title: Cell surface protein glycosylation in cancer.
abstract: 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.
authors: Department of Chemistry and Biomolecular Sciences, Faculty of Science, Biomolecular Frontiers Research Centre, Macquarie University, Sydney, Australia.
authors: Maja N
authors: MN
authors: Christiansen
authors: Jenny
authors: J
authors: Chik
authors: Ling
authors: L
authors: Lee
authors: Merrina
authors: M
authors: Anugraham
authors: Jodie L
authors: JL
authors: Abrahams
authors: Nicolle H
authors: NH
authors: Packer
mesh_terms: D014408:Biomarkers, Tumor / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D005936:Glucans / Q000378:metabolism; D006031:Glycosylation; D016695:Glycosyltransferases / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009369:Neoplasms / Q000175:diagnosis / Q000378:metabolism* / Q000473:pathology; D011379:Prognosis
chemical_list: D014408:Biomarkers, Tumor; D005936:Glucans; D008565:Membrane Proteins; D016695:Glycosyltransferases
keywords: Biomarkers; Cancer; Glycoproteomics; Glycosylation; Glycosyltransferases; Membrane proteins