Evidence map›Paper›PMID 34540145›Full record

ArticleUpsala journal of medical sciences2021

Assembly of tetraspanins, galectin-3, and distinct N-glycans defines the solubilization signature of seminal prostasomes from normozoospermic and oligozoospermic men.

Tamara Janković, Jelena Danilović Luković, Irena Miler, Ninoslav Mitić, Ljiljana Hajduković, Miroslava Janković

Open access · diamondAbstract read
In one paragraph

Article in Upsala journal of medical sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity.Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia · 2024
    Article
  3. Review
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Tamara JankovićUniversity of Belgrade, Institute for the Application of Nuclear Energy, INEP, Belgrade, Serbia.
Jelena Danilović LukovićUniversity of Belgrade, Institute for the Application of Nuclear Energy, INEP, Belgrade, Serbia.
Irena MilerUniversity of Belgrade, Institute for the Application of Nuclear Energy, INEP, Belgrade, Serbia.
Ninoslav MitićUniversity of Belgrade, Institute for the Application of Nuclear Energy, INEP, Belgrade, Serbia.
Ljiljana HajdukovićUniversity of Belgrade, Institute for the Application of Nuclear Energy, INEP, Belgrade, Serbia.
Miroslava JankovićUniversity of Belgrade, Institute for the Application of Nuclear Energy, INEP, Belgrade, Serbia.
University of Belgrade · RS

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProstasomes, 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.

methodsProstasomes 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.

resultsComparative 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.

conclusionsSolubilization 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.

Indexed as

Galectin 3SemenHumansMalePolysaccharidesSpermatozoaTetraspaninsGalectin 3PolysaccharidesTetraspaninsCD63CD9detergent sensitivityExtracellular vesiclesgamma-glutamyl transferasemolecular patternsnormozoospermiaoligozoospermia

Identifiers

PMID34540145
PMCPMC8431989
OpenAlexW3196381838

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.