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.
Highlights
While genomics and proteomics are producing unparalleled discoveries that are advancing the understanding of biological processes and cancer, this is often incomplete without a knowledge and understanding of post-translational modifications (PTMs) of proteins, which greatly increase the size, diversity and function of the proteome [1]
It is becoming clear that a reductionist approach will not adequately explain the complex interactions between glycans and glycan-binding proteins, glycan:glycan interactions and cell:cell interactions mediated by glycans
Within the breast cancer micro-environment cross-talk occurs between cancer cells, immune cells and stromal cells [77], often mediated by glycan-binding proteins [72]; complex co-culture methods will be needed to really investigate and dissect the role of aberrant mucin-type glycosylation in breast cancer
Summary
While genomics and proteomics are producing unparalleled discoveries that are advancing the understanding of biological processes and cancer, this is often incomplete without a knowledge and understanding of post-translational modifications (PTMs) of proteins, which greatly increase the size, diversity and function of the proteome [1]. It is becoming clear that a reductionist approach will not adequately explain the complex interactions between glycans and glycan-binding proteins, glycan:glycan interactions and cell:cell interactions mediated by glycans.
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