Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins
aut.relation.issue | 11 | |
aut.relation.journal | International Journal of Molecular Sciences | |
aut.relation.startpage | 5725 | |
aut.relation.volume | 25 | |
dc.contributor.author | Slivka, EV | |
dc.contributor.author | Shilova, NV | |
dc.contributor.author | Obraztsova, EA | |
dc.contributor.author | Kapustkina, DS | |
dc.contributor.author | Khaidukov, SV | |
dc.contributor.author | Nokel, AY | |
dc.contributor.author | Ryzhov, IM | |
dc.contributor.author | Henry, SM | |
dc.contributor.author | Bovin, NV | |
dc.contributor.author | Rapoport, EM | |
dc.date.accessioned | 2024-10-14T03:41:24Z | |
dc.date.available | 2024-10-14T03:41:24Z | |
dc.date.issued | 2024-05-24 | |
dc.description.abstract | Glycans of MVs are proposed to be candidates for mediating targeting specificity or at least promoting it. In contrast to exosomes, glycomic studies of MVs are largely absent. We studied the glycoprofile of endothelial cell-derived MVs using 21 plant lectins, and the results show the dominance of oligolactosamines and their α2-6-sialylated forms as N-glycans and low levels of α2-3-sialylated glycans. The low levels of α2-3-sialosides could not be explained by the action of extracellular glycosidases. Additionally, the level of some Man-containing glycans was also decreased in MVs. Spatial masking as the causative relationship between these low level glycans (as glycosphingolipids) by integral proteins or proteoglycans (thus, their lack of interaction with lectins) seems unlikely. The results suggest that integral proteins do not pass randomly into MVs, but instead only some types, differing in terms of their specific glycosylation, are integrated into MVs. | |
dc.identifier.citation | International Journal of Molecular Sciences, ISSN: 1661-6596 (Print); 1422-0067 (Online), MDPI AG, 25(11), 5725-. doi: 10.3390/ijms25115725 | |
dc.identifier.doi | 10.3390/ijms25115725 | |
dc.identifier.issn | 1661-6596 | |
dc.identifier.issn | 1422-0067 | |
dc.identifier.uri | http://hdl.handle.net/10292/18127 | |
dc.language | eng | |
dc.publisher | MDPI AG | |
dc.relation.uri | https://www.mdpi.com/1422-0067/25/11/5725 | |
dc.rights | © 2024 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). | |
dc.rights.accessrights | OpenAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.subject | endothelial cells | |
dc.subject | extracellular vesicles | |
dc.subject | glycans | |
dc.subject | glycosphingolipids | |
dc.subject | microvesicles | |
dc.subject | 3101 Biochemistry and Cell Biology | |
dc.subject | 31 Biological Sciences | |
dc.subject | 0399 Other Chemical Sciences | |
dc.subject | 0604 Genetics | |
dc.subject | 0699 Other Biological Sciences | |
dc.subject | Chemical Physics | |
dc.subject | 3101 Biochemistry and cell biology | |
dc.subject | 3107 Microbiology | |
dc.subject | 3404 Medicinal and biomolecular chemistry | |
dc.subject.mesh | Polysaccharides | |
dc.subject.mesh | Plant Lectins | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Endothelial Cells | |
dc.subject.mesh | Glycosylation | |
dc.subject.mesh | Cell-Derived Microparticles | |
dc.subject.mesh | Endothelial Cells | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Polysaccharides | |
dc.subject.mesh | Plant Lectins | |
dc.subject.mesh | Glycosylation | |
dc.subject.mesh | Cell-Derived Microparticles | |
dc.subject.mesh | Polysaccharides | |
dc.subject.mesh | Plant Lectins | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Endothelial Cells | |
dc.subject.mesh | Glycosylation | |
dc.subject.mesh | Cell-Derived Microparticles | |
dc.title | Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins | |
dc.type | Journal Article | |
pubs.elements-id | 569716 |
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