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Volumn 46, Issue 4, 1997, Pages 581-586

Trypsin-like enzymes during fertilization in the shrimp Rhynchocinetes typus

Author keywords

egg coat; fertilization; shrimp; sperm; trypsin like

Indexed keywords

TRYPSIN;

EID: 0030972918     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2795(199704)46:4<581::AID-MRD15>3.0.CO;2-Z     Document Type: Article
Times cited : (24)

References (24)
  • 1
    • 0023905377 scopus 로고
    • Proacrosin/acrosin during guinea pig spermatogenesis
    • Arboleda C, Gerton G (1988): Proacrosin/acrosin during guinea pig spermatogenesis. Dev Biol 125:217-225.
    • (1988) Dev Biol , vol.125 , pp. 217-225
    • Arboleda, C.1    Gerton, G.2
  • 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
    • 0022597489 scopus 로고
    • Sperm-egg interaction in the shrimp Rhynchocinetes typus
    • Barros C, Dupré E, Viveros L (1986): Sperm-egg interaction in the shrimp Rhynchocinetes typus. Gamete Res 14:171-180.
    • (1986) Gamete Res , vol.14 , pp. 171-180
    • Barros, C.1    Dupré, E.2    Viveros, L.3
  • 4
    • 1842279356 scopus 로고
    • Acrosina en la penetración espermática en mamíferos
    • J Becerra, Perez-Figares (eds): Málaga, Spain: Servicio de Publicaciones de la Universidad de Málaga
    • Barros C, Valdivia M, Yunes R, Meléndez J (1993): Acrosina en la penetración espermática en mamíferos. In J Becerra, Perez-Figares (eds): "Progresos en Biología Celular." Málaga, Spain: Servicio de Publicaciones de la Universidad de Málaga, pp 113-119.
    • (1993) Progresos en Biología Celular , pp. 113-119
    • Barros, C.1    Valdivia, M.2    Yunes, R.3    Meléndez, J.4
  • 6
    • 0000228754 scopus 로고
    • In vitro fertilization with non-motile spermatozoa of the brown shrimp Penaeus aztecus
    • Clark W, Talbot P, Neal R, Mock C, Salser B (1973): In vitro fertilization with non-motile spermatozoa of the brown shrimp Penaeus aztecus. Mar Biol 22:353-354.
    • (1973) Mar Biol , vol.22 , pp. 353-354
    • Clark, W.1    Talbot, P.2    Neal, R.3    Mock, C.4    Salser, B.5
  • 7
    • 0006856598 scopus 로고
    • Role of acrosin and antibodies to acrosin in gamete interactions
    • N Alexander, D Griffin, J Spieler, G Waites (eds): New York: Wiley-Liss
    • De Ioannes A, Becker MI, Pérez C, Capote C, Barros C (1990): Role of acrosin and antibodies to acrosin in gamete interactions. In N Alexander, D Griffin, J Spieler, G Waites (eds): "Gamete Interaction: Prospects for Immunocontraception." New York: Wiley-Liss, pp 185-195.
    • (1990) Gamete Interaction: Prospects for Immunocontraception , pp. 185-195
    • De Ioannes, A.1    Becker, M.I.2    Pérez, C.3    Capote, C.4    Barros, C.5
  • 8
    • 0020616033 scopus 로고
    • Fine structure of the mature spermatozoon of Rhynchocinetes typus, Crustacea decapoda
    • Dupré E, Barros C (1983): Fine structure of the mature spermatozoon of Rhynchocinetes typus, Crustacea decapoda. Gamete Res 7:1-18.
    • (1983) Gamete Res , vol.7 , pp. 1-18
    • Dupré, E.1    Barros, C.2
  • 9
    • 0019983914 scopus 로고
    • p-aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction
    • Fraser L (1982): p-aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction. J Reprod Fertil 65:185-194.
    • (1982) J Reprod Fertil , vol.65 , pp. 185-194
    • Fraser, L.1
  • 10
    • 0025108642 scopus 로고
    • Induction of acrosomal filament formation in the sperm of Sicyonia ingentis
    • Griffin F, Clark W (1990): Induction of acrosomal filament formation in the sperm of Sicyonia ingentis. J Exp Zool 254:296-304.
    • (1990) J Exp Zool , vol.254 , pp. 296-304
    • Griffin, F.1    Clark, W.2
  • 11
    • 0019401849 scopus 로고
    • Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi: Effects of protease inhibitors
    • Hoshi M, Numakuna T, Sawada H (1981): Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi: Effects of protease inhibitors. Dev Biol 86:117-121.
    • (1981) Dev Biol , vol.86 , pp. 117-121
    • Hoshi, M.1    Numakuna, T.2    Sawada, H.3
  • 12
    • 0029047132 scopus 로고
    • Identification of a 10S trypsin-like protease that cross-reacts with anti-proteasome antibody in sea urchin egg-jelly
    • Inaba K, Morisawa M (1995): Identification of a 10S trypsin-like protease that cross-reacts with anti-proteasome antibody in sea urchin egg-jelly. Arch Biochem Biophys 319:177-184.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 177-184
