메뉴 건너뛰기




Volumn 58, Issue 3-4, 2000, Pages 215-228

Immunolocalization of proacrosin/acrosin in bovine sperm and sperm penetration through the zona pellucida

Author keywords

Cattle, male reproduction; Proacrosin acrosin; Sperm characteristics; Zona pellucida

Indexed keywords

ACROSIN; ENZYME PRECURSOR; PROACROSIN;

EID: 0034654369     PISSN: 03784320     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4320(99)00077-9     Document Type: Article
Times cited : (20)

References (59)
  • 1
    • 0031035977 scopus 로고    scopus 로고
    • Spermatozoa lacking acrosin protein show delayed fertilization
    • Adham I.M., Nafernia K., Engel W. Spermatozoa lacking acrosin protein show delayed fertilization. Mol. Reprod. Dev. 46:1997;370-376.
    • (1997) Mol. Reprod. Dev. , vol.46 , pp. 370-376
    • Adham, I.M.1    Nafernia, K.2    Engel, W.3
  • 3
    • 0023372825 scopus 로고
    • Glycosaminoglycans as probes to monitor differences in fertility of bulls
    • Ax R.L., Lenz R.W. Glycosaminoglycans as probes to monitor differences in fertility of bulls. J. Dairy Sci. 70:1987;1477-1486.
    • (1987) J. Dairy Sci. , vol.70 , pp. 1477-1486
    • Ax, R.L.1    Lenz, R.W.2
  • 4
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization
    • Baba T., Azuma S., Kashiwabara S., Toyoda Y. Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J. Biol. Chem. 269:1994;31845-31849.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 5
    • 0017507336 scopus 로고
    • Is the activated spermatozoon really capacitated?
    • Barros C., Berrios M. Is the activated spermatozoon really capacitated? J. Exp. Zool. 201:1977;65-72.
    • (1977) J. Exp. Zool. , vol.201 , pp. 65-72
    • Barros, C.1    Berrios, M.2
  • 7
    • 0027089753 scopus 로고
    • Immunodetection of acrosin during the acrosome reaction of hamster, guinea pig and human spermatozoa
    • Barros C., Capote C., Perez C., Crosby J.A., Becker M.I., De Ioannes A. Immunodetection of acrosin during the acrosome reaction of hamster, guinea pig and human spermatozoa. Biol. Res. 25:1992;31-40.
    • (1992) Biol. Res. , vol.25 , pp. 31-40
    • Barros, C.1    Capote, C.2    Perez, C.3    Crosby, J.A.4    Becker, M.I.5    De Ioannes, A.6
  • 8
    • 0021337322 scopus 로고
    • Relationship between the length of sperm preincubation and zona penetration in the golden hamster: A scanning electron microscopy study
    • Barros C., Jedlicki A., Bize I., Aguirre E. Relationship between the length of sperm preincubation and zona penetration in the golden hamster: a scanning electron microscopy study. Gamete Res. 9:1984;31-43.
    • (1984) Gamete Res. , vol.9 , pp. 31-43
    • Barros, C.1    Jedlicki, A.2    Bize, I.3    Aguirre, E.4
  • 9
    • 0343881234 scopus 로고
    • Protease involvement in penetration of egg coats: A comparative approach
    • (Suppl.)
    • Barros C., Melendez J., Valdivia M., Yunes R., Rios M. Protease involvement in penetration of egg coats: a comparative approach. J. Reprod. Dev. 39:1993;71-72. (Suppl.).
    • (1993) J. Reprod. Dev. , vol.39 , pp. 71-72
    • Barros, C.1    Melendez, J.2    Valdivia, M.3    Yunes, R.4    Rios, M.5
  • 10
    • 0018164791 scopus 로고
    • Normal penetration of rabbit spermatozoa through a trypsin and acrosin resistant zona pellucida
    • Bedford J.M., Cross N.L. Normal penetration of rabbit spermatozoa through a trypsin and acrosin resistant zona pellucida. J. Reprod. Fertil. 54:1978;385-392.
    • (1978) J. Reprod. Fertil. , vol.54 , pp. 385-392
    • Bedford, J.M.1    Cross, N.L.2
  • 12
    • 0023731968 scopus 로고
    • Identification of a secondary sperm receptor in the mouse egg zona pellucida: Role in maintenance of binding of acrosome-reacted sperm to eggs
    • Bleil J.D., Greve J.M., Wassarman P.M. Identification of a secondary sperm receptor in the mouse egg zona pellucida: role in maintenance of binding of acrosome-reacted sperm to eggs. Dev. Biol. 128:1988;376-385.
