Characterization of sperm surface protein patterns of ejaculated and capacitated boar sperm, with the detection of ZP binding candidates
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23916641
DOI
10.1016/j.ijbiomac.2013.07.014
PII: S0141-8130(13)00410-8
Knihovny.cz E-zdroje
- Klíčová slova
- PKDREJ protein, Sperm surface proteins, Zona pellucida-binding receptors,
- MeSH
- hmotnostní spektrometrie MeSH
- kapacitace spermií * MeSH
- membránové glykoproteiny metabolismus MeSH
- membránové proteiny metabolismus MeSH
- myši MeSH
- proteom MeSH
- proteomika metody MeSH
- spermie metabolismus MeSH
- Sus scrofa MeSH
- vazba proteinů MeSH
- zona pellucida metabolismus MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- myši MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- membránové glykoproteiny MeSH
- membránové proteiny MeSH
- proteom MeSH
Complementary molecules on the surface of both gametes are responsible for the interaction of sperm protein receptors with zona pellucida (ZP) saccharide structures, and many primary sperm receptors for ZP glycoproteins have been disclosed in various mammals. For our study, proteins were obtained from the surface of ejaculated and in vitro capacitated boar sperm. The isolated proteins were characterized by 1D- and 2D-electrophoretic protein profiles, and by glycoprotein staining. Our results show quantitative and qualitative differences in protein and glycoprotein patterns between ejaculated and capacitated sperm. Far-western blotting with ZP glycoproteins identified 17 interactions in the subproteome of the ejaculated sperm and 14 interactions in the subproteome of the capacitated sperm. High-molecular-mass proteins, coincident with binding to ZP, were sequence-identified. Angiotensin-converting enzyme (ACE), polycystic kidney disease receptor and egg jelly receptor (PKDREJ), and acrosin precursor were successfully identified. This is the first time PKDREJ has been identified on the surface of boar spermatozoa.
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