Altered Glycosylation of Proteins in Cancer: What Is the Potential for New Anti-Tumour Strategies

Author(s): S. A. Brooks, T. M. Carter, L. Royle, D. J. Harvey, S. A. Fry, C. Kinch, R. A. Dwek, P. M. Rudd

Journal Name: Anti-Cancer Agents in Medicinal Chemistry
(Formerly Current Medicinal Chemistry - Anti-Cancer Agents)

Volume 8 , Issue 1 , 2008

Become EABM
Become Reviewer


It is becoming increasingly apparent that cell surface oligosaccharides play pivotal roles as recognition molecules in a range of cell communication and adhesion processes. Alterations in cellular glycosylation are also associated with diseases, including cancer, and may have functional significance. This paper gives an overview of the complex topic of cellular glycosylation mechanisms and reviews the well-documented alterations in cellular glycosylation of proteins in malignancy. One particular type of cancer-associated glycosylation change, the incomplete synthesis of O-linked glycans, is highlighted, and its possible functional significance in cancer cell metastatic mechanisms is discussed. The significance that cancer-associated changes in glycoprotein glycosylation may have in new approaches to anti-tumour therapies is explored.

Keywords: Glycoprotein, glycosylation, glycan analysis, cancer, metastasis, Helix pomatia agglutinin, HPA

open access plus

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2008
Page: [2 - 21]
Pages: 20
DOI: 10.2174/187152008783330860

Article Metrics

PDF: 39