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 inInternational journal of molecular sciences Vol. 25; no. 11; p. 5725
Main Authors Slivka, Ekaterina V, Shilova, Nadezhda V, Obraztsova, Ekaterina A, Kapustkina, Daria S, Khaidukov, Sergey V, Nokel, Alexey Yu, Ryzhov, Ivan M, Henry, Stephen M, Bovin, Nicolai V, Rapoport, Eugenia M
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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.
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
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Keywords endothelial cells
extracellular vesicles
glycans
microvesicles
glycosphingolipids
Language English
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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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Volume 25
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