Identification of trypsin-like activity in sturgeon spermatozoa
Andrzej Ciereszko
School of Natural Resources, The Ohio State University, Columbus, Ohio 43210
Centre for Agrotechnology and Veterinary Sciences, Polish Academy of Sciences, 10-718 Olsztyn, Poland
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Konrad Dabrowski
School of Natural Resources, The Ohio State University, Columbus, Ohio 43210
The Ohio State University, School of Natural Resources, 210 Kottman Hall, 2021 Coffey Rd., Columbus, OH 43210===Search for more papers by this authorFeng Lin
School of Natural Resources, The Ohio State University, Columbus, Ohio 43210
Search for more papers by this authorSerge I. Doroshov
Department of Animal Sciences, University of California, Davis, California 95616
Search for more papers by this authorAndrzej Ciereszko
School of Natural Resources, The Ohio State University, Columbus, Ohio 43210
Centre for Agrotechnology and Veterinary Sciences, Polish Academy of Sciences, 10-718 Olsztyn, Poland
Search for more papers by this authorCorresponding Author
Konrad Dabrowski
School of Natural Resources, The Ohio State University, Columbus, Ohio 43210
The Ohio State University, School of Natural Resources, 210 Kottman Hall, 2021 Coffey Rd., Columbus, OH 43210===Search for more papers by this authorFeng Lin
School of Natural Resources, The Ohio State University, Columbus, Ohio 43210
Search for more papers by this authorSerge I. Doroshov
Department of Animal Sciences, University of California, Davis, California 95616
Search for more papers by this authorAbstract
We documented amidase activity in lake sturgeon (Acipenser fulvescens) and white sturgeon (Acipenser transmontanus) spermatozoa. This activity was inhibited by benzamidine and soybean trypsin inhibitor (SBTI), and N-α-p-tosyl-L-lysine chloromethyl ketone-HCl (TLCK), but not by N-tosyl-L-phenylalanine chloromethyl keton (TPCK), indicating the presence of trypsin-like activity in sturgeon spermatozoa. Higher activity occurred at pH 8.5 and 9.0 than at 8.0. No effect of 10 mM KCl and 100 mM NaCl on trypsin-like activity was found. Calcium ions inhibited the activity at 10 and 50 mM. Similar activities were documented in neat semen and washed sperm suspension. Presence of trypsin-like activity corresponds to the presence of acrosomes and acrosome reaction in spermatozoa of these fishes. © 1994 Wiley-Liss, Inc.
Literature Cited
- Arboleda, C. E., and G. L. Gerton (1987) Studies of three major proteases associated with guinea pig sperm acrosomes. J. Exp. Zool., 244: 277–287.
- Bacceti, B., A. G., Burrini, G. Collodel, P. Piomboni, T. Renieri, and C. Sensini (1989) Localization of acrosomal enzymes in Arthropoda, Echinodermata and Vertebrata. J. Submicrosc. Cytol. Pathol., 21: 385–389.
-
Calvete, J. J.,
L., Sanz, and
E. Topfer-Petersen
(1992)
Carbohydrate-binding proteins involved in gamete interaction in the pig. In:
Spermatogenesis-Fertilization-Contraception.
E. Nieschlag and
U.-F. Habenicht, eds.
Springer-Verlag,
Berlin, Heidelberg, New York, London, Paris, Tokyo, Hong Kong, Barcelona, Budapest,
pp. 395–417.
10.1007/978-3-662-02815-5_17 Google Scholar
- Cherr, G. N., and W. H. Clark, Jr. (1984a) An acrosome reaction in sperm from the white sturgeon Acipenser transmonatus. J. Exp. Zool., 232: 129–139.
- Cherr, G. N., and W. H. Clark, Jr. (1984b) An egg envelope component induces the acrosome reaction in sturgeon sperm. J. Exp. Zool., 234: 75–85.
-
Cherr, G. N., and
W. H. Clark, Jr.
(1986)
Induction of the acrosomal reaction in sperm from the white sturgeon, Acipenser transmontanus. In:
Advances in Experimental Medicine and Biology, the Molecular and Cellular Biology of Fertilization.
