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Transglutaminases and the clotting of mammalian seminal fluids

  • Transglutaminase
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Summary

Rapid coagulation of seminal fluid in rats, guinea pigs, and several other mammalian species including certain non-human primates is responsible for the post-coital formation of copulatory plugs in the vagina. The clotting of rodent seminal plasma results from coagulation of certain proteins derived from the seminal vesicles by enzymes secreted mainly by the coagulating (anterior prostate) gland. Several lines of evidence indicate that the clotting enzymes of coagulating gland secretions are trans glutaminases, and that the extreme insolubility of the seminal clot in rodents is due to transglutaminase-catalyzed formation of ε(γ-glutamyl)ly-sine cross-links between polypeptide chains. Various features of the apparently unique forms of transglutaminases produced by rat coagulating gland and the actions of these enzymes on vesicular secretory and other proteins are discussed. The aliphatic polyamines spermidine and spermine are incorporated covalently into the proteins of the clot as the corresponding N-mono-ε-(γ-glutamyl)- and N,N-bis(γ-glutamyl)-adducts during the enzymatic coagulation process. At the greater than millimolar concentrations at which cross-spermidine and spermine are present in normal rat seminal plasma, these polyamines attenuate the formation of hard clots in reconstituted rat semen coagulation systems, seemingly by competing with lysyl residues in vesicular secretion proteins as transglutaminase amine donor substrates, and thus preventing formation of ε-(γ-glutamyl)lysine cross-bridges. It is proposed that in those species such as the rat and man in which seminal plasma contains large amounts of spermidine and(or) spermine of prostatic origin, the seminal polyamines may serve to stop blockage of the urethra by preventing too explosive a rate of seminal clot formation during the ejaculatory process.

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References

  1. Lorand, L., 1972. Ann. N.Y. Acad. Sci. 202: 6–30.

    Google Scholar 

  2. Lorand, L. and Stenberg, P., 1976. In: CRC Handbook on Biochemistry and Molecular Bilogy, Vol. 11 Proteins (Fasman, G. D., ed.), 3rd ed. pp. 669–685, Chemical Rubber Publ. Co., Cleveland.

  3. Curtis, C. G. and Lorand, L., 1977. In: Haemostasis: Biochemistry, Physiology and Pathology (Ogston, D. and Bennett, B., eds.), Chapter 8, pp. 186–201, Wiley, Chichester.

  4. Folk, J. E. and Finlayson, J. S., 1977. Adv. Protein Chem. 31: 1–133.

    Google Scholar 

  5. Rice, R. H. and Green, H., 1977. Cell 11: 417–422.

    Google Scholar 

  6. Goldsmith, L. A. and Martin, C. M., 1975. J. Invest. Dermatol. 64: 316–321.

    Google Scholar 

  7. Notides, A. C. and Williams-Ashman, H. G., 1967. Proc. Natl. Acad. Sci. U.S.A. 58: 1991–1995.

    Google Scholar 

  8. Williams-Ashman, H. G., Notides, A. C., Pabalan, S. S. and Lorand, L., 1972. Proc. Natl. Acad. Sci. U.S.A. 69: 2322–2325.

    Google Scholar 

  9. Williams-Ashman, H. G., Beil, R. E., Wilson, J., Hawkins, M., Grayhack, J., Zunamon, A. and Winstein, N. K., 1980. Adv. Enzyme Regul. 18: 239–258.

    Google Scholar 

  10. Price, D. and Williams-Ashman, H. G., 1961. In: Sex and Internal Secretions (Young, W. C., ed.), 3rd ed, Vol. 1, Chapter 6, pp. 366–448, Williams and Wilkins, Baltimore.

  11. Mann, T., 1964. The Biochemistry of Semen and of the Male Reproductive Tract. Wiley, New York.

    Google Scholar 

  12. Mann, T. and Lutwak-Mann, C., 1981. Male Reproductive Function and Semen. Springer, New York.

    Google Scholar 

  13. Hartman, C. G., 1924. Anat. Rec. 27: 293–304.

    Google Scholar 

  14. Eadie, W. R., 1948. Anat. Rec. 102: 259–267.

    Google Scholar 

  15. Stockard, C. R. and Papanicolaou, G. N., 1919. Biol. Bull. 37:222–245.

    Google Scholar 

  16. Tauber, P. F. and Zaneveld, L. J. D., 1976. In: Human Semen and Fertility Regulation in Men (Hafez, E. S. E., ed.), Chapter 14, pp. 153–166, Mosby, St. Louis.