    • Inaba, K.1    Morisawa, M.2
  • 14
    • 0011429960 scopus 로고
    • A morphological examination of sperm-egg interaction in the fresh water prawn, Macrobrachium rosembergii
    • Lynn J, Clark W (1983): A morphological examination of sperm-egg interaction in the fresh water prawn, Macrobrachium rosembergii. Biol Bull 164:446-458.
    • (1983) Biol Bull , vol.164 , pp. 446-458
    • Lynn, J.1    Clark, W.2
  • 15
    • 0025764331 scopus 로고
    • Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction
    • Matsumura K, Aketa K (1991): Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. Mol Reprod Dev 29:189-199.
    • (1991) Mol Reprod Dev , vol.29 , pp. 189-199
    • Matsumura, K.1    Aketa, K.2
  • 16
    • 0025143682 scopus 로고
    • Chymotrypsin-like enzymes are involved in sperm penetration through the vitelline coats of Ciona intestinales egg
    • Pinto M, Hoshi M, Marino R, Amoroso A, De Santis R (1990): Chymotrypsin-like enzymes are involved in sperm penetration through the vitelline coats of Ciona intestinales egg. Mol Reprod Dev 26:319-323.
    • (1990) Mol Reprod Dev , vol.26 , pp. 319-323
    • Pinto, M.1    Hoshi, M.2    Marino, R.3    Amoroso, A.4    De Santis, R.5
  • 17
    • 0021982921 scopus 로고
    • A 53,000-Da esterase in Strongylocentrotus purpuratus semen is derived from phagocytic cells, not sperm
    • Resing K, Green JD, Walsh KA (1985): A 53,000-Da esterase in Strongylocentrotus purpuratus semen is derived from phagocytic cells, not sperm. Dev Biol 107:87-93.
    • (1985) Dev Biol , vol.107 , pp. 87-93
    • Resing, K.1    Green, J.D.2    Walsh, K.A.3
  • 18
    • 0013670661 scopus 로고
    • Involvement of trypsin-like activity in binding of mouse spermatozoa to zonae pellucidae
    • Saling P (1981): Involvement of trypsin-like activity in binding of mouse spermatozoa to zonae pellucidae. Proc Natl Acad Sci USA 78:6231-6235.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6231-6235
    • Saling, P.1
  • 19
    • 0021178498 scopus 로고
    • Evidence for the participation of two sperm proteases, spermosin and acrosin, in fertilization of the Ascidian, Halocynthia Roretzi: Inhibitory effects of Leupeptin analogs on enzyme activities and fertilization
    • Sawada H, Yokosawa H, Someno T, Saino T, Ishii S (1984): Evidence for the participation of two sperm proteases, spermosin and acrosin, in fertilization of the Ascidian, Halocynthia Roretzi: Inhibitory effects of Leupeptin analogs on enzyme activities and fertilization. Dev Biol 105:246-249.
    • (1984) Dev Biol , vol.105 , pp. 246-249
    • Sawada, H.1    Yokosawa, H.2    Someno, T.3    Saino, T.4    Ishii, S.5
  • 20
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrysin
    • Schwert G, Takenake A (1955): A spectrophotometric determination of trypsin and chymotrysin. Biochim Biophys Acta 16:570-575.
    • (1955) Biochim Biophys Acta , vol.16 , pp. 570-575
    • Schwert, G.1    Takenake, A.2
  • 21
    • 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 (1996): Proacrosin and acrosin determination during capacitation and acrosome reaction in rabbit spermatozoa. Biocell 20:133-142.
    • (1996) Biocell , vol.20 , pp. 133-142
    • Sillerico, T.1    Valdivia, M.2    De Ioannes, A.3    Barros, C.4
  • 22
    • 0026831439 scopus 로고
    • Presence of a trypsin-like protease in starfish sperm acrosome
    • Sousa M, Moradas-Ferreira P, Acevedo C (1992): Presence of a trypsin-like protease in starfish sperm acrosome. J Exp Zool 261:349-354.
    • (1992) J Exp Zool , vol.261 , pp. 349-354
    • Sousa, M.1    Moradas-Ferreira, P.2    Acevedo, C.3
  • 23
    • 0000094382 scopus 로고
    • Isolation of bindin: The protein responsible for adhesion of sperm to sea urchin eggs
    • Vacquier V, Moy G (1977): Isolation of bindin: The protein responsible for adhesion of sperm to sea urchin eggs. Proc Natl Acad Sci USA 74:2456-2460.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2456-2460
    • Vacquier, V.1    Moy, G.2
  • 24
    • 0019723960 scopus 로고
    • Vitelline layer lytic activity in sperm extracts of the sea urchin, Hemicentrotus purpuratus
    • Yamada Y, Aketa K (1981): Vitelline layer lytic activity in sperm extracts of the sea urchin, Hemicentrotus purpuratus. Gamete Res 4:193-202.
    • (1981) Gamete Res , vol.4 , pp. 193-202
    • Yamada, Y.1    Aketa, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.