Summary
The presence of hydrolytic enzymes in and associated with the sperm head has long argued for their functioning in fertilization. Several observations led investigators to propose that the acrosomal trypsin-like enzyme, acrosin in mammals, functioned in fertilization in aiding the sperm to penetrate the zona pellucida. While many have raised significant objections to this role, the action of acrosin on its presumed physiological substrate has not been characterized in a biochemical fashion. The intent of this study was to examine the effect of sperm proteases on the innermost egg envelopes in a parallel study, with the pig, Sous scrofa and the South African clawed frog, Xenopus laevis. With the pig, a great deal of information exists concerning the boar enzyme, acrosin, but little is known about the chemical structure of the zona pellucida. The opposite situation exists in X. laevis where the vitelline envelope is well characterized chemically, but little is known about the putative sperm lysins.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
REFERENCES
Ames, G.F.L. and Nikaido, K. 1976. Two dimensional gel electrophoresis of membrane proteins. Biochem. 15: 616–623.
Austin, C.R. and Bishop, M.W.H. 1958. Role of the rodent acrosome and perforatorium in fertilization. Proc. R. Soc. London Ser. B. 149: 241–248.
Bedford, J.M. 1974. Mechanisms involved in penetration of spermatozoa through the vestments of the mammalian egg, in: Physiology and Genetics of Reproduction, Part B ( E.M. Coutinho and F. Fuchs, eds.), Plenum Press, New York, pp. 55–68.
Bedford, J.M. and Cross, N.L. 1978. Normal penetration of rabbit spermatozoa through a trypsin- and acrosin-resistant zona pellucida. J. Reprod. Fert. 54: 385–392.
Brown, C.R. 1983. Purification of mouse sperm acrosin, its activation from proacrosin and effect on homologous egg investments. J. Reprod. Fert. 69: 289–295.
Brown, C.R. and Harrison, R.A.P. 1978. The activation of proacrosin in spermatozoa from ram, bull, boar. Biochem. Biophys. Acta 526: 202–217.
Chase, T. and Shaw, E. 1970. Titration of trypsin, phasmin, and thrombin with p-nitrophenyl-p -quanidinobenzoate HC1. Methods Enzyme. 19: 20–27.
Cleveland, D.W., Fisher, S.G., Kirschner, M.W., and Laemmli, U.K. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252: 1102–1106.
Dunbar, B.S., Wardrip, N.J., and Hedrick, J.L. 1980. Isolation, physicochemical properties and macromolecular composition of zona pellucida from porcine oocytes. Biochem. 19: 356–365.
Dudkiewicz, A.G. and Garrison, G.A. 1982. Substrate preference of boar acrosin in zona pellucida lysis. J. Cell Biol. 95: 165a.
Frazer, L.R. 1982. p-Aminobenzamidine, and acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction. J. Reprod. Fert. 65: 185–194.
Gould, K.G. 1973. Application of in vitro fertilization. Fed. Proc. 32: 2069–2074.
Green, D.P.L. and Purves, R.D. 1984. Mechanical hypothesis of sperm penetration. Biophys. J. 45: 659–662.
Greenberg, L.J. 1962. Fluorometric measurement of alkaline phosphatase and aminopeptidase activities in the order of l0′ mole. Biochem. Biophys. Res. Comm. 9: 430–435.
Hartmann, J.F. and Hutchinson, C.F. 1974. Nature of the prepenetration contact interactions between gametes in vitro. J. Reprod. Fert. 36: 49–57.
Hartree, E.F. 1977. Spermatozoa, eggs and proteinases. Biochem. Soc. Trans. 5: 375–394.
Hedrick, J.L. and Wardrip, N.J. 1981. Microheterogeneity in the glycoproteins of the zona pellucida is due to the carbohydrate moeity. J. Cell Biol. 91: 177a.
Hedrick, J.L. and Wardrip, N.J. 1982. Topographical Radiolabeling of zona pellucida glycoproteins. J. Cell Biol. 95: 162a.
Hibbard, J. 1928. Contribution a l’étude de l’oogenèse de la fécondation, et de l’histogenèse chez Piscoglossus pictus. Otth. Arch. Biol. 38: 251–326.
Howiett, G.J., Yeh, E., and Schachman, H.K. 1978. Protein-ligand binding studies with a table-top, air-driven high-speed centrifuge. Arch. Biochem. Biophys. 190: 809–819.
Huneau, D., Harrison, R.A.P., and Flechon, J.E. 1984. Ultrastructural localization of proacrosin and acrosin in ram spermatozoa. Gamete Res. 9: 425–440.
Karp, D.R., Atkinson, J.P., and Shreffer, D.C. 1982. Genetic variation in glycosylation of the fourth component of murine complement. Association with hemolytic activity. J. Biol. Chem. 257: 7330–7335.
Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of bacteriophage T4. Nature 227: 680–685.
Meizel, S. 1978. The mammalian sperm acrosome reaction: A biochemical approach, in: Development in Mammals, Volume 3 ( M.H. Johnson, ed.), North-Holland, Amsterdam, pp 1–62.
Meizel, S. and Mukerji, S.K. 1976. Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa. Biol. Reprod. 14: 444–450.
McLean, D. and Rowlands, I.W. 1942. Role of hyaluronidase in fertilization. Nature 150: 627–628.
