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The Action of Acrosin on the Zona Pellucida

  • Chapter
The Molecular and Cellular Biology of Fertilization

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.

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REFERENCES

  1. Ames, G.F.L. and Nikaido, K. 1976. Two dimensional gel electrophoresis of membrane proteins. Biochem. 15: 616–623.

    Article  Google Scholar 

  2. 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.

    Article  Google Scholar 

  3. 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.

    Google Scholar 

  4. 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.

    Article  Google Scholar 

  5. 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.

    Article  Google Scholar 

  6. 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.

    Google Scholar 

  7. Chase, T. and Shaw, E. 1970. Titration of trypsin, phasmin, and thrombin with p-nitrophenyl-p -quanidinobenzoate HC1. Methods Enzyme. 19: 20–27.

    Article  Google Scholar 

  8. 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.

    Google Scholar 

  9. 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.

    Article  Google Scholar 

  10. Dudkiewicz, A.G. and Garrison, G.A. 1982. Substrate preference of boar acrosin in zona pellucida lysis. J. Cell Biol. 95: 165a.

    Google Scholar 

  11. 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.

    Google Scholar 

  12. Gould, K.G. 1973. Application of in vitro fertilization. Fed. Proc. 32: 2069–2074.

    Google Scholar 

  13. Green, D.P.L. and Purves, R.D. 1984. Mechanical hypothesis of sperm penetration. Biophys. J. 45: 659–662.

    Article  ADS  Google Scholar 

  14. 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.

    Article  Google Scholar 

  15. Hartmann, J.F. and Hutchinson, C.F. 1974. Nature of the prepenetration contact interactions between gametes in vitro. J. Reprod. Fert. 36: 49–57.

    Article  Google Scholar 

  16. Hartree, E.F. 1977. Spermatozoa, eggs and proteinases. Biochem. Soc. Trans. 5: 375–394.

    Google Scholar 

  17. 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.

    Google Scholar 

  18. Hedrick, J.L. and Wardrip, N.J. 1982. Topographical Radiolabeling of zona pellucida glycoproteins. J. Cell Biol. 95: 162a.

    Google Scholar 

  19. 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.

    Google Scholar 

  20. 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.

    Article  Google Scholar 

  21. 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.

    Article  Google Scholar 

  22. 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.

    Google Scholar 

  23. Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of bacteriophage T4. Nature 227: 680–685.

    Article  ADS  Google Scholar 

  24. 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.

    Google Scholar 

  25. Meizel, S. and Mukerji, S.K. 1976. Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa. Biol. Reprod. 14: 444–450.

    Article  Google Scholar 

  26. McLean, D. and Rowlands, I.W. 1942. Role of hyaluronidase in fertilization. Nature 150: 627–628.

    Article  ADS  Google Scholar 

  27. Muller-Esterl, W. and Fritz, H. 1980. Interactions of boar acrosin with detergents. Hoppe-Seyler’s Z. Physiol. Chem. 361: 1673–1682.

    Article  Google Scholar 

  28. Muller-Esterl, W., Kupfer, S., and Fritz, H. 1980. Purification and properties of boar acrosin. Hoppe-Seyler’s Z. Physiol. Chem. 361: 1811–1821.

    Article  Google Scholar 

  29. 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.

    Article  Google Scholar 

  30. O’Farrell, P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007–4021.

    Google Scholar 

  31. 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.

    Article  Google Scholar 

  32. 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.

    Google Scholar 

  33. 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.

    Article  ADS  Google Scholar 

  34. 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.

    Article  Google Scholar 

  35. 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.

    Google Scholar 

  36. Stambaugh, R. and Buckley, J. 1968. Zona pellucida dissolution enzymes of the rabbit sperm head. Science 161: 585–586.

    Article  ADS  Google Scholar 

  37. 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.

    Article  Google Scholar 

  38. 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.

    Article  Google Scholar 

  39. 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.

    Article  ADS  Google Scholar 

  40. 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.

    Article  Google Scholar 

  41. Waldschmidt, M., Hoffman, B., and Karg, H. 1966. Unterschungen über die tryptische enzymaktivitat in geschlectssekreten von bullen. Zychthygiene 1: 15.

    Article  Google Scholar 

  42. Wardrip, N.J. and Hedrick, J.L. 1980. The macromolecular composition of the porcine zona pellucida. Fed. Proc. 39: 2081.

    Google Scholar 

  43. 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.

    Google Scholar 

  44. Wintrebert, P. 1933. La fonction enzymatique de l’acrosome Spermien du Discoglosse. C.R. Soc. Biol. 112: 1636–1640.

    Google Scholar 

  45. 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.

    Article  Google Scholar 

  46. Yamane, J. 1930. The proteolytic action of mammalian spermatozoa and its bearing upon the second maturation division of ova. Cytologia 1: 394–403.

    Google Scholar 

  47. 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.

    Google Scholar 

  48. 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.

    Google Scholar 

  49. 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.

    Google Scholar 

  50. 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.

    Article  Google Scholar 

  51. 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.

    Google Scholar 

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  1. Department of Biochemistry and Biophysics, University of California, Davis, CA, 95616, USA

    Umbert A. Urch

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  1. University of California, Davis, Davis, California, USA

    Jerry L. Hedrick

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© 1986 Plenum Press, New York

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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

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  • 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

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