression. A variety of high-throughput approaches have been used to characterize sialylated glycoproteins, which include lectin affinity, titanium dioxide affinity chromatography, strong cation exchange columns, conditional hydrazide chemistry, or the combination of diagonal chromatographic technology and neuraminidase treatments. We have developed a strategy to analyze sialylated glycoprotein found in pancreatic cancer cells including robust Labeling of several glycoproteins associated with tumors occurs, lectin affinity selection, identification, and characterization of sialoglycoproteins using liquid chromatography with tandem mass spectrometry (LC-MS/MS).

Advantages of Us

  • Identification of sialylated structures by lectins
  • Customized strategy to analyze sialylated glycoprotein
  • Experienced technical team
  • Detailed data and analysis reports

CD BioGlyco employs various approaches to provide you with professional and rapid analysis services of sialic acids in pancreatic cancer. If you are interested in our services, please contact us for more detailed information.


  1. Tian, Y.; et al. Identification of sialylated glycoproteins from metabolically oligosaccharide engineered pancreatic cells. Clinical proteomics. 2015, 12(1): 1-13.
  2. Munkley, J. The glycosylation landscape of pancreatic cancer. Oncology letters. 2019, 17(3): 2569-2575.
This service is for Research Use Only, not intended for any clinical use.

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