p-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse

Zygote

Volumn 6, Issue 4, 1998, Pages 311-319

  Yamagata, Kazuo ^b   Murayama, Keitaro ^b   Kohno, Nobuhisa ^b   Kashiwabara, Shin Ichi ^b   Baba, Tadashi ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b NONE

Author keywords

Acrosin; Egg; Mouse; Sperm; Zona pellucida

Indexed keywords

4 AMINOBENZAMIDINE; 4-AMINOBENZAMIDINE; ACROSIN; BENZAMIDINE DERIVATIVE; DYFLOS; PROTEINASE; PROTEINASE INHIBITOR; TOSYLLYSYL CHLOROMETHYL KETONE;

ACROSOME; ANIMAL; ARTICLE; CHEMISTRY; ENZYMOLOGY; FEMALE; FERTILITY; IN VITRO STUDY; INSTITUTE FOR CANCER RESEARCH MOUSE; MALE; MOLECULAR WEIGHT; MOUSE; PHYSIOLOGY; ZONA PELLUCIDA;

ACROSIN; ACROSOME; ANIMALS; BENZAMIDINES; ENDOPEPTIDASES; FEMALE; ISOFLUROPHATE; MALE; MICE; MICE, INBRED ICR; MOLECULAR WEIGHT; PROTEASE INHIBITORS; SPERM-OVUM INTERACTIONS; TOSYLLYSINE CHLOROMETHYL KETONE; ZONA PELLUCIDA;

EID: 0032197525     PISSN: 09671994     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0967199498000264     Document Type: Article

References (28)

1. Baba, T., Kashiwabara, S., Watanabe, K., Itoh, H., Michikawa, Y., Kimura, K., Takada, M., Fukamizu, A. & Arai, Y. (1989). Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure. J. Biol. Chem., 264, 11920-7.
2. Baba, T., Niida, Y., Michikawa, Y., Kashiwabara, S., Kodaira, K., Takenaka, M., Kohno, N., Gerton, G.L. & Arai, Y. (1994a). An acrosomal protein, sp32, in mammalian sperm is a binding protein specific for two proacrosins and an acrosin intermediate. J. Biol. Chem. 269, 10133-40.
3. Baba, T., Azuma, S., Kashiwabara, S. & Toyoda, Y. (1994b). Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J. Biol. Chem. 269, 31845-9.
4. Cheng, A., Le, T., Palacios, M., Bookbinder, L.H., Wassarman, P.M., Suzuki, F. & Bleil, J.D. (1994). Sperm-egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3. J. Cell Biol. 125, 867-78.
5. Eddy, E.M., & O'Brien, D.A. (1994). The spermatozoon. In The Physiology of Reproduction, ed. E. Knobil & J. Neill, pp. 29-77. New York: Raven Press.
6. Foster, J.A., Friday, B.B., Maulit, M.T., Blobel, C., Winfrey, V.P., Olson, G.E., Kim, K.-S. & Gerton, G.L. (1997). AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. J. Biol. Chem. 272, 12714-22.
7. Fraser, L.R. (1982). p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction. J. Reprod. Fertil. 65, 185-94.
8. Green, D.P.L. (1978). The activation of proteolysis in the aerosome reaction of guinea-pig sperm. J. Cell Sci. 32, 153-64.
9. Hsu, S.-M. & Soban, E. (1982). Color modification of diaminobenzidine (DAB) precipitation by metallic ions and its application for double immunohistochemistry. J. Histochem. Cytochem. 30, 1079-82.
10. Huang, T.T.F. Jr, Hardy, D.M., Yanagimachi, H., Teuscher, C., Tung, K., Wild, G. & Yanagimachi, R. (1985). pH and protease control of acrosomal content stasis and release during the guinea pig sperm acrosome reaction. Biol. Reprod. 32, 451-62.
11. Klemm, U., Müller-Esterl, W. & Engel, W. (1991). Acrosin, the peculiar sperm-specific serine protease. Hum. Genet. 87, 635-41.
12. Kohno, N., Yamagata, K., Yamada, S., Kashiwabara, S., Sakai, Y. & Baba, T. (1998). Two novel testicular serine proteases, TESP1 and TESP2, are present in the mouse sperm acrosome. Biochem. Biophys. Res. Commun., 245, 658-65.
13. Meizel, S. & Lui, C.W. (1976). Evidence for the role of a trypsin-like enzyme in the hamster sperm acrosome reaction. J. Exp. Zool. 195, 137-44.
14. Miyamoto, H. & Chang, M.C. (1973). Effect of protease inhibitors on the fertilizing capacity of hamster spermatozoa. Biol. Reprod. 9, 533-7.
15. Okabe, M., Takada, K., Adachi, T., Kohama, Y. & Mimura, T. (1986). Inconsistent reactivity of an anti-sperm monoclonal antibody and its relationship to sperm capacitation. J. Reprod. Immunol. 9, 67-70.
16. α-acrosin. J. Biol. Chem. 253, 8428-32.
17. Siegel, M.S. & Palakoski, K.L. (1985). Evaluation of the human sperm proacrosin-acrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biol. Reprod. 32, 713-20.
18. Stambaugh, R., Brackett, B.G. & Mastroianni, L. (1969). Inhibition of in vitro fertilization of rabbit ova by trypsin inhibitors. Biol. Reprod. 1, 223-7.
19. 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.
20. Toshimori, K., Tanii, I. & Araki, S. (1995). Intra-acrosomal 155 000 dalton protein increases the antigenicity during mouse sperm maturation in the epididymis: a study using a monoclonal antibody MC101. Mol. Reprod. Dev. 42, 72-9.
21. Toyoda, Y., Yokoyama, M. & Hoshi, T. (1971). Studies on the fertilization of mouse eggs in vitro. Jpn. J. Anim. Reprod. 16, 147-51.
22. Ward, C.R. & Kopf, G.S. (1993). Molecular events mediating sperm activation. Dev. Biol. 158, 9-34.
23. Wassarman, P.M. (1988). Zona pellucida glycoproteins. Annu. Rev. Biochem. 57, 415-41.
24. Wassarman, P.M. (1990). Profile of a mammalian sperm receptor. Development 108, 1-17.
25. Yamagata, K., Murayama, K., Okabe, M., Toshimori, K., Nakanishi, T., Kashiwabara, S. & Baba, T. (1998). Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction. J. Biol. Chem. 273, 10470-4.
26. Yanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Reproduction, ed. E. Knobil & J. Neill, pp. 189-317. New York: Raven Press.
27. Yanagimachi, R. & Teichman, R.J. (1972). Cytochemical demonstration of acrosomal proteinase in mammalian and avian spermatozoa by a silver proteinage method. Biol. Reprod. 6, 87-97.
28. Zaneveld, L.J.D., Polakoski, K.L., Robertson, R.T. & Williams, W.L. (1971). Trypsin inhibitors and fertilization. In Proceedings of the First International Conference on Proteinase Inhibitors, pp 236-44. Berlin: Walter de Gruyter.