O-glycan recognition and function in mice and human cancers.
O-glycan recognition and function in mice and human cancers.
Biochem J. 2020 Apr 30;477(8):1541-1564
Authors: Cervoni GE, Cheng JJ, Stackhouse KA, Heimburg-Molinaro J, Cummings RD
Abstract
Protein glycosylation represents a nearly ubiquitous post-translational modification, and altered glycosylation can result in clinically significant pathological consequences. Here we focus on O-glycosylation in tumor cells of mice and humans. O-glycans are those linked to serine and threonine (Ser/Thr) residues via N-acetylgalactosamine (GalNAc), which are oligosaccharides that occur widely in glycoproteins, such as those expressed on the surfaces and in secretions of all cell types. The structure and expression of O-glycans are dependent on the cell type and disease state of the cells. There is a great interest in O-glycosylation of tumor cells, as they typically express many altered types of O-glycans compared with untransformed cells. Such altered expression of glycans, quantitatively and/or qualitatively on different glycoproteins, is used as circulating tumor biomarkers, such as CA19-9 and CA-125. Other tumor-associated carbohydrate antigens (TACAs), such as the Tn antigen and sialyl-Tn antigen (STn), are truncated O-glycans commonly expressed by carcinomas on multiple glycoproteins; they contribute to tumor development and serve as potential biomarkers for tumor presence and stage, both in immunohistochemistry and in serum diagnostics. Here ...
Source: The Biochemical Journal - Category: Biochemistry Authors: Cervoni GE, Cheng JJ, Stackhouse KA, Heimburg-Molinaro J, Cummings RD Tags: Biochem J Source Type: research
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