Surface glycans contribute to differences between seminal prostasomes from normozoospermic and oligozoospermic men

Ups J Med Sci. 2019 Apr;124(2):111-118. doi: 10.1080/03009734.2019.1592266. Epub 2019 Apr 8.

Abstract

Background: Extracellular vesicles (EVs), released from the plasma membrane or intracellular compartments, have a specific composition related to their parent cells, but they can, additionally, be modified by the extracellular environment. Although glycans are known to contribute to EV composition and may have biomedical importance as biomarkers and recognition signals, they have not been extensively investigated. In this study, seminal prostasomes, i.e. EVs from seminal plasma (SP) of normo- and oligozoospermic men, were analyzed in order to detect possible changes in their surface glycans under altered physiological conditions. Methods: Prostasomes were isolated from pooled SP by differential centrifugation and gel filtration, followed by glycobiochemical characterization using lectin/immune-transmission microscopy and ion-exchange chromatography. Results: Within the frame of overall similarity in protein composition, surface glycans specifically contributed to the differences between the examined groups of prostasomes in terms of presentation of sialylated and mannosylated moieties. These changes did not affect their anti-oxidative capacity, but implied a possible influence on the accessibility of galectin-3 to its ligands on the prostasomal surface. Conclusions: Subtle differences in the presentation of surface molecules may be helpful for differentiation among vesicles sharing the same physical properties. In addition, this may point to some unexpected regulatory mechanisms of interaction of distinct populations of vesicles with their binding partners.

Keywords: Glycosylation; prostasomes; seminal plasma; sialic acid.

Publication types

  • Comparative Study

MeSH terms

  • Antioxidants / chemistry
  • Biomarkers / metabolism
  • Centrifugation
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Galectin 3 / chemistry
  • Glycosylation
  • Humans
  • Ligands
  • Male
  • Microscopy, Electron, Transmission
  • N-Acetylneuraminic Acid / chemistry
  • Oligospermia / metabolism*
  • Oligospermia / physiopathology*
  • Polysaccharides / chemistry*
  • Prostate / metabolism*
  • Protein Binding
  • Reactive Oxygen Species / metabolism
  • Semen / metabolism*
  • Spermatozoa / metabolism*

Substances

  • Antioxidants
  • Biomarkers
  • Galectin 3
  • Ligands
  • Polysaccharides
  • Reactive Oxygen Species
  • N-Acetylneuraminic Acid

Grants and funding

This work was supported by the Ministry for Education, Science and Technological Development of the Republic of Serbia under Grant 173010.