The polysulphate binding domain of human proacrosin/acrosin is involved in both the enzyme activation and spermatozoa-zona pellucida interaction

Zygote

Volumn 6, Issue 1, 1998, Pages 75-83

  Moreno, R D ^a   Sepulveda M S ^a,c   De Ioannes, A ^a   Barros, C ^a,b  

^a PONTIFICIA UNIVERSIDAD CATÓLICA DE CHILE   (Chile)

^b Laboratory of Embryology   (Chile)

^c CLÍNICA LAS CONDES   (Chile)

Author keywords

Acrosin; Fucoidan; Proacrosin; Spermatozoon; Zona pellucida

Indexed keywords

MAMMALIA;

ACROSIN; ENZYME PRECURSOR; FUCOIDIN; MONOCLONAL ANTIBODY; POLYSACCHARIDE; PROACROSIN; SULFATE;

ACROSOME; ANIMAL; ARTICLE; BINDING SITE; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; FEMALE; FERTILITY; HAMSTER; HUMAN; IMMUNOLOGY; MALE; METABOLISM; SYRIAN HAMSTER; ZONA PELLUCIDA;

ACROSIN; ACROSOME; ANIMALS; ANTIBODIES, MONOCLONAL; BINDING SITES; CRICETINAE; ENZYME ACTIVATION; ENZYME PRECURSORS; FEMALE; HUMANS; MALE; MESOCRICETUS; POLYSACCHARIDES; SPERM-OVUM INTERACTIONS; SULFATES; ZONA PELLUCIDA;

EID: 0031993410     PISSN: 09671994     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0967199400005104     Document Type: Article

References (61)