Muller-Esterl, W. and Fritz, H. 1980. Interactions of boar acrosin with detergents. Hoppe-Seyler’s Z. Physiol. Chem. 361: 1673–1682.
Muller-Esterl, W., Kupfer, S., and Fritz, H. 1980. Purification and properties of boar acrosin. Hoppe-Seyler’s Z. Physiol. Chem. 361: 1811–1821.
Muller-Esterl, W., Wendt, V., Leidl, W., Dann, O., Shaw, E, Wagner, G., and Fritz, H. 1983. Intra-acrosomal inhibition of boar acrosin by synthetic proteinase inhibitors. J. Repro. Fert. 67: 13–18.
O’Farrell, P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007–4021.
Peterson, G.L. 1977. A simplification of the protein assay method of Lowry et al. whch is more generally applicable. Anal. Biochem. 83: 346–356.
Salacinski, P.R.P., McLean, L., Sykes, J.E.G., Clement-Jones, V.V., and Lowry, P.J. 1981. lodination of proteins, glycoproteins and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3a, 6a-diphenyl glycouril (Iodogen). Anal. Biochem. 117: 136–146.
Saling, P.M. 1981. Involvement of trypsin-like activity in binding of mouse spermatozoa to zonae pellucidae. Proc. Natl. Acad. Sci. USA. 78: 6231–6235.
Schill, W.B., Feifel, M., Fritz, H., and Hammerstein, J. 1981. Inhibitors of acrosomal proteinase as antifertility agents. A problem of acrosomal membrane permeability. Int. J. Androl. 4: 25–38.
Segel, I.H. 1975. Enzyme kinetics. Behavior and analysis of rapid equilibrium and steady state enzyme systems. Wiley-Interscience, John Wiley and Sons, New York.
Stambaugh, R. and Buckley, J. 1968. Zona pellucida dissolution enzymes of the rabbit sperm head. Science 161: 585–586.
Stambaugh, R., Brackett, B.G., and Mastroianni, L. 1969. Inhibition of in vitro fertilization of rabbit ova by trypsin inhibitors. Biol. Reprod. 1: 223–227.
Srivastava, P.N., Adams, C.E., and Hartree, E.F. 1965. Enzymatic action of acrosomal preparations on the rabbit ovum in vitro. J. Reprod. Fertil. 10: 61–67.
Tyler, A. 1939. Extraction of an egg membrane lysin from sperm of the giant keyhole limpet (Megathura crenulata). Proc. Natl. Acad. Sei. USA, 25: 317–323.
Urch, U.A., Nishihara, T., and Hedrick, J.L. 1979. The use of radioiodination protein substrates for the assay of trypsin and the hatching enzyme from the amphibian Xenopus laevis. Anal. Biochem. 100: 325–356.
Waldschmidt, M., Hoffman, B., and Karg, H. 1966. Unterschungen über die tryptische enzymaktivitat in geschlectssekreten von bullen. Zychthygiene 1: 15.
Wardrip, N.J. and Hedrick, J.L. 1980. The macromolecular composition of the porcine zona pellucida. Fed. Proc. 39: 2081.
Wardrip, N.J., Goldhawk, D.E., and Hedrick, J.L. 1984. Deglycosylation studies of pig zona pellucida. Third International Congress on Cell Biology. S. Seno and Y. Okada, eds., Academic Press, p. 401.
Wintrebert, P. 1933. La fonction enzymatique de l’acrosome Spermien du Discoglosse. C.R. Soc. Biol. 112: 1636–1640.
Wolf, D.P., Nishihara, T., West, D.M., Wyrick, R.E., and Hedrick, J.L. 1976. Isolation, physicochemical properties, and the macromolecular composition of the vitelline and fertilization envelopes from Xenopus laevis eggs. Biochem. 15: 3671–3678.
Yamane, J. 1930. The proteolytic action of mammalian spermatozoa and its bearing upon the second maturation division of ova. Cytologia 1: 394–403.
Yamane, J. 1935. Kausal-analytishe Studien über die befruchtung des kaninchenesis II. Die isoliering der auf das eizytoplasma auflosend wirkenden substanzen aus den spermatozoen. Cytologia 6: 474–483.
Yanagimachi, R. 1981. Mechanisms of fertilization in mammals, in: Fertilization and Embryonic Development in vitro (Biggers, J.D. and L. Mastrioanni, eds), Plenum Press, New York, pp 81–182.
Zaneveld, L.J.D., Robertson, R.T., Kessler, M., Srivastava, P.N., and Williams, W.L. 1970. Inhibition of fertilization in vivo by mammalian trypsin inhibitors. Fedn. Proc. 29: 644.
Zaneveld, L.J.D., Robertson, R.T., Kessler, M., and Williams, W.L. 1971. Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors. J. Reprod. Fert. 25: 387–392.
Zimmerman, M., Ashe, B., Yurewicz E.C., and Patel, G. 1977. sensitive assays for trypsin, elastase and chymotrypsin using new fluorogenic substrate. Anal. Biochem. 78: 47–51.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1986 Plenum Press, New York
About this chapter
Cite this chapter
Urch, U.A. (1986). The Action of Acrosin on the Zona Pellucida. In: Hedrick, J.L. (eds) The Molecular and Cellular Biology of Fertilization. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2255-9_8
Download citation
DOI: https://doi.org/10.1007/978-1-4613-2255-9_8
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-9320-0
Online ISBN: 978-1-4613-2255-9
eBook Packages: Springer Book Archive