    • (1988) Dev. Biol. , vol.128 , pp. 376-385
    • Bleil, J.D.1    Greve, J.M.2    Wassarman, P.M.3
  • 13
    • 0022552266 scopus 로고
    • Autoradiography visualization of the mouse egg sperm receptor bound to sperm
    • Bleil J.D., Wassarman P.M. Autoradiography visualization of the mouse egg sperm receptor bound to sperm. J. Cell Biol. 102:1986;1363-1371.
    • (1986) J. Cell Biol. , vol.102 , pp. 1363-1371
    • Bleil, J.D.1    Wassarman, P.M.2
  • 14
    • 0023731968 scopus 로고
    • Identification of a secondary sperm receptor in the mouse egg zona pellucida. Role in maintenance of binding of acrosome-reacted sperm to egg
    • Bleil J.D., Wassarman P.M. Identification of a secondary sperm receptor in the mouse egg zona pellucida. Role in maintenance of binding of acrosome-reacted sperm to egg. Dev. Biol. 126:1988;376-385.
    • (1988) Dev. Biol. , vol.126 , pp. 376-385
    • Bleil, J.D.1    Wassarman, P.M.2
  • 15
    • 0020083074 scopus 로고
    • Effects of ram sperm acrosin on their vestments of sheep, pig, mouse and gerbil eggs
    • Brown C.R. Effects of ram sperm acrosin on their vestments of sheep, pig, mouse and gerbil eggs. J. Reprod. Fertil. 64:1982;457-462.
    • (1982) J. Reprod. Fertil. , vol.64 , pp. 457-462
    • Brown, C.R.1
  • 17
    • 0031942285 scopus 로고    scopus 로고
    • Characterization of the functional domains of board acrosin involved in non-enzymatic binding to homologous zona pellucida glycoproteins
    • Crosby J., Jones R., Barros C., Carvallo P. Characterization of the functional domains of board acrosin involved in non-enzymatic binding to homologous zona pellucida glycoproteins. Mol. Reprod. Dev. 49:1998;426-434.
    • (1998) Mol. Reprod. Dev. , vol.49 , pp. 426-434
    • Crosby, J.1    Jones, R.2    Barros, C.3    Carvallo, P.4
  • 20
    • 0021015405 scopus 로고
    • Inhibition of fertilization in the rabbit by anti-acrosin antibodies
    • Dudkiewicz A. Inhibition of fertilization in the rabbit by anti-acrosin antibodies. Gamete Res. 8:1983;183-197.
    • (1983) Gamete Res. , vol.8 , pp. 183-197
    • Dudkiewicz, A.1
  • 21
    • 0022051350 scopus 로고
    • Proteolysis of specific porcine zona pellucida glycoproteins by boar acrosin
    • Dumbar B.S., Dudkiewicz A.B, Bundman D.S. Proteolysis of specific porcine zona pellucida glycoproteins by boar acrosin. Biol. Reprod. 32:1985;618-630.
    • (1985) Biol. Reprod. , vol.32 , pp. 618-630
    • Dumbar, B.S.1    Dudkiewicz, A.B.2    Bundman, D.S.3
  • 22
    • 0025986429 scopus 로고
    • Activation and subsequent degradation of proacrosin is mediated by zona pellucida glycoproteins, negatively charged polysaccharides and DNA
    • Eberspaecher U., Gerwien J., Habenicht U., Schleuning W., Donner P. Activation and subsequent degradation of proacrosin is mediated by zona pellucida glycoproteins, negatively charged polysaccharides and DNA. Mol. Reprod. Dev. 30:1991;164-170.
    • (1991) Mol. Reprod. Dev. , vol.30 , pp. 164-170
    • Eberspaecher, U.1    Gerwien, J.2    Habenicht, U.3    Schleuning, W.4    Donner, P.5
  • 24
    • 0021710179 scopus 로고
    • Enzymatic dissection of the functions of the mouse egg's receptor for sperm
    • Florman H.M., Bechtol K.B., Wassarman P.M. Enzymatic dissection of the functions of the mouse egg's receptor for sperm. Dev. Biol. 106:1984;243-255.
