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Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity
SM. Alavi, P. Postlerová-Maňásková, A. Hatef, M. Pšenička, J. Pěknicová, K. Inaba, A. Ciereszko, O. Linhart,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
ProQuest Central
od 1997-01-01 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2003-03-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 1997-01-01 do Před 1 rokem
- MeSH
- akrosin metabolismus MeSH
- akrozom enzymologie MeSH
- analýza rozptylu MeSH
- histologické techniky veterinární MeSH
- imunoelektronová mikroskopie veterinární MeSH
- inhibitory proteas farmakologie MeSH
- motilita spermií účinky léků fyziologie MeSH
- neparametrická statistika MeSH
- proteasy farmakologie MeSH
- rosanilinová barviva MeSH
- ryby fyziologie MeSH
- sperma enzymologie MeSH
- spermie účinky léků enzymologie fyziologie MeSH
- tosylfenylalanylchlormethylketon farmakologie MeSH
- tosyllysinchlormethylketon farmakologie MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
In mammals, proteases are present in sperm acrosome and play key role in fertilization. Sturgeon sperm has an acrosome, but its physiology, biochemistry, and potential role in fertilization are unknown. In the present study, we have observed high protease activity in acidic extract of intact sperm compared to that of seminal plasma in sterlet (Acipenser ruthenus). The protease activity was decreased and increased in acidic extract of motility-activated sperm and in the activation medium, respectively. Molecular analysis revealed total protease and serine (acrosin) protease activities in sperm acidic extract which was accumulated in a protein band with relative molecular mass of 35 kDa. Immunoelectron microscopy using an affinity-purified polyclonal antibody for boar acrosin localized the protease at the acrosome region. Moreover, initiation of sperm motility was inhibited after activation in the presence of inhibitors for both trypsin-like and chymotrypsin-like proteases, while the effects of protease inhibitors on sperm velocity were uncertain. Our results indicate similarities in physiology and biochemistry of acrosome between sturgeon and mammals and suggest potential role of protease in the initiation of sperm motility in sturgeon.
Citace poskytuje Crossref.org
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