  17. Walker, G., 1911. Johns Hopkins Hosp. Rep. 16: 223–226.

    Google Scholar 

  18. Blandau, R. L., 1945. Am. J. Anat. 77: 253–272.

    Google Scholar 

  19. Pang, S. F., Chow, P. H. and Wong, T. M., 1979. J. Reprod. Fertil. 56: 129–132.

    Google Scholar 

  20. Zaneveld, L. J. D., Tauber, P. F., Port, C., Propping, D. and Schumacher, G. B. F., 1974. J. Reprod. Fertil. 40: 223–230.

    Google Scholar 

  21. Martan, J. and Shepherd, B. A., 1976. J. Ex. Zool. 196: 79–84.

    Google Scholar 

  22. Williams-Ashman, H. G., 1983. Current Topics in Cellular Regulation 23: 201–275.

    Google Scholar 

  23. Gotterer, G., Ginsburg, D., Schulman, T., Banks, J. and Williams-Ashman, H. G., 1955. Nature 176: 1209–1211.

    Google Scholar 

  24. Gotterer, G. and Williams-Ashman, H. G., 1957. Proc. Soc. Exp. Biol. Med. 94: 60–64.

    Google Scholar 

  25. Ballard, P. and Williams-Ashman, H. G., 1964. Invest. Urol. 2:38–46.

    Google Scholar 

  26. Veneziale, C. M. and Deering, N. G., 1976. Andrologia 8: 73–82.

    Google Scholar 

  27. Pabalan, S. S., 1975. Guinea Pig Seminal Vesicle Basic Secretory Protein. Ph. D. Thesis, Northwestern University, Evanston, Illinois.

    Google Scholar 

  28. Veneziale, C. M., 1977. Biochem. J. 166: 155–166.

    Google Scholar 

  29. Pisano, T. J., Finlayson, J. S. and Peyton, M. P., 1969. Biochemistry 8: 871–876.

    Google Scholar 

  30. Chung, S. L, 1977. In: ‘Isozymes’ (Markert, C. L., ed.), Vol. 1, pp. 259–274, Academic Press, New York.

  31. Wing, D. A., 1977. Guinea Pig Coagulating Gland Transamidase. Ph. D. Thesis, Northwestern University, Evanston, Illinois.

    Google Scholar 

  32. Tong, Y. S., 1980. Guinea Pig Prostate Gland Transamidases. Ph. D. Thesis, Northwestern University, Evanston, Illinois.

    Google Scholar 

  33. Lorand, L., Siefring, Jr., G. E., Tong, Y. S., Bruner-Lorand, J., and Gray, Jr., A. J., 1979. Anal. Biochem. 93: 453–458.

    Google Scholar 

  34. Hart, R. G., 1968. J. Reprod. Fertil. 17: 223–226.

    Google Scholar 

  35. Hart, R. G., 1970. Biol. Reprod. 3: 347–352.

    Google Scholar 

  36. Beil, R. E. and Hart, R. G., 1973. Biol. Reprod. 8: 613–617.

    Google Scholar 

  37. Ostrowski, M., Kistler, W. S. and Williams-Ashman, H. G., 1979. Biochem. Biophys. Res. Commun. 87: 171–176.

    Google Scholar 

  38. Ostrowski, M. C. and Kistler, W. S., 1980. Biochemistry 19: 2639–2645.

    Google Scholar 

  39. Ostrowski, M. C., Kistler, M. K. and Kistler, W. S., 1979. J. Biol. Chem. 254: 383–390.

    Google Scholar 

  40. Pan, Y.-C. E., Silverberg, A. G., Harris, S. E. and Li, S. S.-I., 1980. Int. J. Peptide Protein Res. 16: 143–146.

    Google Scholar 

  41. Williams-Ashman, H. G., Wilson, J., Beil, R. E., and Lorand, L., 1977. Biochem. Biophys. Res. Commun. 79: 1192–1198.

    Google Scholar 

  42. Higgins, S. J., Burchell, J. M. and Mainwaring, W.I.P., 1976. Biochem. J. 160: 43–48.

    Google Scholar 

  43. Bradshaw, B. S. and Wolfe, H. G., 1977. Biol. Reprod. 16: 292–297.

    Google Scholar 

  44. Birckbichler, P. J., Orr, G. R., Cartes, H. A. and Patterson, M. K., 1979. Biochem. Biophys Res. Commun. 78: 1–7.

    Google Scholar 

  45. Lorand, L., Rule, N. G., Ong, H. H., Furlanetto, R., Jacobson, A., Downey, J., Öner, N. and Brunes-Lorand, J., 1968. Biochemistry 7: 1214–1223.