J. L. Hedrick, ed.
Plenum Press,
New York and London,
Vol. 209,
pp. 235–249.
10.1007/978-1-4613-2255-9_14 Google Scholar
- Ciereszko, A., and K. Dabrowski (1993a) Estimation of sperm concentration of rainbow trout, whitefish and yellow perch using a spectrophotometric technique. Aquaculture, 109: 367–373.
- Ciereszko, A., and K. Dabrowski (1993b) Some biochemical characteristics of lake sturgeon (Acipenser fulvescens) milt in comparison with rainbow trout (Oncorhynchus mykiss) and yellow perch (Perca flavescens). 2nd International Symposium on the Sturgeon, Moscow Kostroma, Russia, September 6–11, 1993.
- Dabrowski, K., and A. Ciereszko (in press) Proteinase inhibitor(s) in seminal plasma of teleost fish. J. Fish Biol.
- Folz, D. J., D. G., Czesklaba, and T. F. Thuemler (1983) Artificial spawning of lake sturgeon in Wisconsin. Prog. Fish-Cult., 45: 231–233.
- Froman, D. P. (1990) Chicken acrosin: Extraction and purification. Poultry Sci., 69: 812–817.
- Gallis, J. L., E., Fedrigo, P. Jatteau, E. Bonpunt, and R. Billard (1991) Siberian sturgeon Acipenser baeri spermatozoa: Effects of dilution, pH, osmotic pressure, sodium and potassium ions on motility. In: Acipenser, P. Williot, ed. CEMAGREF Publ., Bordeaux, France, pp. 143–151.
- Ginzburg, A. S. (1968) Fertilization in fishes and the problem of polyspermy. In: Israel Program for Scientific Translations, Ltd. (1972). T. A. Detlaf, ed., Jerusalem, pp. 1–175.
-
Harrison, R. A. P.
(1983)
The acrosome, its hydrolases, and egg penetration. In:
The Sperm Cell: Fertilizing Power, Surface Properties, Motility, Nucleus and Acrosome, Evolutionary Aspects.
J. Andre, ed.
Nijho,
The Hague,
pp. 259–273.
10.1007/978-94-009-7675-7_48 Google Scholar
- Jamieson, B. G. M. (1991) Fish evolution and systematics: Evidence from spermatozoa. Cambridge University Press, Cambridge, New York, Port Chester, Melbourne, Sydney.
- Jones, R. (1990) Identification and functions of mammalian—egg recognition molecules during fertilization. J. Reprod. Fertil. Suppl., 42: 89–105.
- Kennedy, W. P., J. M. Kaminski, H. H. Van der Ven, R. S. Jeyndran, D. S. Reid, J. Blackwell, P. Bielfeld, and L. J. D. Zaneveld (1989) A simple clinical assay to evaluate the acrosin activity of human spermatozoa. J. Androl., 10: 221–231.
- Lahsteiner, F., T., Weisman, and R. A. Patzner (1992) Fine structural changes in spermatozoa of the grayling, Thymallus thymallus (Pisces: Teleostei), during routine cryopreservation. Aquaculture, 103: 73–84.
- Matsumara, K., and K. Aketa (1991) Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. Mol. Reprod. Dev., 29: 189–199.
- Miller, B. J., C. N., Graves, and J. R. Lodge (1988) Effect of in vitro storage of bovine spermatozoa on acrosomal integrity, proteolytic activity, binding, and initiation of penetration of oocytes. Gamete Res., 20: 53–65.
- Sawada, H., H., Yokosawa, and S. Ishii (1984) Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi. J. Biol. Chem., 259: 2900–2904.
- Siegel, M. S., and K. L. Polakoski (1985) Evaluation of the human proacrosin–acrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biol. Reprod., 32: 713–720.
- Siegel, M. S., D. S., Bechtold, J. L. Willand, and K. L. Polakoski (1987) Partial purification and characterization of human sperminogen. Biol. Reprod., 36: 1063–1068.
- Sousa, M., P., Moradas-Ferraira, and C. Azevedo (1992) Presence of a trypsin-like protease in starfish sperm acrosome. J. Exp. Zool., 261: 349–354.