메뉴 건너뛰기




Volumn 20, Issue 2, 1996, Pages 133-142

Proacrosin and acrosin determination during capacitation and acrosome reaction in rabbit spermatozoa

Author keywords

Acrosin; Acrosome; Proacrosin; Rabbit; Spermatozoon

Indexed keywords

ACROSIN; ENZYME PRECURSOR; PROACROSIN;

EID: 0030202506     PISSN: 03279545     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (45)
  • 1
    • 0024968227 scopus 로고
    • Activation of boar proacrosin is effected by processing at both N- and C-terminal portions of the zymogen molecule
    • BABA T, WATANABE K, KASHIWABARA S-I, ARAI Y (1989). Activation of boar proacrosin is effected by processing at both N- and C-terminal portions of the zymogen molecule. FEBS Letters 244(1): 132-136.
    • (1989) FEBS Letters , vol.244 , Issue.1 , pp. 132-136
    • Baba, T.1    Watanabe, K.2    Kashiwabara, S.-I.3    Arai, Y.4
  • 2
    • 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 (1994). Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 269: 31845-31849.
    • (1994) J Biol Chem , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 3
    • 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 (1984a). Relationship between the length of sperm preincubation and zona penetration in the golden hamster: A scanning electron microscopy study. Gamete Res 9: 31-43.
    • (1984) Gamete Res , vol.9 , pp. 31-43
    • Barros, C.1    Jedlicki, A.2    Bize, I.3    Aguirre, E.4
  • 4
    • 0021700037 scopus 로고
    • Selection of morphologically abnormal spermatozoa by human cervical mucus
    • BARROS C, VIGIL P, HERRERA E, ARGUELLO B, WALKER R (1984b). Selection of morphologically abnormal spermatozoa by human cervical mucus. Arch Androl 12 (Suppl): 95-107.
    • (1984) Arch Androl , vol.12 , Issue.SUPPL. , pp. 95-107
    • Barros, C.1    Vigil, P.2    Herrera, E.3    Arguello, B.4    Walker, R.5
  • 6
    • 0027089753 scopus 로고
    • Immunodetection of acrosin during the acrosome reaction of hamster, guinea-pig and human spermatozoa
    • BARROS C, CAPOTE C, PEREZ C, CROSBY JA, BECKER MI, DE IOANNES A (1992). Immunodetection of acrosin during the acrosome reaction of hamster, guinea-pig and human spermatozoa. Biol Res 25: 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
    • 0002647611 scopus 로고
    • The culture of mouse embryos in vitro
    • J.C. Daniels and W.H. Freeman, Eds. San Francisco
    • BIGGERS JD, WHITTEN WK, WHITTINGHAM DG (1971). The culture of mouse embryos in vitro. In: Methods in Mammalian Embryology. J.C. Daniels and W.H. Freeman, Eds. San Francisco, pp. 86-116.
    • (1971) Methods in Mammalian Embryology , pp. 86-116
    • Biggers, J.D.1    Whitten, W.K.2    Whittingham, D.G.3
  • 9
    • 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 JD, GREVE JM, WASSARMAN PM (1988). 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: 376-385.
    • (1988) Dev Biol , vol.128 , pp. 376-385
    • Bleil, J.D.1    Greve, J.M.2    Wassarman, P.M.3
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • BRADFORD M (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 11
    • 0000734668 scopus 로고
    • An improved artificial vagina for collecting rabbit semen
    • BREDDERMAN PJ, FOOTE RH, YASSEN AM (1964). An improved artificial vagina for collecting rabbit semen. J Reprod Fert 7:401-403.
    • (1964) J Reprod Fert , vol.7 , pp. 401-403
    • Bredderman, P.J.1    Foote, R.H.2    Yassen, A.M.3
  • 13
    • 0343009704 scopus 로고
    • The acrosin gene: Structure, regulation and function
    • F. Dondero and P.M. Johnson, Eds. Serono Symp Publ
    • ENGEL W, ADHAM IM, KEIME S, KREMLING H, SCHLOSSER M, NAYERNIA K (1993). The acrosin gene: structure, regulation and function. In: Reproductive Immunology. F. Dondero and P.M. Johnson, Eds. Serono Symp Publ Vol 97, pp 87-93.
    • (1993) Reproductive Immunology , vol.97 , pp. 87-93
