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O-linked mucin-type glycosylation in breast cancer

Research output: Contribution to journalArticlepeer-review

Original languageEnglish
Pages (from-to)779-788
Number of pages10
JournalBiochemical Society Transactions
Issue number4
Early online date14 Jun 2018
Accepted/In press16 May 2018
E-pub ahead of print14 Jun 2018
PublishedAug 2018


King's Authors


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 a number of mechanisms involved including increased/altered expression of glycosyltransferases and relocalization 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 microenvironment 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.

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