1. Baba, T., Kashiwabara, S.I., Watanabe, K., Itoh, H., Michikawa, Y., Kimura, K., Takada, M., Fukamazu, A. & Arai, Y. (1989a). Activation and maturation mechanism of boar acrosin zymogen based on the deduced primary structure. J. Biol. Chem. 264, 11920-7.
2. Baba, T., Michikawa, Y., Kawakura, K. & Arai, Y. (1989b). Activation of boar proacrosin is effected by processing at both N- and C-terminal portions of the zymogen molecule. FEBS Lett. 244, 132-6.
3. Barros, C. & Jedlicki, A. (1985). Human sperm fertilizing ability: quality criteria. In Human In Vitro Fertilization, ed. J. Testart & R. Frydman, pp. 79-91. New York: INSERM Symposium. Elsevier.
4. Barros, C., Gonzalez, J., Herrera, E. & Bustos-Obregón, E. (1979). Human sperm penetration into zona-free hamster oocyte as a test to evaluate the sperm fertilizing ability. Andrologia 11, 197-210.
5. Barros, C., Jedlicki, A., Bize, I. & Aguirre, E. (1984). Relationship between the length of sperm preincubation and zona penetration in the golden hamster: a scanning electron microscopy study. Gamete Res. 9, 31-43
6. Barros, C., Crosby, J.A. & Moreno, R.D. (1996) Early steps of sperm-egg interactions during mammalian fertilisation. Cell Biol. Int. 20, 33-9.
7. Berger, T., Davis, A;., Wardrip, N.J. & Hedrick, J.L. (1989). Sperm binding to the pig zona pellucida and inhibition of binding by solubilized components of the zona pellucida. J. Reprod. Fertil. 86, 559-65.
8. Berman, H.A., Becktel, W. & Taylor, P. (1981). Spectroscopic studies on acetylcholinesterase: influence of peripheral-site occupation on active-center conformation. Biochemistry 20, 4803-10.
9. Biggers, J., Whitten, W. & Whittingham D (1971). The culture of mouse embryos in vitro. In Methods in Mammalian Embryology, ed. J.C. Daniel, pp. 86-116. San Francisco: W.H. Freeman.
10. Danishefky, L. & Klein S (1977). Effect of heparin modification on its activity in enhancing the inhibition of thrombin by antithrombin III. Biochim. Biophys. Acta 498, 215-22.
11. de Ioannes, A.E., Becker, M.I., Perez, C., Capote, C. * Barros, C. (1990). Role of acrosin and antibodies to acrosin in gamete interactions. In Gamete Interactions: Prospects for Immunocontraception, ed. N. Alexander, D. Griffin, J. Spieler & G. Waites, pp. 185-95. New York: Wiley-Liss.
12. Drahorad, J., Cechova, D. & Tesarik, J. (1988) Activation of proacrosin by a locally produced component of human follicular fluid. J. Reprod. Fertil. 83, 599-603.
13. Drahorad, J., Tesarik, J., Cechova, D. & Vilim, V. (1991). Proteins and glycosaminoglycans in the intercellular matrix of the human cumulus-oophorus and their effect on conversion of proacrosin to acrosin. J. Reprod. Fertil. 93, 253-62.
14. 2 on the penetration of zona pellucida-free hamster eggs by acrosome-reacted hamster sperm. J. Androl. 3, 388-95.
15. Dudkiewicz, A.B. (1983). Inhibition of fertilisation in the rabbit by anti-acrosin antibodies. Gamete Res. 8, 183-7.
16. Dumbar, B.S., Dudkiewicz, A.B. & Bundman, D.S. (1985). Proteolysis of specific porcine zona pellucida glycoproteins by boar acrosin. Biol. Reprod. 32, 619-30.
17. Eberspaecher, U., Gerwien, J., Habenicht, U.-F., Schleuning, W.-D. & Donner, P. (1991). Activation and subsequent degradation of proacrosin is mediated by zona pellucida glycoproteins, negatively charged polysaccharides, and DNA. Mol. Reprod. Dev. 30, 164-70
18. Fock-Nüzel, R., Lottspeich, F., Henschen, A. & Müller-Esterl, W. (1984). Boar acrosin is a two chain molecule: isolation and primary structure of the light chain; homology with the propart of other serine proteases. Eur. J. Biochem. 141, 441-6.
19. Green, D.P.L. (1978). The activation of proteolysis in the acrosome reaction of guinea-pig sperm. J. Cell Sci. 32, 153-64.
20. Hardy, D.M., Oda, M.N., Friend, D.S. & Huang, T.F. Jr (1991). A mechanism for differential release of acrosomal enzymes during the acrosome reaction. Biochem. J. 275, 759-66.
21. Harlow, E. & Lane, D. (1988). Antibodies: A Laboratory Manual, pp. 472-510. New York: Cold Spring Harbor Laboratory Press.
22. Huang, T.T.F. & Yanagimachi, R. (1982). Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals. Gamete Res. 5, 355-61.
23. Huang, T.T.F. & Yanagimachi, R. (1984). Fucoidan inhibits attachment of guinea pig spermatozoa to the zona pellucida through binding to the inner acrosomal membrane and equatorial domains. Exp. Cell Res. 153, 363-73.
24. Jansen, S., Quigley, M., Reik, W. & Jones, R. (1995). Analysis of polysulphate-binding domains in porcine proacrosin, a putative zona adhesion protein from mammalian spermatozoa. Int. J. Dev. Biol. 39, 501-510.
25. Jones, R. (1991). Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding proteins from mammalian spermatozoa. Development 11, 1155-63
26. Jones, R., Brown, C.R. & Lancaster, R.T. (1988). Carbohydrate-binding properties of boar sperm proacrosin and assessment of its role in sperm-egg recognition and adhesion during fertilisation. Development. 102. 781-92.
27. Kreienkamp, H.J., Weise, C., Raba, R., Aaviksaar, A. & Hucho, F. (1991). Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom. Proc. Natl. Acad. Sci. USA 88, 6117-21.
28. Laemmli, U.K. (1970). Cleavage of the structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-5.
29. Leyton, L., De Ioannes, A., Croxatto, H., Graham, E. & Elce, J. (1986). Two satisfactory methods for purification of human acrosin. Biochem. Cell Biol. 64, 1020-4.