    • (1984) Dev. Biol. , vol.106 , pp. 243-255
    • Florman, H.M.1    Bechtol, K.B.2    Wassarman, P.M.3
  • 25
    • 0023708198 scopus 로고
    • The regulation of acrosomal exocytosis: II. The zona pellucida-induced acrosome reaction of bovine spermatozoa is controlled by extrinsic positive regulatory elements
    • Florman H.M., First N. The regulation of acrosomal exocytosis: II. The zona pellucida-induced acrosome reaction of bovine spermatozoa is controlled by extrinsic positive regulatory elements. Dev. Biol. 128:1988;464-473.
    • (1988) Dev. Biol. , vol.128 , pp. 464-473
    • Florman, H.M.1    First, N.2
  • 26
    • 0030116182 scopus 로고    scopus 로고
    • Effects of oocyte maturation length, sperm capacitation time and heparin on bovine embryo development
    • Gliedt D.W., Rosenkrans C.F. Jr., Rorie R.W., Rakes J.M. Effects of oocyte maturation length, sperm capacitation time and heparin on bovine embryo development. J. Dairy Sci. 79:1996;532-535.
    • (1996) J. Dairy Sci. , vol.79 , pp. 532-535
    • Gliedt, D.W.1    Rosenkrans C.F., Jr.2    Rorie, R.W.3    Rakes, J.M.4
  • 27
    • 0020487559 scopus 로고
    • Bovine serum albumin, sperm motility, and the dilution effect
    • Harrison R.A., Dott H.M., Foster G.C. Bovine serum albumin, sperm motility, and the dilution effect. J. Exp. Zool. 222:1982;81-88.
    • (1982) J. Exp. Zool. , vol.222 , pp. 81-88
    • Harrison, R.A.1    Dott, H.M.2    Foster, G.C.3
  • 28
    • 0021228342 scopus 로고
    • Ultraestructural localization of proacrosin and acrosin in ram spermatozoa
    • Huneau D., Harrison R.A., Flechon J.L. Ultraestructural localization of proacrosin and acrosin in ram spermatozoa. Gamete Res. 9:1984;425-440.
    • (1984) Gamete Res. , vol.9 , pp. 425-440
    • Huneau, D.1    Harrison, R.A.2    Flechon, J.L.3
  • 29
    • 0025619642 scopus 로고
    • Identification and functions of mammalian sperm egg recognition molecules during fertilization
    • (Suppl.)
    • Jones R. Identification and functions of mammalian sperm egg recognition molecules during fertilization. J. Reprod. Fertil. 42:1990;89-105. (Suppl.).
    • (1990) J. Reprod. Fertil. , vol.42 , pp. 89-105
    • Jones, R.1
  • 30
    • 0025801953 scopus 로고
    • Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with acrosin, the putative egg-binding protein from mammalian spermatozoa
    • Jones R. Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with acrosin, the putative egg-binding protein from mammalian spermatozoa. Development. 111:1991;1155-1163.
    • (1991) Development , vol.111 , pp. 1155-1163
    • Jones, R.1
  • 31
    • 0023885039 scopus 로고
    • Carbohydrate-binding properties of board sperm proacrosin end assessment of its role in sperm-egg recognition and adhesion during fertilization
    • Jones R., Brown C.R., Lancaster T. Carbohydrate-binding properties of board sperm proacrosin end assessment of its role in sperm-egg recognition and adhesion during fertilization. Development. 102:1988;781-792.
    • (1988) Development , vol.102 , pp. 781-792
    • Jones, R.1    Brown, C.R.2    Lancaster, T.3
  • 32
    • 0019422067 scopus 로고
    • Evidence for an intrazymogen mechanism in the conversion of proacrosin into acrosin
    • Kennedy W.P., Polakoski K.L. Evidence for an intrazymogen mechanism in the conversion of proacrosin into acrosin. Biochemistry. 20:1981;2240-2245.
    • (1981) Biochemistry , vol.20 , pp. 2240-2245
    • Kennedy, W.P.1    Polakoski, K.L.2
  • 35
    • 0342658079 scopus 로고
    • Auro-Probe One: A new and universal ultra small gold particle based (immuno)detection system for high sensitivity and improved penetration
    • Leunisses J.L., Van De Plas P.F., Borghgraef P.E.J. Auro-Probe One: a new and universal ultra small gold particle based (immuno)detection system for high sensitivity and improved penetration. Aurofile. 2:1989;1-2.
