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EMBO Rep. 2006 Jun;7(6):599-604.

Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions.

Author information

1
Department of Medicine and Biochemistry, Human Mobility Research Centre, Queen's University, Kingston General Hospital, Angada 1, Kingston, Ontario K7L 2V7, Canada. brockhau@post.queensu.ca

Abstract

The glycoproteins of tumour cells are often abnormal, both in structure and in quantity. In particular, the mucin-type O-glycans have several cancer-associated structures, including the T and Tn antigens, and certain Lewis antigens. These structural changes can alter the function of the cell, and its antigenic and adhesive properties, as well as its potential to invade and metastasize. Cancer-associated mucin antigens can be exploited in diagnosis and prognosis, and in the development of cancer vaccines. The activities and Golgi localization of glycosyltransferases are the basis for the glycodynamics of cancer cells, and determine the ranges and amounts of specific O-glycans produced. This review focuses on the glycosyltransferases of colon and breast cancer cells that determine the pathways of mucin-type O-glycosylation, and the proposed functional and pathological consequences of altered O-glycans.

PMID:
16741504
PMCID:
PMC1479595
DOI:
10.1038/sj.embor.7400705
[Indexed for MEDLINE]
Free PMC Article

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