30. Lo Leggio, L., Williams, R.M. & Jones, R. (1994). Some effects of zona pellucida glycoproteins and sulphated polymers on the autoactivation of boar sperm proacrosin and activity of α-acrosin J. Reprod. Fertil. 100, 177-185.
31. Lui, C.W. & Meizel, S. (1979). Further evidence in support of a role for hamster sperm hydrolytic enzymes in the acrosome reaction. J. Exp. Zool. 207, 173-85.
32. Meizel, S. & Lui, C.W. (1976). Evidence for a role of a trypsin-like enzyme in the hamster sperm acrosome reaction. J. Exp. Zool. 195, 137-44.
33. Moreno, R.D. & Barros, C. (1991). Effect of TEST-yolk upon human sperm acrosome reaction. Micr. Electr. Biol. Cel. 15, 107-18.
34. Nakano, M., Tanak, Y., Kimura, T., Hatanak, Y. & Tobita, T. (1989). Boar acrosin digestion of the porcine egg coat, zona pellucida, and rearrangement of the zona proteins. J. Biochem. 105, 138-142.
35. Olson, G.E., Winfrey, V.P. (1994). Structure of acrosomal matrix domains of rabbit sperm. J. Struct. Biol. 112, 41-8.
36. Ordentlich, A., Barak, D., Kronman, C., Ariel, N., Segall, Y., Velan, B. & Shaffernam, A. (1995). Contribution of aromatic moieties of tyrosine 133 of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase. J. Biol. Chem. 270, 2082-91.
37. Parrish, R., Wincek, T.J. & Polakoski, K.L. (1980). Glycosaminoglycan stimulation of the in vitro conversion of boar proacrosin into acrosin. J. Androl. 1, 89-95.
38. Polakoski, K.L. & Parrish, R.F. (1977). Boar proacrosin: purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J. Biol. Chem. 252, 1888-94.
39. Radic, Z., Reiner, E. & Taylor, P. (1991). Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrate excess and coumarin derivates. Mol. Pharmacol. 39, 98-104.
40. Richardson, R.T. & O'Rand, M.G. (1996). Site-directed mutagenesis of rabbit proacrosin. J. Biol. Chem. 271, 24069-74.
41. Rosenberg, R.D., Oosta, G.M., Jordan, R.E. & Gardner, W.T. (1980). The interaction of heparin with thrombin and antithrombin. Biochem. Biophys. Res. Commun. 96, 1200-8.
42. Sepulveda, M.S., Becker, M.I., Barros, C. & de Ioannes, A. (1993). Interference of gamete interactions by monoclonal antibodies to acrosin. In Reproductive Immunology, ed. F. Dondero & P.M. Johnson, pp. 335-8. Serono Symposia.
43. Shafferman, A., Velan, B., Ordentlich, A., Kronman, C., Grosfeld, H., Leimer, M., Flashner, Y., Cohen, S., Barav, D. & Ariel, N. (1992). Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center. EMBO J. 11, 3561-68.
44. Sillerico, T., Valdivia, M., de Ioannes, A. & Barros, C. (1996). Proacrosin and acrosin determination during capacitation and acrosome reaction in rabbit spermatozoa. Biocell 20, 133-42.
45. Stambaugh, R. & Mastroianni, L. Jr (1980). Stimulation of rhesus monkey (Macaca mulatto) proacrosin activation by oviduct fluid. J. Reprod. Fertil. 59, 479-84.
46. Takano, H., Yanagimachi, R. & Urch, U.A. (1993). Evidence that acrosin activity is important for the development of fusibility of mammalian spermatozoa with the oolemma: inhibitor studies using the golden hamster. Zygote 1, 79-91.
47. Töpfer-Petersen, E. & Cechova, D. (1990). Zona pellucida induces conversion of proacrosin to acrosin. Int. J. Androl. 13, 190-6.
48. Töpfer-Petersen, E. & Henschen, A. (1988). Zona pellucida-binding and fucose-binding of boar sperm acrosin is not correlated with proteolytic activity. Biol. Chem. Hoppe-Seyler 369, 69-76.
49. Töpfer-Petersen, E., Calvete, J., Schäfer, W. & Henscheri, A. (1990a). Complete localization of the disulphide bridges and glycosylation sites in boar sperm acrosin. FEBS Lett. 275, 139-142.
50. Töpfer-Petersen, E., Steinberg, M., von Eschenbach, C. & Zucker, C. (1990b). Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain). FEBS Lett. 265, 51-4.
51. Towbin, H., Stachelin, T. & Gordon, J. (1979). Electrophoreric transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4.
52. Urch, U.A., Hedrick, J.L. (1988). The inhibition of boar acrosin amidase activity by sulphated polysaccharides. biol. Chem. Hoppe-Seyler 369, 727-32.
53. Urch, U.A. & Patel, H. (1991). The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida and with polysulphated polysaccharides. Development 11, 1165-72.
54. Urch, U.A., Wardrip, N.J. & Hedrick, J.L. (1985). Limited and specific proteolysis of the zona pellucida by acrosin. J. Exp. Zool. 233, 479-83.
55. Valdivia, M., Yunes, R., Melendez, J., de Ioannes, A.E., Leyton, L., Becker, M.I. & Barros, C (1994). Immunolocalization of proacrosin/acrosin in rabbit sperm during aerosome reaction and in spermatozoa recovered from the perivitelline space. Mol. Reprod. Dev. 37, 216-22.
56. Williams, R.M. & Jones, R. (1990). Specific binding of sulphated polymers to ram sperm acrosin. FEBS Lett. 270, 168-72.
57. Wincek, T., Parrish, R. & Polakoski, K. (1979). Fertilization: a uterine glycosaminoglycan stimulates the conversion of sperm proacrosin to acrosin. Science 203, 553-4.
58. Windt, M.-L., Franken, D.R., de Beer, P.M., Bouic, P.J.D. & Kruger, T.F. (1991). The hemizona assay (HZA) as an experimental model to evaluate the inhibition of sperm binding to the murine zona pellucida by isolated zona pellucida protein. Andrologia 23, 209-12.
59. Wolf, D.P. (1977). Involvement of a trypsin-like activity in sperm penetration of zone-free mouse ova. J Exp. Zool. 199, 149-55.
60. Yanagimachi, R. (1994). Mammalian fertilisation. In Physiology of Reproduction, ed. E. Knobil & J.D. Neill, pp. 189-317. New York: Raven Press.
61. Yurewicz, E.C., Pack, B.A. & Sacco, A.G. (1991). Isolation, composition, and biological activity of sugar of porcine oocyte zona pellucida 55K glycoproteins. Mol. Reprod. Dev. 30, 126-34.