    • Engel, W.1    Adham, I.M.2    Keime, S.3    Kremling, H.4    Schlosser, M.5    Nayernia, K.6
  • 14
    • 0020532591 scopus 로고
    • Gelatin-substrate film technique for detection of acrosin in single mammalian sperm
    • FICSOR G, LEONARD L, OLDFOLD G, ROY S, BECKER R (1983). Gelatin-substrate film technique for detection of acrosin in single mammalian sperm. Fertil Steril 39(4): 548-552.
    • (1983) Fertil Steril , vol.39 , Issue.4 , pp. 548-552
    • Ficsor, G.1    Leonard, L.2    Oldfold, G.3    Roy, S.4    Becker, R.5
  • 15
    • 84987566745 scopus 로고
    • Acrosin, proacrosin, and acrosin inhibitor of human spermatozoa: Extraction, quantitation, and stability
    • GOODPASTURE J, POLAKOSKI K, ZANEVELD L (1980). Acrosin, proacrosin, and acrosin inhibitor of human spermatozoa: extraction, quantitation, and stability. J Reprod 1: 16-27.
    • (1980) J Reprod , vol.1 , pp. 16-27
    • Goodpasture, J.1    Polakoski, K.2    Zaneveld, L.3
  • 16
    • 84987492116 scopus 로고
    • Relationship of human sperm acrosin and proacrosin to semen parameters I. Comparisons between symptomatic men of infertile couples and asymptomatic men, and between different split ejaculate fractions
    • GOODPASTURE J, ZAVOS P, COHEN M, ZANEVELD L (1982). Relationship of human sperm acrosin and proacrosin to semen parameters I. Comparisons between symptomatic men of infertile couples and asymptomatic men, and between different split ejaculate fractions. J Androl 3: 151-156.
    • (1982) J Androl , vol.3 , pp. 151-156
    • Goodpasture, J.1    Zavos, P.2    Cohen, M.3    Zaneveld, L.4
  • 17
    • 0023615957 scopus 로고
    • Relationship of human sperm acrosin and proacrosin to semen parameters II. Correlations
    • GOODPASTURE JC, ZAVOS PM, COHEN MR (1987). Relationship of human sperm acrosin and proacrosin to semen parameters II. Correlations. J Androl 8: 267-271.
    • (1987) J Androl , vol.8 , pp. 267-271
    • Goodpasture, J.C.1    Zavos, P.M.2    Cohen, M.R.3
  • 18
    • 0024497451 scopus 로고
    • Caprine acrosin. Purification, characterization and proteolysis of the porcine zona pellucida
    • HARDY DM, SCHOOTS FM, HEDRICK JL (1989). Caprine acrosin. Purification, characterization and proteolysis of the porcine zona pellucida. Biochem j 257: 447-453.
    • (1989) Biochem J , vol.257 , pp. 447-453
    • Hardy, D.M.1    Schoots, F.M.2    Hedrick, J.L.3
  • 19
    • 0025801953 scopus 로고
    • Interaction of zona pellucida glycoproteins, sulfated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding protein from mammalian spermatozoa
    • JONES R (1991). Interaction of zona pellucida glycoproteins, sulfated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding protein from mammalian spermatozoa. Development 111: 1155-1163.
    • (1991) Development , vol.111 , pp. 1155-1163
    • Jones, R.1
  • 20
    • 0026058935 scopus 로고
    • Acrosin, the peculiar sperm-specific serine protease
    • KLEMM U, MULLER-ESTERL W, ENGEL W (1991). Acrosin, the peculiar sperm-specific serine protease. Hum Genet 87: 635-641.
    • (1991) Hum Genet , vol.87 , pp. 635-641
    • Klemm, U.1    Muller-Esterl, W.2    Engel, W.3
  • 22
    • 0027463992 scopus 로고
    • Inhibition of acrosin activity with a trypsin inhibitor blocks human sperm penetration of the zona pellucida
    • LIU DY, BAKER G (1993). Inhibition of acrosin activity with a trypsin inhibitor blocks human sperm penetration of the zona pellucida. Biol Reprod 48: 340-348.
    • (1993) Biol Reprod , vol.48 , pp. 340-348
    • Liu, D.Y.1    Baker, G.2
  • 23
    • 0016017003 scopus 로고
    • Biochemistry of mammalian fertilization
    • MCRORIE R, WILLIAMS W (1974). Biochemistry of mammalian fertilization. Ann Rev Biochem 43: 777-803.
    • (1974) Ann Rev Biochem , vol.43 , pp. 777-803
    • Mcrorie, R.1    Williams, W.2
  • 24
    • 0017227135 scopus 로고
    • Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa
    • MEIZEL S, MUKERJI S (1976). Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa. Biol Reprod 14: 444-450.
    • (1976) Biol Reprod , vol.14 , pp. 444-450
    • Meizel, S.1    Mukerji, S.2
  • 25
    • 0025806456 scopus 로고
    • Human spermatozoa selected by percoll gradient or swim-up are equally capable of binding to the human zona pellucida and undergoing the acrosome reaction
    • MORALES P, VANTMAN D, BARROS C, VIGIL P (1991). Human spermatozoa selected by percoll gradient or swim-up are equally capable of binding to the human zona pellucida and undergoing the acrosome reaction. Hum Reprod 6(3): 401-404.
    • (1991) Hum Reprod , vol.6 , Issue.3 , pp. 401-404
    • Morales, P.1    Vantman, D.2    Barros, C.3    Vigil, P.4
  • 26
    • 0025785915 scopus 로고
    • Differential binding of gold labeled zona pellucida glycoproteins mZP2 and mZP to mouse sperm membrane compartments
    • MORTILLO S, WASSARMAN P (1991). Differential binding of gold labeled zona pellucida glycoproteins mZP2 and mZP to mouse sperm membrane compartments. Development 113: 141-149.
    • (1991) Development , vol.113 , pp. 141-149
    • Mortillo, S.1    Wassarman, P.2
  • 27
    • 0026414449 scopus 로고
    • Mechanism of maturation and nature of carbohydrate chains of boar sperm acrosin
    • MOOS J, TESARICK J, LECA G, PEKNICOVA J (1991). Mechanism of maturation and nature of carbohydrate chains of boar sperm acrosin. FEBS Letters 294(1): 27-30.
    • (1991) FEBS Letters , vol.294 , Issue.1 , pp. 27-30
    • Moos, J.1    Tesarick, J.2    Leca, G.3    Peknicova, J.4
  • 28
    • 0027464762 scopus 로고
    • Relation between molecular conversions of acrosin and the progression of exocytosis in the calcium ionophore-induced acrosome reaction
    • MOOS J, PEKNICOVA J, TESARICK J (1993). Relation between molecular conversions of acrosin and the progression of exocytosis in the calcium ionophore-induced acrosome reaction. Biochem Biophys Acta 1176: 199-207.
    • (1993) Biochem Biophys Acta , vol.1176 , pp. 199-207
    • Moos, J.1    Peknicova, J.2    Tesarick, J.3
  • 29
    • 0026304914 scopus 로고
    • The acrosin system of bull, boar and ram sperm
    • NEHRING H (1991). The acrosin system of bull, boar and ram sperm. Arch Exp Veterinarmed 45(1): 5-14.
    • (1991) Arch Exp Veterinarmed , vol.45 , Issue.1 , pp. 5-14
    • Nehring, H.1
  • 30
    • 0025062498 scopus 로고
    • Proacrosin activation and acrosin release during the guinea pig acrosome reaction
    • NUZZO N, ANDERSON R, ZANEVELD L (1990). Proacrosin activation and acrosin release during the guinea pig acrosome reaction. Molecular Reprod and Development 25: 52-60.
    • (1990) Molecular Reprod and Development , vol.25 , pp. 52-60
    • Nuzzo, N.1    Anderson, R.2    Zaneveld, L.3
  • 31
    • 0022958105 scopus 로고
    • Sperm membrane and zona pellucida interaction during fertilization
    • D.S. Dhindsa and O. Bahl, Eds. Plenum, New York
    • O'RAND MG, WELCH JE, FISHER SJ (1986). Sperm membrane and zona pellucida interaction during fertilization. In: Molecular and Cellular Aspects of Reproduction. D.S. Dhindsa and O. Bahl, Eds. Plenum, New York, pp 131-144.
    • (1986) Molecular and Cellular Aspects of Reproduction , pp. 131-144
    • O'Rand, M.G.1    Welch, J.E.2    Fisher, S.J.3
  • 32
    • 0017640285 scopus 로고
    • Demonstration of proacrosin and quantitation of acrosin in ejaculated human spermatozoa
    • POLAKOSKI K, ZAHLER W, PAULSON J (1977). Demonstration of proacrosin and quantitation of acrosin in ejaculated human spermatozoa. Fertil Steril 25(6): 668-671.
    • (1977) Fertil Steril , vol.25 , Issue.6 , pp. 668-671
    • Polakoski, K.1    Zahler, W.2    Paulson, J.3
  • 33
    • 0023841041 scopus 로고
    • The sperm acrosome: Functional and clinical aspects