    • (1989) Aurofile , vol.2 , pp. 1-2
    • Leunisses, J.L.1    Van De Plas, P.F.2    Borghgraef, P.E.J.3
  • 36
    • 0024356204 scopus 로고
    • Evidence that aggregation of mouse sperm receptors by ZP3 triggers the acrosome reaction
    • Leyton L., Saling P. Evidence that aggregation of mouse sperm receptors by ZP3 triggers the acrosome reaction. J. Cell Biol. 108:1989;2163-2168.
    • (1989) J. Cell Biol. , vol.108 , pp. 2163-2168
    • Leyton, L.1    Saling, P.2
  • 37
    • 0025785915 scopus 로고
    • Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments
    • Mortillo S., Wassarman P.M. Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments. Development. 113:1991;141-149.
    • (1991) Development , vol.113 , pp. 141-149
    • Mortillo, S.1    Wassarman, P.M.2
  • 38
    • 0018831489 scopus 로고
    • Penetration of human spermatozoa into the human zona pellucida and the zona-free hamster eggs: A study of fertile donors and infertile patients
    • Overstreet J.W., Yanagimachi R., Katz D.F., Hayashi K., Hanson F.W. Penetration of human spermatozoa into the human zona pellucida and the zona-free hamster eggs: a study of fertile donors and infertile patients. Fertil. Steril. 33:1980;534-554.
    • (1980) Fertil. Steril. , vol.33 , pp. 534-554
    • Overstreet, J.W.1    Yanagimachi, R.2    Katz, D.F.3    Hayashi, K.4    Hanson, F.W.5
  • 41
    • 0017365296 scopus 로고
    • Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm
    • Polakoski K.L., Parrish R.F. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J. Biol. Chem. 252:1977;1888-1894.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1888-1894
    • Polakoski, K.L.1    Parrish, R.F.2
  • 42
    • 0013670661 scopus 로고
    • Involvement of trypsin like activity in binding of mouse spermatozoa to zona pellucida
    • Saling P. Involvement of trypsin like activity in binding of mouse spermatozoa to zona pellucida. Proc. Natl. Acad. Sci. U.S.A. 78:1981;6231-6235.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6231-6235
    • Saling, P.1
  • 43
    • 0030202506 scopus 로고    scopus 로고
    • Proacrosin and acrosin determination during capacitation and acrosome reaction in rabbit spermatozoa
    • Sillerico T., Valdivia M., De Ioannes A., Barros C. Proacrosin and acrosin determination during capacitation and acrosome reaction in rabbit spermatozoa. Biocell. 20:1996;133-142.
    • (1996) Biocell , vol.20 , pp. 133-142
    • Sillerico, T.1    Valdivia, M.2    De Ioannes, A.3    Barros, C.4
  • 45
    • 0006837089 scopus 로고
    • Enzymic action of acrosomal preparations on the rabbit ovum in vitro
    • Srivastava P.N., Adams C.E., Hartree E.F. Enzymic action of acrosomal preparations on the rabbit ovum in vitro. J. Reprod. Fertil. 10:1965;61-67.
    • (1965) J. Reprod. Fertil. , vol.10 , pp. 61-67
    • Srivastava, P.N.1    Adams, C.E.2    Hartree, E.F.3
  • 46
    • 0014562257 scopus 로고
    • Inhibition of in vitro fertilization of rabbit ova by trypsin inhibitors
    • Stambaugh R., Brackett B.G., Mastroianni L. Inhibition of in vitro fertilization of rabbit ova by trypsin inhibitors. Biol. Reprod. 1:1969;223-227.
    • (1969) Biol. Reprod. , vol.1 , pp. 223-227
    • Stambaugh, R.1    Brackett, B.G.2    Mastroianni, L.3
  • 47
    • 0025114177 scopus 로고
    • Acrosin activation follow its surface exposure and precedes membrane fusion in human sperm acrosome reaction
    • Tesarik J., Drahorad J., Testart J., Mendoza C. Acrosin activation follow its surface exposure and precedes membrane fusion in human sperm acrosome reaction. Development. 110:1990;391-400.
    • (1990) Development , vol.110 , pp. 391-400
    • Tesarik, J.1    Drahorad, J.2    Testart, J.3    Mendoza, C.4
  • 48
    • 0025353025 scopus 로고
    • Zona pellucida binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin β-chain (heavy chain)
    • Töpfer-Petersen E., Steinberg M., von Eschenbach C., Zucker C. Zona pellucida binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin β-chain (heavy chain). FEBS Letters. 265:1990;51-54.
