O-linked mucin-type glycosylation in breast cancer

Biochem Soc Trans. 2018 Aug 20;46(4):779-788. doi: 10.1042/BST20170483. Epub 2018 Jun 14.

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.

Keywords: O-linked mucin-type glycosylation; breast cancer; glycosyltransferases; immunotherapy; lectins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylgalactosamine / metabolism
  • Biological Transport
  • Breast Neoplasms / immunology
  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology
  • Disease Progression
  • Female
  • Gene Expression Regulation, Enzymologic
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism
  • Glycosylation
  • Glycosyltransferases / genetics
  • Glycosyltransferases / metabolism
  • Golgi Apparatus / enzymology
  • Golgi Apparatus / metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • Mucin-1 / metabolism*
  • Neoplasm Metastasis
  • Tumor Microenvironment

Substances

  • MUC1 protein, human
  • Mucin-1
  • Glycosyltransferases
  • Glycoside Hydrolases
  • Acetylgalactosamine