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Biomolecules 2015, 5(3), 1741-1761; doi:10.3390/biom5031741

Extracellular Vesicles from Ovarian Carcinoma Cells Display Specific Glycosignatures

1
Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, Oeiras 2780-157, Portugal
2
BET, Instituto de Biologia Experimental e Tecnológica, Oeiras 2780-157, Portugal
3
Skin Cancer Unit, German Cancer Research Center (DKFZ), Heidelberg 69120, Germany
4
Department of Dermatology, Venereology and Allergology, University Medical Center Mannheim, Ruprecht-Karl University of Heidelberg, Mannheim 68135, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Hans Vliegenthart
Received: 21 June 2015 / Revised: 22 June 2015 / Accepted: 28 July 2015 / Published: 4 August 2015
(This article belongs to the Special Issue Challenges in Glycan, Glycoprotein and Proteoglycan Research)
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Abstract

Cells release vesicles to the extracellular environment with characteristic nucleic acid, protein, lipid, and glycan composition. Here we have isolated and characterized extracellular vesicles (EVs) and total cell membranes (MBs) from ovarian carcinoma OVMz cells. EVs were enriched in specific markers, including Tsg101, CD63, CD9, annexin-I, and MBs contained markers of cellular membrane compartments, including calnexin, GRASP65, GS28, LAMP-1, and L1CAM. The glycoprotein galectin-3 binding protein (LGALS3BP) was strongly enriched in EVs and it contained sialylated complex N-glycans. Lectin blotting with a panel of lectins showed that EVs had specific glycosignatures relative to MBs. Furthermore, the presence of glycoproteins bearing complex N-glycans with α2,3-linked sialic acid, fucose, bisecting-GlcNAc and LacdiNAc structures, and O-glycans with the T-antigen were detected. The inhibition of N-glycosylation processing from high mannose to complex glycans using kifunensine caused changes in the composition of EVs and induced a decrease of several glycoproteins. In conclusion, the results showed that glycosignatures of EVs were specific and altered glycosylation within the cell affected the composition and/or dynamics of EVs release. Furthermore, the identified glycosignatures of EVs could provide novel biomarkers for ovarian cancer. View Full-Text
Keywords: glycosylation; extracellular vesicles; ovarian cancer; galectin-3-binding protein; glycosignatures; kifunensine; biomarkers glycosylation; extracellular vesicles; ovarian cancer; galectin-3-binding protein; glycosignatures; kifunensine; biomarkers
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Gomes, J.; Gomes-Alves, P.; Carvalho, S.B.; Peixoto, C.; Alves, P.M.; Altevogt, P.; Costa, J. Extracellular Vesicles from Ovarian Carcinoma Cells Display Specific Glycosignatures. Biomolecules 2015, 5, 1741-1761.

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