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Glycan Node Analysis: A Bottom-up Approach to Glycomics

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O-glycan recognition and function in mice and human cancers.

Gabrielle E Cervoni¹, Jane J Cheng¹, Kathryn A Stackhouse¹

¹Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, CLS 11087, 3 Blackfan Circle, Boston, MA 02115, U.S.A.

The Biochemical Journal

|April 30, 2020

Summary

Altered O-glycosylation in tumor cells, involving specific oligosaccharides, impacts cancer development and serves as biomarkers. Understanding these changes offers new avenues for cancer diagnostics and therapeutics.

Keywords:

O-glycans glycan function glycan recognition human cancers human glycans mouse glycans

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Area of Science:

Biochemistry
Glycobiology
Oncology

Background:

Protein glycosylation, a common post-translational modification, has significant pathological consequences when altered.
O-glycosylation, the attachment of N-acetylgalactosamine (GalNAc) to serine/threonine residues, produces diverse oligosaccharides crucial for cell function.
Tumor cells exhibit distinct O-glycan profiles compared to normal cells, making them key areas of research.

Purpose of the Study:

To explore O-glycosylation in murine and human tumor cells, focusing on colorectal, breast, and pancreatic cancers.
To detail the structure, function, and recognition of O-glycans in the context of cancer.
To highlight the potential of O-glycosylation knowledge for developing novel cancer diagnostics and therapeutics.

Main Methods:

Review of existing literature on O-glycosylation in cancer.
Analysis of O-glycan structures and their expression patterns in various tumor types.
Examination of the role of O-glycans as tumor-associated carbohydrate antigens (TACAs).

Main Results:

Tumor cells characteristically display altered O-glycan structures, both quantitatively and qualitatively.
Specific O-glycans, such as Tn antigen and sialyl-Tn antigen (STn), are prevalent in carcinomas and contribute to tumor progression.
Altered O-glycans function as valuable circulating tumor biomarkers (e.g., CA19-9, CA-125) and immunohistochemical markers.

Conclusions:

O-glycosylation patterns are significantly dysregulated in cancer cells.
Tumor-associated O-glycans offer promising targets for cancer diagnosis and staging.
Exploiting the understanding of tumor O-glycosylation presents substantial opportunities for advancing cancer treatment strategies.