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Glycosylation in cancer: mechanisms and clinical implications

Glycosylation in cancer: mechanisms and clinical implications Glycosylation is a key cellular mechanism regulating several physiological and pathological functions. Alterations in glycoproteins, glycosphingolipids and proteoglycans are common features of cancer cells. The most-widely occurring cancer-associated changes in protein glycosylation are increased sialylation, increased branched-glycan structures and overexpression of 'core' fucosylation. The overexpression of branched-N-glycan structures interferes with epithelial cadherin-mediated cell–cell adhesion, promoting tumour cell dissociation and invasion. Modifications of integrins with branched N-glycans, truncated O-glycans and/or sialylated structures modulate tumour cell–matrix interactions, fostering the process of tumour cell migration. Altered expression of proteoglycans and their glycosaminoglycan chains interfere with extracellular signalling molecules and modulate the activation of tyrosine kinase protein receptors. Altered glycosylation of growth factor receptors and the modified expression of gangliosides affect cancer cell signal transduction pathways, modulating tumour cell growth and proliferation. Glycans and their corresponding endogenous carbohydrate-recognition lectins are key regulators of the inflammation and immune response towards the tumour cells. Several serological markers currently used in the clinic are based on the detection of circulating glycoproteins or glycoconjugates with altered glycosylation. Glycans have major potential applications in improving early diagnosis, determination of prognosis and risk stratification, as well as in serving as markers of specific therapeutic targets. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Reviews Cancer Springer Journals

Glycosylation in cancer: mechanisms and clinical implications

Nature Reviews Cancer , Volume 15 (9) – Aug 20, 2015

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References (245)

Publisher
Springer Journals
Copyright
Copyright © 2015 by Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
Subject
Biomedicine; Biomedicine, general; Cancer Research
ISSN
1474-175X
eISSN
1474-1768
DOI
10.1038/nrc3982
Publisher site
See Article on Publisher Site

Abstract

Glycosylation is a key cellular mechanism regulating several physiological and pathological functions. Alterations in glycoproteins, glycosphingolipids and proteoglycans are common features of cancer cells. The most-widely occurring cancer-associated changes in protein glycosylation are increased sialylation, increased branched-glycan structures and overexpression of 'core' fucosylation. The overexpression of branched-N-glycan structures interferes with epithelial cadherin-mediated cell–cell adhesion, promoting tumour cell dissociation and invasion. Modifications of integrins with branched N-glycans, truncated O-glycans and/or sialylated structures modulate tumour cell–matrix interactions, fostering the process of tumour cell migration. Altered expression of proteoglycans and their glycosaminoglycan chains interfere with extracellular signalling molecules and modulate the activation of tyrosine kinase protein receptors. Altered glycosylation of growth factor receptors and the modified expression of gangliosides affect cancer cell signal transduction pathways, modulating tumour cell growth and proliferation. Glycans and their corresponding endogenous carbohydrate-recognition lectins are key regulators of the inflammation and immune response towards the tumour cells. Several serological markers currently used in the clinic are based on the detection of circulating glycoproteins or glycoconjugates with altered glycosylation. Glycans have major potential applications in improving early diagnosis, determination of prognosis and risk stratification, as well as in serving as markers of specific therapeutic targets.

Journal

Nature Reviews CancerSpringer Journals

Published: Aug 20, 2015

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