Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins
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 ol...
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Published in | International journal of molecular sciences Vol. 25; no. 11; p. 5725 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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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. |
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AbstractList | 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. 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.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. |
Audience | Academic |
Author | Henry, Stephen M Shilova, Nadezhda V Ryzhov, Ivan M Bovin, Nicolai V Slivka, Ekaterina V Obraztsova, Ekaterina A Kapustkina, Daria S Nokel, Alexey Yu Khaidukov, Sergey V Rapoport, Eugenia M |
AuthorAffiliation | 2 National Medical Research Center for Obstetrics, Gynecology and Perinatology of the Ministry of Health of the Russian Federation, 4 Oparina Str., Moscow 117997, Russia 1 Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, 16/10 Miklukho-Maklaya Str., Moscow 117997, Russia; slivkaekaterina6@gmail.com (E.V.S.); pumatnv@gmail.com (N.V.S.); imryzhov@gmail.com (I.M.R.); eugenia_rapoport@mail.ru (E.M.R.) 3 School of Engineering, Auckland University of Technology, Auckland 1010, New Zealand; shenry@kodebiotech.com |
AuthorAffiliation_xml | – name: 2 National Medical Research Center for Obstetrics, Gynecology and Perinatology of the Ministry of Health of the Russian Federation, 4 Oparina Str., Moscow 117997, Russia – name: 1 Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, 16/10 Miklukho-Maklaya Str., Moscow 117997, Russia; slivkaekaterina6@gmail.com (E.V.S.); pumatnv@gmail.com (N.V.S.); imryzhov@gmail.com (I.M.R.); eugenia_rapoport@mail.ru (E.M.R.) – name: 3 School of Engineering, Auckland University of Technology, Auckland 1010, New Zealand; shenry@kodebiotech.com |
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Keywords | endothelial cells extracellular vesicles glycans microvesicles glycosphingolipids |
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Snippet | 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... |
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SubjectTerms | Cell-Derived Microparticles - metabolism Dendritic cells endothelial cells Endothelial Cells - metabolism Endothelium extracellular vesicles Flow cytometry glycans glycosphingolipids Glycosylation Humans Investigations Lectins Lipids Melanoma Membrane proteins microvesicles Plant lectins Plant Lectins - chemistry Plant Lectins - metabolism Plasma Polysaccharides Polysaccharides - chemistry Polysaccharides - metabolism Proteins Pulmonary arteries |
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Title | Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins |
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