Mechanisms of cancer-associated glycosylation changes.

00:05 EST 29th November 2014 | BioPortfolio

Summary of "Mechanisms of cancer-associated glycosylation changes."

Cell membrane glycoconjugates undergo characteristic changes as a consequence of neoplastic transformation. The cancer-associated carbohydrate structures play key roles in cancer progression by altering the cell-cell and cell-environment interactions. In this review, we will discuss some of the most relevant cancer-associated carbohydrate structures, including the b1,6-branching of N-linked chains, the sialyl Lewis antigens, the a2,6-sialylated lactosamine, the Thomsen-Friedenreich-related antigens and gangliosides. We will describe the mechanisms leading to the expression of these structures and their interactions with sugar binding molecules, such as selectins and galectins. Finally, we will discuss how the glycosylation machinery of the cell is controlled by signal transduction pathways, epigenetic mechanisms and responds to hypoxia.

Affiliation

Department of Experimental Pathology, University of Bologna, Via S. Giacomo 14, 40126 Bologna, Italy.

Journal Details

This article was published in the following journal.

Name: Frontiers in bioscience : a journal and virtual library
ISSN: 1093-4715
Pages: 670-99

Links

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Medical and Biotech [MESH] Definitions

A genetically heterogeneous group of heritable disorders resulting from defects in protein N-glycosylation.

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