Altered glycosylation of proteins in cancer: what is the potential for new anti-tumour strategies

Brooks, S.A., Carter, T.M., Royle, L., Harvey, D.J., Fry, S., Kinch, C., Dwek, R.A. and Rudd, P.M. 2008. Altered glycosylation of proteins in cancer: what is the potential for new anti-tumour strategies. Anti-Cancer Agents in Medicinal Chemistry. 8 (1), pp. 2-21.

TitleAltered glycosylation of proteins in cancer: what is the potential for new anti-tumour strategies
AuthorsBrooks, S.A., Carter, T.M., Royle, L., Harvey, D.J., Fry, S., Kinch, C., Dwek, R.A. and Rudd, P.M.
Abstract

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.

JournalAnti-Cancer Agents in Medicinal Chemistry
Journal citation8 (1), pp. 2-21
ISSN1871-5206
YearJan 2008
PublisherBentham Science Publishers
Publication dates
PublishedJan 2008

Related outputs

Cadherin-5: a biomarker for metastatic breast cancer with optimum efficacy in oestrogen receptor-positive breast cancers with vascular invasion
Fry, S., Robertson, C.E., Swann, R. and Dwek, M. 2016. Cadherin-5: a biomarker for metastatic breast cancer with optimum efficacy in oestrogen receptor-positive breast cancers with vascular invasion. British Journal of Cancer. 114, pp. 1019-1026. https://doi.org/10.1038/bjc.2016.66

A targeted glycoproteomic approach identifies cadherin-5 as a novel biomarker of metastatic breast cancer
Fry, S., Sinclair, J., Timms, J.F., Leathem, A. and Dwek, M. 2013. A targeted glycoproteomic approach identifies cadherin-5 as a novel biomarker of metastatic breast cancer. Cancer Letters. 328 (2), pp. 335-344. https://doi.org/10.1016/j.canlet.2012.10.011

Lectin array based strategies for identifying metastasis-associated changes in glycosylation
Fry, S., Afrough, B., Leathem, A. and Dwek, M. 2012. Lectin array based strategies for identifying metastasis-associated changes in glycosylation. Methods in Molecular Biology. 878, pp. 267-272. https://doi.org/10.1007/978-1-61779-854-2_18

Association of serum anti-Tn IgM with breast cancer recurrence
Afrough, B., Fry, S., Lomax-Browne, H., Perkins, A., Leathem, A. and Dwek, M. 2011. Association of serum anti-Tn IgM with breast cancer recurrence. Immunology. 135 (Supp.1), p. 153. https://doi.org/10.1111/j.1365-2567.2011.03534.x

Lectin microarray profiling of metastatic breast cancers
Fry, S., Afrough, B., Lomax-Browne, H., Timms, J.F., Velentzis, L.S. and Leathem, A. 2011. Lectin microarray profiling of metastatic breast cancers. Glycobiology. 21 (8), pp. 1060-1070. https://doi.org/10.1093/glycob/cwr045

Abstract LB14 - Lectin microarray profilling of metastatic breast cancers
Fry, S., Afrough, B., Lomax-Browne, H., Timms, J.F., Velentzis, L.S. and Dwek, M. 2011. Abstract LB14 - Lectin microarray profilling of metastatic breast cancers. National Cancer Research Institute (NCRI) Cancer Conference 2011. BT Convention Centre, Liverpool, UK 06 - 09 Nov 2011

The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors
Van den Steen, P.E., Van Aelst, I., Hvidberg, V., Piccard, H., Fiten, P., Jacobsen, C., Moestrup, S.K., Fry, S., Royle, L., Wormald, M.R., Wallis, R., Rudd, P.M., Dwek, R.A. and Opdenakker, G. 2006. The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors. Journal of Biological Chemistry. 281 (27), pp. 18626-18637.

Cancer-associated glycoforms of gelatinase B exhibit a decreased level of binding to galectin-3
Fry, S., Van den Steen, P.E., Royle, L., Wormald, M.R., Leathem, A., Opdenakker, G., McDonnell, J.M., Dwek, R.A. and Rudd, P.M. 2006. Cancer-associated glycoforms of gelatinase B exhibit a decreased level of binding to galectin-3. Biochemistry. 45 (51), pp. 15249-15258. https://doi.org/10.1021/bi061254l

Differential glycosylation of gelatinase B from neutrophils and breast cancer cells
Fry, S., Van den Steen, P.E., Royle, L., Wormald, M.R., Leathem, A., Opdenakker, G., Rudd, P.M. and Dwek, R.A. 2005. Differential glycosylation of gelatinase B from neutrophils and breast cancer cells. Advances in Experimental Medicine and Biology. 564, pp. 103-112. https://doi.org/10.1007/0-387-25515-X_18

Permalink - https://westminsterresearch.westminster.ac.uk/item/9136z/altered-glycosylation-of-proteins-in-cancer-what-is-the-potential-for-new-anti-tumour-strategies


Share this

Usage statistics

159 total views
0 total downloads
These values cover views and downloads from WestminsterResearch and are for the period from September 2nd 2018, when this repository was created.