title: Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity.
abstract: 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.
authors.affiliation: Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, University of South Bohemia, 389 25, Vodňany, Czech Republic, alavi@af.czu.cz.
authors.forename: Sayyed Mohammad Hadi
authors.initials: SM
authors.lastname: Alavi
authors.forename: Pavla
authors.initials: P
authors.lastname: Postlerová-Maňásková
authors.forename: Azadeh
authors.initials: A
authors.lastname: Hatef
authors.forename: Martin
authors.initials: M
authors.lastname: Pšenička
authors.forename: Jana
authors.initials: J
authors.lastname: Pěknicová
authors.forename: Kazuo
authors.initials: K
authors.lastname: Inaba
authors.forename: Andrzej
authors.initials: A
authors.lastname: Ciereszko
authors.forename: Otomar
authors.initials: O
authors.lastname: Linhart
mesh_terms: D000176:Acrosin / Q000378:metabolism; D000177:Acrosome / Q000201:enzymology; D000704:Analysis of Variance; D000818:Animals; D005399:Fishes / Q000502:physiology*; D006652:Histological Techniques / Q000662:veterinary; D008297:Male; D016253:Microscopy, Immunoelectron / Q000662:veterinary; D010447:Peptide Hydrolases / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000494:pharmacology*; D012394:Rosaniline Dyes; D012661:Semen / Q000201:enzymology; D013081:Sperm Motility / Q000187:drug effects* / Q000502:physiology; D013094:Spermatozoa / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology*; D018709:Statistics, Nonparametric; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology
chemical_list: D011480:Protease Inhibitors; D012394:Rosaniline Dyes; D014107:Tosyllysine Chloromethyl Ketone; D014108:Tosylphenylalanyl Chloromethyl Ketone; D010447:Peptide Hydrolases; D000176:Acrosin; C004692:coomassie Brilliant Blue