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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Acknowledgments
This work was supported by GACR P503/12/1834 (to J.P. and S.M.H.A.), AVOZ 50520701 (to P.P.-M), CENAKVA CZ.1.05/2.1.00/01.0024 (to O.L.), GACR P503/13/34049P (to A.H.), BIOCEVCZ.1.05/1.1.00/02.0109 (to J.P. and P.P.-M.), and UNCE204025/2012 (to J.P. and P.P.-M.). S.M.H. Alavi wrote the article during stay at the Tohoku University, supported by the Japan Society for the Promotion of Science. We warmly appreciate the Polish Institute of Animal Reproduction and Food Research, Tsukuba University and Japanese Association for Marine Biology, for supporting A. Ciereszko and K. Inaba.
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Alavi, S.M.H., Postlerová-Maňásková, P., Hatef, A. et al. Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity. Fish Physiol Biochem 40, 1393–1398 (2014). https://doi.org/10.1007/s10695-014-9933-8
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DOI: https://doi.org/10.1007/s10695-014-9933-8