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Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity |
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| Authors: | Sayyed Mohammad Hadi Alavi Pavla Postlerová-Maňásková Azadeh Hatef Martin P?eni?ka Jana Pěknicová Kazuo Inaba Andrzej Ciereszko Otomar Linhart |
| Institution: | 1. Faculty of Fisheries and Protection of Waters, Research Institute of Fish Culture and Hydrobiology, University of South Bohemia, 389 25, Vodňany, Czech Republic 2. Department of Biological Resource Sciences, Faculty of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Sendai, 981-8555, Japan 7. Department of Veterinary Sciences, Faculty of Agrobiology, Food and Natural Resources, Czech University of Life Sciences, 165 21, Prague 6, Czech Republic 3. Laboratory of Reproductive Biology, Institute of Biotechnology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20, Prague, Czech Republic 4. Department of Veterinary Biomedical Sciences, Western College of Veterinary Medicine, University of Saskatchewan, Saskatoon, SK, S7N 5B4, Canada 5. Shimoda Marine Research Center, University of Tsukuba, Shimoda 5-10-1, Shizuoka, 415-0025, Japan 6. Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, 10-747, Olsztyn, Poland |
| 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. |
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