    • (1990) FEBS Letters , vol.265 , pp. 51-54
    • Töpfer-Petersen, E.1    Steinberg, M.2    Von Eschenbach, C.3    Zucker, C.4
  • 49
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T.T., Gordon J. Electrophoretic transfer of proteins from polyacrilamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.T.2    Gordon, J.3
  • 50
    • 0023020208 scopus 로고
    • The action of acrosin on the zona pellucida
    • J.L. Hendrick. New York: Plenum
    • Urch U.A. The action of acrosin on the zona pellucida. Hendrick J.L. The Molecular and Cellular Biology and Fertilization. 1986;113-132 Plenum, New York.
    • (1986) The Molecular and Cellular Biology and Fertilization , pp. 113-132
    • Urch, U.A.1
  • 51
    • 0001667679 scopus 로고
    • Biochemistry and function of acrosin
    • P.M. Wassarman. Chicago: CRL Press
    • Urch U.A. Biochemistry and function of acrosin. Wassarman P.M. The Biology of Mammalian Fertilization. 1991;233-248 CRL Press, Chicago.
    • (1991) The Biology of Mammalian Fertilization , pp. 233-248
    • Urch, U.A.1
  • 52
    • 0025805799 scopus 로고
    • The interaction of boar sperm proacrosin with its natural substrate, the zona Pellucida, and with polysulfated polysaccharides
    • Urch U.A., Patel H. The interaction of boar sperm proacrosin with its natural substrate, the zona Pellucida, and with polysulfated polysaccharides. Development. 111:1991;1165-1172.
    • (1991) Development , vol.111 , pp. 1165-1172
    • Urch, U.A.1    Patel, H.2
  • 53
    • 0033128595 scopus 로고    scopus 로고
    • Proteolytic activity of rabbit perivitelline spermatozoa
    • (In Press)
    • Valdivia M., Sillerico T., De Ioannes A., Barros C. Proteolytic activity of rabbit perivitelline spermatozoa. Zygote. 7:1999;. (In Press).
    • (1999) Zygote , vol.7
    • Valdivia, M.1    Sillerico, T.2    De Ioannes, A.3    Barros, C.4
  • 54
    • 0028344754 scopus 로고
    • Immunolocalization of proacrosin/acrosin in rabbit sperm during acrosome reaction and in spermatozoa recovered from the perivitelline space
    • Valdivia M., Yunes R., Meléndez J., De Ioannes A., Leyton L., Becker M.I., Barros C. Immunolocalization of proacrosin/acrosin in rabbit sperm during acrosome reaction and in spermatozoa recovered from the perivitelline space. Mol. Reprod. Dev. 37:1994;216-222.
    • (1994) Mol. Reprod. Dev. , vol.37 , pp. 216-222
    • Valdivia, M.1    Yunes, R.2    Meléndez, J.3    De Ioannes, A.4    Leyton, L.5    Becker, M.I.6    Barros, C.7
  • 55
    • 0023320462 scopus 로고
    • The zona pellucida: A coat of many colors
    • Wassarman P.M. The zona pellucida: a coat of many colors. BioEssays. 6:1987;161-166.
    • (1987) BioEssays , vol.6 , pp. 161-166
    • Wassarman, P.M.1
  • 56
    • 0026332964 scopus 로고
    • Mouse gamete adhesion molecules
    • Wassarman P.M. Mouse gamete adhesion molecules. Biol. Reprod. 46:1992;186-191.
    • (1992) Biol. Reprod. , vol.46 , pp. 186-191
    • Wassarman, P.M.1
  • 57
    • 0001779987 scopus 로고
    • Gamete interactions during mammalian fertilization
    • Wassarman P.M. Gamete interactions during mammalian fertilization. Theriogenology. 41:1994;31-44.
    • (1994) Theriogenology , vol.41 , pp. 31-44
    • Wassarman, P.M.1
  • 58
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • E. Knobil, Neill J.D. New York: Raven Press
    • Yanagimachi N. Mammalian fertilization. Knobil E., Neill J.D. The Physiology of Reproduction. Vol. 1:1994;189-317 Raven Press, New York.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 189-317
    • Yanagimachi, N.1
  • 59
    • 0015071907 scopus 로고
    • Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors
    • Zaneveld L., Robertson R., Kessler M., Williams W. Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors. J. Reprod. Fertil. 25:1971;387-392.
    • (1971) J. Reprod. Fertil. , vol.25 , pp. 387-392
    • Zaneveld, L.1    Robertson, R.2    Kessler, M.3    Williams, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.