    Google Scholar 

  46. Buxman, M. M., Lopitz, C. J. and Wuepper, K. D., 1980. J. Biol. Chem. 255: 1200–1203.

    Google Scholar 

  47. Bures, D. M., Goldsmith, L. A. and Stone, K. R., 1980. Invest. Urol. 17: 298–302.

    Google Scholar 

  48. Rhodes, J. B. and Williams-Ashman, H. G., 1964. Med. Exp. 10:281–285.

    Google Scholar 

  49. Williams-Ashman, H. G. and Lockwood, D. H., 1970. Ann. N.Y. Acad. Sci. 171: 882–894.

    Google Scholar 

  50. Folk, J. L., Park, M. H., Chung, S. I., Schrode, J., Lester, E. P. and Cooper, H. L., 1980. J. Biol. Chem. 255: 3695–3700.

    Google Scholar 

  51. Williams-Ashman, H. G., 1981. Adv. Polyamine Res. 3: 55–64.

    Google Scholar 

  52. Williams-Ashman, H. G., Jänne, J., Coppoc, G. L., Geroch, M. E. and Schenone, A., 1972. Adv. Enzyme Regul. 10: 225–245.

    Google Scholar 

  53. Williams-Ashman, H. G. and Canellakis, Z. N., 1979. Perspect. Biol. Med. 22: 421–453.

    Google Scholar 

  54. Williams-Ashman, H. G. and Canellakis, Z. N., 1980. Physiol. Chem. Phys. 12: 457–472.

    Google Scholar 

  55. Schrode, J. and Folk, J. E., 1978. J. Biol. Chem. 253: 4837–4840.

    Google Scholar 

  56. Vulpé, M., Usher, D. and Leblond, C. P., 1956. Endocrinology 59: 257–259.

    Google Scholar 

  57. Clayton, B. E., Hammant, J. E. and Hawkins, J. B., 1956. Nature 178: 1296–1297.

    Google Scholar 

  58. Haddox, M. K. and Russell, D. H., 1981. J. Cell. Physiol. 109:447–452.

    Google Scholar 

  59. Ambron, R. T. and Kremzner, L., 1982. Proc. Natl. Acad. Sci. U.S.A. 79: 3442–3446.

    Google Scholar 

  60. Patterson, M. K., Maxwell, M. D., Birchbichler, P. J., Conway, E. and Carter, H. A., 1982. Cell. Biol. Int. Rep. 6: 461–470.

    Google Scholar 

  61. Canellakis, Z. N., Lande, L. A., and Bondy, P. K., 1981. Biochem. Biophys. Res. Commun. 100: 675–680.

    Google Scholar 

  62. Chan, W. Y., Griesmann, G. and Rennert, O. M., 1981. Adv. Polyamine Res. 3: 213–223.

    Google Scholar 

  63. Park, M. H., Cooper, H. L. and Folk, J. E., 1981. Proc. Natl. Acad. Sci. U.S.A. 79: 2869–2873.

    Google Scholar 

  64. Park, M. H., Cooper, H. L. and Folk, J. E., 1982. J. Biol. Chem 257: 7217–7222.

    Google Scholar 

  65. Cooper, H. L., Park, M. H. and Folk, J. E., 1982. Cell. 29: 791–797.

    Google Scholar 

  66. Fink, M. L., Chung, S. I. and Folk, J. E., 1980. Proc. Natl. Acad. Sci. U.S.A. 77: 4564–4568.

    Google Scholar 

  67. Joshi, M. S., Yaron, A., and Lindner, H. R., 1972. J. Reprod. Fertil. 30: 27–37.

    Google Scholar 

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Williams-Ashman, H.G. Transglutaminases and the clotting of mammalian seminal fluids. Mol Cell Biochem 58, 51–61 (1984). https://doi.org/10.1007/BF00240604

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