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Volumn 264, Issue 1, 2003, Pages 299-307

Extracellular ubiquitin system implicated in fertilization of the ascidian, Halocynthia roretzi: Isolation and characterization

Author keywords

Ascidian; Egg; Fertilization; Proteasome; Sperm; Ubiquitin

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; AGAROSE; CALCIUM CHLORIDE; CELLULOSE; DIETHYLAMINOETHYL CELLULOSE; GLYCEROL; HRVC70 RECEPTOR; RECEPTOR; SEA WATER; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0242456264     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ydbio.2003.07.016     Document Type: Article
Times cited : (27)

References (49)
  • 1
    • 0031035977 scopus 로고    scopus 로고
    • Spermatozoa lacking acrosin protein show delayed fertilization
    • Adham I.M., Nayernia 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    Nayernia, K.2    Engel, W.3
  • 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. 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
  • 3
    • 0035122390 scopus 로고    scopus 로고
    • Isolation and identification of sperm membrane antigens recognized by antisperm antibodies, and their possible role in immunological infertility disease
    • Bohring C., Krause E., Habermann B., Krause W. Isolation and identification of sperm membrane antigens recognized by antisperm antibodies, and their possible role in immunological infertility disease. Mol. Hum. Reprod. 7:2001;113-118.
    • (2001) Mol. Hum. Reprod. , vol.7 , pp. 113-118
    • Bohring, C.1    Krause, E.2    Habermann, B.3    Krause, W.4
  • 4
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:1996;801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 5
    • 0018895683 scopus 로고
    • A study of the chorion and the follicle cells in relation to the sperm-egg interaction in the ascidian, Ciona intestinalis
    • De Santis R., Jamunno G., Rosati F. A study of the chorion and the follicle cells in relation to the sperm-egg interaction in the ascidian, Ciona intestinalis. Dev. Biol. 74:1980;490-499.
    • (1980) Dev. Biol. , vol.74 , pp. 490-499
    • De Santis, R.1    Jamunno, G.2    Rosati, F.3
  • 7
    • 0001625727 scopus 로고
    • Self and nonself recognition between gametes of the ascidian, Halocynthia roretzi
    • Fuke T.M. Self and nonself recognition between gametes of the ascidian, Halocynthia roretzi. Roux's Arch. Dev. Biol. 192:1983;347-352.
    • (1983) Roux's Arch. Dev. Biol. , vol.192 , pp. 347-352
    • Fuke, T.M.1
  • 9
    • 21144480796 scopus 로고
    • The acrosome and its differentiation during spermiogenesis in Halocynthia roretzi (Ascidiacea, Tunicata)
    • Fukumoto M., Numakunai T. The acrosome and its differentiation during spermiogenesis in Halocynthia roretzi (Ascidiacea, Tunicata). Zool. Sci. 10:1993;103-109.
    • (1993) Zool. Sci. , vol.10 , pp. 103-109
    • Fukumoto, M.1    Numakunai, T.2
  • 11
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko A., Heller H., Elias S., Ciechanover A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258:1983;8206-8214.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 12
    • 0000631966 scopus 로고
    • Lysin
    • C.B. Metz, & A. Monroy. New York: Academic Press
    • Hoshi M. Lysin. Metz C.B., Monroy A. Biology of Fertilization, Vol. 2. 1985;431-462 Academic Press, New York.
    • (1985) Biology of Fertilization, Vol. 2 , pp. 431-462
    • Hoshi, M.1
  • 13
    • 0019401849 scopus 로고
    • Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi: Effects of protease inhibitors
    • Hoshi M., Numakunai T., Sawada H. Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi effects of protease inhibitors . Dev. Biol. 86:1981;117-121.
    • (1981) Dev. Biol. , vol.86 , pp. 117-121
    • Hoshi, M.1    Numakunai, T.2    Sawada, H.3
  • 14
    • 0001051185 scopus 로고
    • Glycosidases, proteases and ascidian fertilization
    • Hoshi M., Takizawa S., Hirohashi N. Glycosidases, proteases and ascidian fertilization. Semin. Dev. Biol. 5:1994;201-208.
    • (1994) Semin. Dev. Biol. , vol.5 , pp. 201-208
    • Hoshi, M.1    Takizawa, S.2    Hirohashi, N.3
  • 15
    • 0005236982 scopus 로고    scopus 로고
    • Identification and localization of sperm SUMO-1 (small ubiquitin-related modifier) in trout and tunicate
    • Inaba K. Identification and localization of sperm SUMO-1 (small ubiquitin-related modifier) in trout and tunicate. Zool. Sci. 17:2000;58S.
    • (2000) Zool. Sci. , vol.17
    • Inaba, K.1
  • 16
    • 0035816624 scopus 로고    scopus 로고