    • SCHILL W-B, TÖPFER-PETERSEN E, HEISSLER E (1988). The sperm acrosome: functional and clinical aspects. Hum Reprod 3(2): 139-145.
    • (1988) Hum Reprod , vol.3 , Issue.2 , pp. 139-145
    • Schill, W.-B.1    Töpfer-Petersen, E.2    Heissler, E.3
  • 34
    • 0343881225 scopus 로고
    • Cell surface galactosyltransferase: Function during gamete recognition
    • SHUR BD (1993). Cell surface galactosyltransferase: function during gamete recognition. J Reprod Development 39 (Suppl): 41-42.
    • (1993) J Reprod Development , vol.39 , Issue.SUPPL. , pp. 41-42
    • Shur, B.D.1
  • 35
    • 0015504330 scopus 로고
    • Studies on acrosomal proteinase of rabbit spermatozoa
    • STAMBAUGH R, BUCKLEY J (1972). Studies on acrosomal proteinase of rabbit spermatozoa. Biochem Biophys Acta 248: 473-477.
    • (1972) Biochem Biophys Acta , vol.248 , pp. 473-477
    • Stambaugh, R.1    Buckley, J.2
  • 36
    • 0016983526 scopus 로고
    • Sperm proteinase release during fertilization of rabbit ova
    • STAMBAUGH R, SMITH M (1976). Sperm proteinase release during fertilization of rabbit ova. J Exp Zool 197: 121-125.
    • (1976) J Exp Zool , vol.197 , pp. 121-125
    • Stambaugh, R.1    Smith, M.2
  • 37
    • 0025373198 scopus 로고
    • Zona pellucida of proacrosin to acrosin
    • TÖPFER-PETERSEN E, CECHOVA D (1990). Zona pellucida of proacrosin to acrosin. Int J Androl 13(3): 190-196.
    • (1990) Int J Androl , vol.13 , Issue.3 , pp. 190-196
    • Töpfer-Petersen, E.1    Cechova, D.2
  • 38
    • 0023662092 scopus 로고
    • Acrosin shows zona and fucose binding, novel properties for a serine proteinase
    • TÖPFER-PETERSEN E, HENSCHEN A (1987). Acrosin shows zona and fucose binding, novel properties for a serine proteinase. FEBS letters 226(1): 38-42.
    • (1987) FEBS Letters , vol.226 , Issue.1 , pp. 38-42
    • Töpfer-Petersen, E.1    Henschen, A.2
  • 41
    • 0009482260 scopus 로고
    • EIectrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • TOWBIN H, STAEHELIN T, GORDON J (1979). EIectrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76 (9): 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.9 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0021959722 scopus 로고
    • Limited and specific proteolysis of the zona pellucida by acrosin
    • URCH UA, WARDRIP NJ, HEDRICK JL (1985). Limited and specific proteolysis of the zona pellucida by acrosin. J Exp Zool 233:478-483.
    • (1985) J Exp Zool , vol.233 , pp. 478-483
    • Urch, U.A.1    Wardrip, N.J.2    Hedrick, J.L.3
  • 43
    • 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, MELENDEZ J, DE IOANNES AE, LEYTON L, BECKER MI, BARROS C (1994). Immunolocalization of proacrosin/acrosin in rabbit sperm during acrosome reaction and in spermatozoa recovered from the perivitelline space. Mol Reprod Develop 37: 216-222.
    • (1994) Mol Reprod Develop , vol.37 , pp. 216-222
    • Valdivia, M.1    Yunes, R.2    Melendez, J.3    De Ioannes, A.E.4    Leyton, L.5    Becker, M.I.6    Barros, C.7
  • 44
    • 0001192303 scopus 로고
    • Kinetics of papain-catalyzed hydrolysis of a-N-benzoyl-L-arginine ethyl ester and a-N-benzoyl-L-argininamide
    • WHITAKER JR, BENDER HL (1965). Kinetics of papain-catalyzed hydrolysis of a-N-benzoyl-L-arginine ethyl ester and a-N-benzoyl-L-argininamide. J Am Chem Soc 87: 2728-2737.
    • (1965) J Am Chem Soc , vol.87 , pp. 2728-2737
    • Whitaker, J.R.1    Bender, H.L.2
  • 45
    • 0002302562 scopus 로고
    • Mammalian Fertilization
    • E Knobil and JD Neil, Eds. Raven Press, Ltd, New York
    • YANAGIMACHI R (1994). Mammalian Fertilization. In: The Physiology of Reproduction. E Knobil and JD Neil, Eds. Raven Press, Ltd, New York, pp 185-317.
    • (1994) The Physiology of Reproduction , pp. 185-317
    • Yanagimachi, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.