These authors contributed equally to this work.
Cell surface protein glycosylation in cancer
Article first published online: 4 MAR 2014
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Special Issue: REVIEWS 2014
Volume 14, Issue 4-5, pages 525–546, March 2014
How to Cite
Christiansen, M. N., Chik, J., Lee, L., Anugraham, M., Abrahams, J. L. and Packer, N. H. (2014), Cell surface protein glycosylation in cancer. Proteomics, 14: 525–546. doi: 10.1002/pmic.201300387
Colour Online: See the article online to view Fig. 1 in colour.
- Issue published online: 4 MAR 2014
- Article first published online: 4 MAR 2014
- Accepted manuscript online: 12 DEC 2013 08:55PM EST
- Manuscript Accepted: 11 NOV 2013
- Manuscript Revised: 7 NOV 2013
- Manuscript Received: 31 AUG 2013
- Membrane proteins
Glycosylation of proteins is one of the most important PTMs, with more than half of all human proteins estimated to be glycosylated. It is widely known that aberrant glycosylation has been implicated in many different diseases due to changes associated with biological function and protein folding. In cancer, there is increasing evidence pertaining to the role of glycosylation in tumour formation and metastasis. Alterations in cell surface glycosylation, particularly terminal motifs, can promote invasive behaviour of tumour cells that ultimately lead to the progression of cancer. While a majority of studies have investigated protein glycosylation changes in cancer cell lines and tumour tissue for individual cancers, the review presented here represents a comprehensive, in-depth overview of literature on the structural changes of glycosylation and their associated synthetic enzymes in five different cancer types originating from the breast, colon, liver, skin and ovary. More importantly, this review focuses on key similarities and differences between these cancers that reflect the importance of structural changes of cell surface N- and O-glycans, such as sialylation, fucosylation, degree of branching and the expression of specific glycosyltransferases for each cancer. It is envisioned that the understanding of these biologically relevant glycan alterations on cellular proteins will facilitate the discovery of novel glycan-based biomarkers which could potentially serve as diagnostic and prognostic indicators of cancer.