O-linked mucin-type glycosylation in breast cancer

Joy M. Burchell; Richard Beatson; Rosalind Graham; Joyce Taylor-Papadimitriou; Virginia Tajadura-Ortega

doi:10.1042/BST20170483

O-linked mucin-type glycosylation in breast cancer

Joy M. Burchell, Richard Beatson, Rosalind Graham, Joyce Taylor-Papadimitriou, Virginia Tajadura-Ortega

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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 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.

Original language	English
Pages (from-to)	779-788
Number of pages	10
Journal	Biochemical Society Transactions
Volume	46
Issue number	4
Early online date	14 Jun 2018
DOIs	https://doi.org/10.1042/BST20170483
Publication status	Published - Aug 2018

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title = "O-linked mucin-type glycosylation in breast cancer",

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 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. ",

author = "Burchell, {Joy M.} and Richard Beatson and Rosalind Graham and Joyce Taylor-Papadimitriou and Virginia Tajadura-Ortega",

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AU - Beatson, Richard

AU - Graham, Rosalind

AU - Taylor-Papadimitriou, Joyce

AU - Tajadura-Ortega, Virginia

PY - 2018/8

Y1 - 2018/8

N2 - 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.

AB - 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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DO - 10.1042/BST20170483

M3 - Article

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SP - 779

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JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

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ER -

O-linked mucin-type glycosylation in breast cancer

Abstract

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