GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
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Aurélie Cazet
Abstract
The disialoganglioside GD3 is an oncofetal marker of a variety of human tumors including melanoma and neuroblastoma, playing a key role in tumor progression. GD3 and 9-O-acetyl-GD3 are overexpressed in approximately 50% of invasive ductal breast carcinoma, but no relationship has been established between disialoganglioside expression and breast cancer progression. In order to determine the effect of GD3 expression on breast cancer development, we analyzed the biosynthesis of gangliosides in several breast epithelial cell lines including MDA-MB-231, MCF-7, BT-20, T47-D, and MCF10A, by immunocytochemistry, flow cytometry, and real-time PCR. Our results show that, in comparison to tumors, cultured breast cancer cells express a limited pattern of gangliosides. Disialogangliosides were not detected in any cell line and GM3 was only observed at the cell surface of MDA-MB-231 cells. To evaluate the influence of GD3 in breast cancer cell behavior, we established and characterized MDA-MB-231 cells overexpressing GD3 synthase. We show that GD3 synthase expressing cells accumulate GD3, GD2, and GT3 at the cell surface. Moreover, GD3 synthase overexpression bypasses the need of serum for cell growth and increases cell migration. This suggests that GD3 synthase overexpression may contribute to increasing the malignant properties of breast cancer cells.
©2009 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Guest Editorial
- Highlight: Perspectives in glycobiology
- Cell biology and glycosylation: protein targeting by O- and N-linked glycosylation
- Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
- Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking
- Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
- MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
- Cell biology and glycosylation: carbohydrate-mediated recognition and signaling in cell proliferation and differentiation
- From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans
- Brain development needs sugar: the role of polysialic acid in controlling NCAM functions
- Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
- Glycosylation and disease
- Management of the human mucosal defensive barrier: evidence for glycan legislation
- Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
- GD3 synthase overexpression enhances proliferation and migration of MDA-MB-231 breast cancer cells
- Tumor-associated MUC1 glycopeptide epitopes are not subject to self-tolerance and improve responses to MUC1 peptide epitopes in MUC1 transgenic mice
- Protein-specific glycosylation and its control
- Protein-specific glycosylation: signal patches and cis-controlling peptidic elements
- O-glycosylation pattern of CD24 from mouse brain
- Advancements in analytical techniques
- Carbohydrate microarrays: key developments in glycobiology
- On-line nano-HPLC/ESI QTOF MS monitoring of α2–3 and α2–6 sialylation in granulocyte glycosphingolipidome
