O-linked mucin-type glycosylation in breast cancer. (14th June 2018)

• Record Type: Journal Article
• Authors: Burchell, Joy M.; Beatson, Richard; Graham, Rosalind; Taylor-Papadimitriou, Joyce; Tajadura-Ortega, Virginia
• Is Part Of: Biochemical Society transactions. Volume 46:Number 4(2018)
• Page Start: 779
• Page End: 788
• Publication Date: 2018-06-14
• Subjects: breast cancer -- glycosyltransferases -- immunotherapy -- lectins -- O-linked mucin-type glycosylation; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20170483
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Changes in mucin-type O-linked glycosylation are seen in over 90% of breast cancers where increased sialylation is often observed and a change from branched glycans to linear glycans is often seen. There are many mechanisms involved including increased/altered expression of glycosyltransferases and relocalisation to the endoplasmic reticulum of the enzymes responsible for the addition of the first sugar, N -acetyl-d -galactosamine. It is now becoming clear that these changes can contribute to tumour growth and progression by modulating the micro-environment through glycan-sensing lectins expressed on immune cells, by modulating interactions with tumour surface receptors and by binding to selectins. The understanding of how changes in mucin-type O-linked glycosylation influence tumour growth and progression reveals new potential targets for therapeutic intervention in the treatment of breast cancer.