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Assembly of tetraspanins, galectin-3, and distinct N-glycans defines the solubilization signature of seminal prostasomes from normozoospermic and oligozoospermic men
dc.creator | Janković, Tamara | |
dc.creator | Danilović Luković, Jelena | |
dc.creator | Miler, Irena | |
dc.creator | Mitic, Ninoslav | |
dc.creator | Hajduković, Ljiljana | |
dc.creator | Janković, Miroslava | |
dc.date.accessioned | 2023-11-28T19:01:25Z | |
dc.date.available | 2023-11-28T19:01:25Z | |
dc.date.issued | 2021 | |
dc.identifier.issn | 0300-9734 | |
dc.identifier.uri | http://rimsi.imsi.bg.ac.rs/handle/123456789/2464 | |
dc.description.abstract | Background: Prostasomes, extracellular vesicles (EVs) abundantly present in seminal plasma, express distinct tetraspanins (TS) and galectin-3 (gal-3), which are supposed to shape their surface by an assembly of different molecular complexes. In this study, detergent-sensitivity patterns of membrane-associated prostasomal proteins were determined aiming at the solubilization signature as an intrinsic multimolecular marker and a new parameter suitable as a reference for the comparison of EVs populations in health and disease. Methods: Prostasomes were disrupted by Triton X-100 and analyzed by gel filtration under conditions that maintained complete solubilization. Redistribution of TS (CD63, CD9, and CD81), gal-3, gamma-glutamyltransferase (GGT), and distinct N-glycans was monitored using solid-phase lectin-binding assays, transmission electron microscopy, electrophoresis, and lectin blot. Results: Comparative data on prostasomes under normal physiology and conditions of low sperm count revealed similarity regarding the redistribution of distinct N-glycans and GGT, all presumed to be mainly part of the vesicle coat. In contrast to this, a greater difference was found in the redistribution of integral membrane proteins, exemplified by TS and gal-3. Accordingly, they were grouped into two molecular patterns mainly consisting of overlapped CD9/gal-3/wheat germ agglutinin-reactive glycoproteins and CD63/ GGT/concanavalin A-reactive glycoproteins. Conclusions: Solubilization signature can be considered as an all-inclusive distinction factor regarding the surface properties of a particular vesicle since it reflects the status of the parent cell and the extracellular environment, both of which contribute to the composition of spatial membrane arrangements. | sr |
dc.language.iso | en | sr |
dc.publisher | Upsala Medical Society | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/inst-2020/200019/RS | sr |
dc.rights | openAccess | sr |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.source | Upsala journal of medical sciences | sr |
dc.subject | Extracellular vesicles | sr |
dc.subject | detergent sensitivity | sr |
dc.subject | CD63 | sr |
dc.subject | CD9 | sr |
dc.subject | gamma-glutamyl transferase | sr |
dc.subject | molecular patterns | sr |
dc.subject | normozoospermia | sr |
dc.subject | oligozoospermia | sr |
dc.title | Assembly of tetraspanins, galectin-3, and distinct N-glycans defines the solubilization signature of seminal prostasomes from normozoospermic and oligozoospermic men | sr |
dc.type | article | sr |
dc.rights.license | BY | sr |
dc.citation.volume | 126 | |
dc.identifier.doi | 10.48101/ujms.v126.7673 | |
dc.identifier.fulltext | http://rimsi.imsi.bg.ac.rs/bitstream/id/6367/bitstream_6367.pdf | |
dc.type.version | publishedVersion | sr |