Proteinase Inhibitors and Proteinases of Human Semen

  • L. J. D. Zaneveld
  • G. F. B. Schumacher
  • P. F. Tauber
  • D. Propping
Part of the Bayer-Symposium book series (BAYER-SYMP, volume 5)

Abstract

During the First International Research Conference on Proteinase Inhibitors, a survey was presented concerning the proteinases of spermatozoa and seminal plasma as was known until that time [1, 2]. In summary, a proteinase from rabbit spermatozoa was purified and characterized, and shown to differ from other known pro-teolytic enzymes. It was given the name “Acrosin” (approved by the Commission on Enzyme Nomenclature), alternately being called “Acrosomal Proteinase” by some authors. Acrosin was thought to be associated with the acrosome, a sac-like structure that caps the anterior portion of the sperm head. This has recently been confirmed by various authors [3, 4, 5]. Acrosin removes the zona pellucida of the rabbit ovum and is apparently used by the spermatozoon to penetrate this layer during the fertilization process. In certain species, such as the rabbit, boar and stallion [1, 6], acrosin activity is high in extracts from epididymal spermatozoa and low in extracts from ejaculated spermatozoa. This is due to the addition of one or more proteinase inhibitors from seminal plasma to the sperm during ejaculation. In various other species, such as the bull and rodents, epididymal spermatozoa possess high levels of inhibitor already, depressing the activity of acrosin. The epididymal inhibitor probably originates from the rete testis [7]. Its concentration in boar epididymal fluid is much lower than in boar seminal plasma, explaining the difference in acrosin activity of epididymal and ejaculated sperm in this species. The ram does not show these differences [6] and indeed the epididymal plasma and seminal plasma possess approximately the same concentration of inhibitor [7]. The molecular weight of the rete testis inhibitor was estimated as 6500 [7], identical to the inhibitor in seminal plasma [1]. Whether these inhibitors are the same remains to be established, however.

Keywords

Trypsin Fructose Gelatin Fibrinogen Amylase 

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References

  1. 1.
    Zaneveld. L.J.D., Polakoski. K.L., Robertson, R.T., Williams, W.L.: In: Fritz, H., Tschesche. H. (Eds.): Proceedings of the International Research Conference on Protei-nase Inhibitors, p.236. Berlin-New York: Walter de Gruyter 1971.Google Scholar
  2. 2.
    Schumacher, G.F.B., Swartwout. J.R.. Zlspan, F.P.: In: FRITZ, H., TSCHESCHE. H. (Eds.): Proceedings of the International Research Conference on Proteinase Inhibitors, p. 247. Berlin-New York: Walter de Gruyter 1971.Google Scholar
  3. 3.
    Gaddlm-Rosse. P.. Blandau. R.J.: Amer. J. Anat. 134. 133 (1972).CrossRefGoogle Scholar
  4. 4.
    Pew. A.. Glfdhill. B.L., Darzynkiewicz. Z.: J. Histochem. Cytochem. 20. 499 (1972).CrossRefGoogle Scholar
  5. 5.
    Yanagimachl, R., Teichman, R.J.: Biol. Reprod. 6, 87 (1972).Google Scholar
  6. 6.
    Zaneveld, L.J.D., Polakoski, K.L., Williams, W.L.: Biol. Reprod. 9, 219 (1973).PubMedGoogle Scholar
  7. 7.
    Suominen, J., Setchel, B.P-: J. Reprod. Fertil. 30, 235 (1973).Google Scholar
  8. 8.
    Srivastava, P.N., Zaneveld, L.J.D, Williams, W.L.: B.B.R.C. 39, 575 (1970).Google Scholar
  9. 9.
    Zaneveld, L. J. D., Dragoje, B. M, Schumacher, G. F. B.: Science 177, 702 (1972).PubMedCrossRefGoogle Scholar
  10. 10.
    Uhlenbruck, G., Sprenger, I., Schumacher, G.F.B., Zaneveld, L.J.D.: Naturwissenschaften 3, 124 (1972).CrossRefGoogle Scholar
  11. 11.
    Schumacher, G. F. B., Zaneveld, L.J.D.: This volume, p. 178.Google Scholar
  12. 12.
    Fritz, H., Förg-Brey, B., Fink, E., Meier, M, Schiessler, H., Schirren, C: Z. physiol. Chem. 353, 1943 (1972).CrossRefGoogle Scholar
  13. 13.
    Fritz, H., Förg-Brey, B., Meier, M., Arnhold, M., Tschesche, H.: Z. physiol. Chem. 353, 1950 (1972).CrossRefGoogle Scholar
  14. 14.
    Fritz, H., Heimburger, N., Meier, M., Arnhold, M., Zaneveld, L.J.D., Schuma-Cher, G.F.B.: Z. physiol. Chem. 353, 1953 (1972).CrossRefGoogle Scholar
  15. 15.
    Zaneveld, L.J.D., Schumacher, G.F.B., Travis, J.: Fert. Ster.24, 479 (1973).Google Scholar
  16. 16.
    Fink, E., Jaumann, E., Fritz, H., Ingrisch, H., Werle, E.: Z. physiol. Chem. 352, 1591 (1971).CrossRefGoogle Scholar
  17. 17.
    Suominen, J.J., Niemi, M.: J. Reprod. Fertil. 29, 163 (1972).PubMedCrossRefGoogle Scholar
  18. 18.
    Zaneveld, L.J.D., Schumacher, G.F.B., Fritz, H., Fink, E., Jaumann, E.: J. Reprod. Fertil. 32, 525 (1973).CrossRefGoogle Scholar
  19. 19.
    Schiessler, H.: Personal communications.Google Scholar
  20. 20.
    Tauber, P. F., Propping, D., Zaneveld, L.J.D., Schumacher, G.F.B.: Biol. Reprod. 9, 62(1973).Google Scholar
  21. 21.
    Bunge, R.G.: Fert. Steril. 21, 639 (1970).Google Scholar
  22. 22.
    Hirschhauser, C., Eliasson, R.: Life Sci. 11, 149 (1972).CrossRefGoogle Scholar

Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • L. J. D. Zaneveld
    • 1
  • G. F. B. Schumacher
    • 1
  • P. F. Tauber
    • 1
  • D. Propping
    • 1
  1. 1.Laboratory for Reproductive Biochemistry and Immunology Department of Obstetrics and GynecologyUniversity of ChicagoChicagoUSA

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