Synthesis of Sialyl-T Antigen Type O-glycan and Relationship to Tumors

The most common forms of mucins in humans are T antigens and sialylated T antigens. O-glycosylation biosynthetic pathway is a relatively competitive reaction process that depends on the availability of glycan substrates and glycosyltransferases. The binding of sialic acid to O-glycans during O-glycans elongation leads to the premature termination of glycan synthesis and to the formation of truncated glycans, such as sialyl-T and Sialyl-Tn. The synthesis of sialyl-T is associated with ST3 beta-galactoside alpha-2,3-sialyltransferase (ST3Gal-I). When core 1 is synthesized, further synthesis of sialyl-T is catalyzed by ST3Gal-I. In tumor cells, substrates and glycosyltransferases are aberrantly expressed, which ultimately leads to structural changes in O-glycans, such as sialyl-T and sialyl-Tn. The study of glycan structure, glycosyltransferases, and glycan polymerization pathways helps to understand the invasive and metastatic mechanisms of tumors, cellular drug resistance mechanisms, etc.

Fig.1 The synthesis of sialyl-T antigen. (Sewell, et al., 2006)

Sialyl-T Antigen Type O-glycan Glycoengineering Service at CD BioGlyco

Research on sialyl-T antigen type O-glycan will support studies on the pathogenesis and therapeutics of diseases such as cancer. We offer a full range of sialyl-T antigen type O-glycan glycoengineering services.

Fig.2 Sialyl-T antigen type O-glycan glycoengineering service. (CD BioGlyco)

• Introduction and modification of Sialyl-T Antigen Type O-glycan

We chemically or enzymatically cleave sialyl-T antigen-type O-glycans from proteins and perform a series of analyses. This approach enables us to validate the role of sialyl-T antigen type O-glycan in proteins, cells, tissues, and so on. We also used a gene-editing approach for targeted modification of sialyl-T antigen type O-glycan on the cell surface. Mutations in the structure of sialyl-T have been associated with the development of certain diseases. Wild mice are found to express the sialyl-T antigen in epithelial cells, hematopoietic cells, and endothelial cells. Mutant mice lacking the T synthase gene expressed non-sialylated T antigen in these cells. Cerebral hemorrhage will occur later in life. We verify the function of this glycosylation in the organism by Knocking Out the sialyl-T antigen synthesis-related enzyme gene. We also add other non-natural analogs in O-glycan synthesis. By this method, we are able to verify the role of sialyl-T antigen type O-glycan in proteins, cells, tissues, etc. It also verifies the role of altered glycosylation in tumorigenesis, migration, and so on.

• O-glycan analysis

O-glycan Analysis is an important part of glycomics research. We also provide analytical services for sialyl-T antigen type O-glycan, including O-glycan cleavage release, liquid chromatography purification and enrichment, mass spectrometry detection, and bioinformatics analysis.

Fig.3 General experimental procedure for sialyl-T antigen type O-glycan analysis. (CD BioGlyco)

Publication

Paper Title: Inhibition of mucin-type O-glycosylation through metabolic processing and incorporation of N-thioglycolyl-D-galactosamine peracetate (Ac₅GalNTGc)

Technology: Glycoengineering Techniques Based on Unnatural GalNAc Analogs

Journal: Journal of the American Chemical Society

IF: 12.3761

Published: 2015

Results: The effect of GalNAc analogs on cell surface glycosylation was investigated using Jurkat cells as a model. The results by mass spectrometry showed the presence of various processed O-glycan structures such as sialyl-T (trisaccharide) in untreated Jurkat cells. While peracetyl N-thioglycolyl-d-galactosamine (Ac₅GalNTGc, 1) treatment inhibited their expression. Only very low levels of sialyl-T were present in treated cells. Non-natural GalNAc analogs would serve as a primary probe to study the relationship between the structure and function of mucins.

Fig.4 MALDI-TOF/TOF spectra revealed the presence of elaborated O-glycans in Jurkat cells and their suppression by 1. (Agarwal, et al., 2015)

Applications

• Lipid and protein glycosylation is altered in cancer cells. Glycoengineering analysis services are used to study the function of glycosylation in cancer cells.
• Glycoengineering techniques have an important role in anti-tumor research. Researchers use this technique to study the function of altered glycosylation in drug resistance in antitumor therapy.
• Sialic acid T antigen is associated with the development of other diseases. Examples include mucin-type O-glycan biosynthesis-deficient diseases. Glycoengineering techniques are used to study the mechanisms of other disease occurrences.

Advantages

• Our studies targeting O-glycans have high coverage. Complex biological matrices can be studied, such as cells, tissues, etc.
• We provide detailed experimental analysis reports, including experimental procedures, O-glycan analysis results, bioinformatics analysis, etc.
• The complete glycan analysis technology helps researchers study the role of altered glycosylation in tumor migration, proliferation, etc. more efficiently.

CD BioGlyco uses an advanced glycoengineering platform with LC chromatography and others to provide efficient and accurate sialyl-T antigen type O-glycan glycoengineering services. All you need to do is tell us the purpose of your experiment. We will complete all the experiments from glycoprotein extraction, and cleavage to mass spectrometry analysis. Welcome to contact us for more detailed information about O-glycan analysis.

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