Transglutaminase-Catalyzed Crosslinking of an Immunosuppressive and Anti-Inflammatory Protein Secreted from the Rat Seminal Vesicles

  • R. Porta
  • C. Esposito
  • P. Persico
  • G. Peluso
  • S. Metafora
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)


It is well known that the mammalian reproduction system is potentially hazardous because of male gamete immunogenicity. In fact, it has been demonstrated by a variety of immunological techniques that the epididymal sperm cells possess non-self specific, highly immunogenic autoantigens and alloantigens on their surface. Therefore, sperm antigens should be able to elicit a dangerous immunological response in the female genital tract where the sperm cells should be rejected. However, even though spermatozoa possess components which are antigenically foreign to the female mammal, the deposition of sperm cells at natural mating does not cause sterilizing anti-sperm immunity. The surface antigenic characteristics of the epididymal sperm cells change following their mixing in the ejaculate with the secretions of the male accessory sexual glands; in fact, the male gametes lose their immunological reactivity in the seminal plasma, adapting themselves to avoid rejecton by the immunocompetent elements normally occurring in the female genital tract.2


Sperm Cell Seminal Plasma Hank Balance Salt Solution Male Gamete Female Genital Tract 
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  1. 1.
    P. J. Hogart, “Immunological Aspects of Mammalian Reproduction,” Blackie, Glasgow and London,.(1982).CrossRefGoogle Scholar
  2. 2.
    K. James and T. B. Hargreave, Immunosuppression by seminal plasma and its possible clinical significance, Immunol. Today 5:357 (1984).CrossRefGoogle Scholar
  3. 3.
    S. S. Witkin, R. J. T. Hancock, R. D. Allen, T. K. Roberts, A. H. Jacobson, D. J. Anderson, Immunosuppression by seminal plasma in vitro — an artefact?, Immunol. Today 7:356 (1986).CrossRefGoogle Scholar
  4. 4.
    D. G. Mukherjee, A. K. Agrawal, R. Manjunath and A. B. Mukherjee, Suppression of epididymal sperm antigenicity in the rabbit by uteroglobin and transglutaminase in vitro, Science 219:989 (1983).PubMedCrossRefGoogle Scholar
  5. 5.
    R. Manjunath, S. I. Chung and A. B. Mukherjee, Crosslinking of uteroglobin by transglutaminase, Biochem. Biophys. Res. Commun. 121:400 (1984).CrossRefGoogle Scholar
  6. 6.
    S. Metafora, F. Facchiano, A. Facchiano, C. Esposito, G. Peluso and R. Porta, Homology between rabbit uteroglobin and the rat seminal vesicle sperm-binding protein: prediction of structural features of glutamine substrates for transglutaminase, J. Prot. Chem. 6:353 (1987).CrossRefGoogle Scholar
  7. 7.
    Y. E. Pan and S. S. Li, Structure of secretory protein IV from rat seminal vesicles, Int. J. Pept. Prot. Res. 20:177 (1978).CrossRefGoogle Scholar
  8. 8.
    S. J. Higgins and J. M. Burchell, Effects of testosterone on messenger ribonucleic acid and protein synthesis in rat seminal vesicle, Biochem. J. 174:543 (1978).PubMedGoogle Scholar
  9. 9.
    M. C. Ostrowski, M. K. Kistler and W. S. Kistler, Purification and cell-free synthesis of a major protein from rat seminal vesicle secretion. A potential marker for androgen action, J. Biol. Chem. 254:383 (1979).PubMedGoogle Scholar
  10. 10.
    S. W. Levin, J. D. Butler, U. K. Schumacher, P. D. Wightman and A. B. Mukherjee, Uteroglobin inhibits phospholipase A2 activity, Life Sci. 38:1813 (1986).PubMedCrossRefGoogle Scholar
  11. 11.
    H. G. Williams-Ashman, Transglutaminases and the clotting of mammalian seminal fluids, Mol. Cell. Biochem. 58:51 (1984).PubMedCrossRefGoogle Scholar
  12. 12.
    G. Paonessa, S. Metafora, G. Tajana, P. Abrescia, A. De Santis, V. Gentile and R. Porta, Transglutaminase-mediated modifications of the rat sperm surface in vitro, Science 226:852 (1984).PubMedCrossRefGoogle Scholar
  13. 13.
    P. Abrescia, G. Lombardi, M. De Rosa, L. Quagliozzi, J. Guardiola and S. Metafora, Identification and preliminary characterization of a sperm-binding protein in normal human semen, J. Reprod. Fertil. 73:71 (1985).PubMedCrossRefGoogle Scholar
  14. 14.
    R. Porta, C. Esposito, A. De Santis, A. Fusco, M. Iannone and S. Metafora, Sperm maturation in human semen: role of transglutaminase-mediated reactions, Biol. Reprod. 35:965 (1986).PubMedCrossRefGoogle Scholar
  15. 15.
    J. M. Connellan, S. I. Chung, N. K. Whetzel, L. M. Bradley and J. E. Folk, Structural properties of guinea pig liver transglutaminases, J. Biol. Chem. 246:1093 (1971).PubMedGoogle Scholar
  16. 16.
    U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227:680 (1970).PubMedCrossRefGoogle Scholar
  17. 17.
    W. M. Bonner and R. A. Laskey, A film detection method for tritium-labeled proteins and nucleic acids in Polyacrylamide gels, Eur. J. Biochem. 46:83 (1974).PubMedCrossRefGoogle Scholar
  18. 18.
    R. Carnuccio, M. Di Rosa, R. Y. Flower, C. S. J. Langham, L. Parente, P. Persico, N. C. Russell-Smith and D. Stone, Glucocorticoids induce the formation and release of anti-inflammatory and anti-phospholipase proteins into the peritoneal cavity of the rat, Br. J. Pharmac. 76:185 (1982).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • R. Porta
    • 1
  • C. Esposito
    • 1
  • P. Persico
    • 2
  • G. Peluso
    • 3
  • S. Metafora
    • 3
  1. 1.Institute of Chemistry and Biological Chemistry, 1st Medical SchoolUniversity of NaplesNaplesItaly
  2. 2.Department of Experimental PharmacologyUniversity of NaplesNaplesItaly
  3. 3.Institute of Protein Biochemistry and EnzymologyCNRArco Felice, NaplesItaly

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