    • CDNA cloning and functional analysis of ascidian sperm proacrosin
    • Kodama E., Baba T., Yokosawa H., Sawada H. cDNA cloning and functional analysis of ascidian sperm proacrosin. J. Biol. Chem. 276:2001;24594-24600.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24594-24600
    • Kodama, E.1    Baba, T.2    Yokosawa, H.3    Sawada, H.4
  • 17
    • 0036161952 scopus 로고    scopus 로고
    • Spermosin, a trypsin-like protease from ascidian sperm: CDNA cloning, protein structures and functional analysis
    • Kodama E., Baba T., Kohno N., Satoh S., Yokosawa H., Sawada H. Spermosin, a trypsin-like protease from ascidian sperm cDNA cloning, protein structures and functional analysis . Eur. J. Biochem. 269:2002;657-663.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 657-663
    • Kodama, E.1    Baba, T.2    Kohno, N.3    Satoh, S.4    Yokosawa, H.5    Sawada, H.6
  • 18
    • 0018246464 scopus 로고
    • Differentiation of apical structures during spermiogenesis and fine structures of the spermatozoon in the ascidian Halocynthia roretzi
    • Kubo M., Ishikawa M., Numakunai T. Differentiation of apical structures during spermiogenesis and fine structures of the spermatozoon in the ascidian Halocynthia roretzi. Acta Embryol. Exp. 1978:1978;283-295.
    • (1978) Acta Embryol. Exp. , vol.1978 , pp. 283-295
    • Kubo, M.1    Ishikawa, M.2    Numakunai, T.3
  • 19
    • 0027292154 scopus 로고
    • + channel involved in sperm-induced fertilization
    • + channel involved in sperm-induced fertilization. Science. 261:1993;484-486.
    • (1993) Science , vol.261 , pp. 484-486
    • Kupitz, Y.1    Atlas, D.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0018350052 scopus 로고
    • Calcium-mediated mitochondrial movement in ascidian sperm during fertilization
    • Lambert C.C., Epel D. Calcium-mediated mitochondrial movement in ascidian sperm during fertilization. Dev. Biol. 69:1979;296-304.
    • (1979) Dev. Biol. , vol.69 , pp. 296-304
    • Lambert, C.C.1    Epel, D.2
  • 22
    • 84985793280 scopus 로고
    • Sperm binding and penetration during ascidian fertilization
    • Lambert C.C., Koch R.A. Sperm binding and penetration during ascidian fertilization. Dev. Growth Differ. 30:1988;325-336.
    • (1988) Dev. Growth Differ. , vol.30 , pp. 325-336
    • Lambert, C.C.1    Koch, R.A.2
  • 25
    • 0036152691 scopus 로고    scopus 로고
    • Extracellular adenosine triphosphate stimulates acrosomal exocytosis in bovine spermatozoa via the P2 purinoceptor
    • Luria A., Rubinstein S., Lax Y., Breitbart H. Extracellular adenosine triphosphate stimulates acrosomal exocytosis in bovine spermatozoa via the P2 purinoceptor. Biol. Reprod. 66:2002;429-437.
    • (2002) Biol. Reprod. , vol.66 , pp. 429-437
    • Luria, A.1    Rubinstein, S.2    Lax, Y.3    Breitbart, H.4
  • 26
  • 27
    • 0000175904 scopus 로고
    • The occurrence and function of proteolytic enzymes in the reproductive tract of mammals
    • A.J. Barrett. New York: North-Holland
    • Morton D.B. The occurrence and function of proteolytic enzymes in the reproductive tract of mammals. Barrett A.J. Proteinases in Mammalian Cells and Tissues. 1977;445-500 North-Holland, New York.
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 445-500
    • Morton, D.B.1
  • 28
    • 0000761253 scopus 로고
    • Periodic spawning of three types of the ascidian, Halocynthia roretzi (Drasche), under continuous light conditions
    • Numakunai T., Hoshino Z. Periodic spawning of three types of the ascidian, Halocynthia roretzi (Drasche), under continuous light conditions. J. Exp. Zool. 212:1980;381-387.
    • (1980) J. Exp. Zool. , vol.212 , pp. 381-387
    • Numakunai, T.1    Hoshino, Z.2
  • 30
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 31
    • 0000097005 scopus 로고
    • Sperm-egg interaction in ascidians
    • C.B. Metz, & A. Monroy. New York: Academic Press
    • Rosati F. Sperm-egg interaction in ascidians. Metz C.B., Monroy A. Biology of Fertilization Vol. 2. 1985;361-388 Academic Press, New York.
    • (1985) Biology of Fertilization Vol. 2 , pp. 361-388
    • Rosati, F.1
  • 32
    • 0017817267 scopus 로고
    • Studies on fertilization in the ascidians. I. Self-sterility and specific recognition between gametes of Ciona intestinalis
    • Rosati F., De Santis R. Studies on fertilization in the ascidians. I. Self-sterility and specific recognition between gametes of Ciona intestinalis. Exp. Cell Res. 112:1978;111-119.
    • (1978) Exp. Cell Res. , vol.112 , pp. 111-119
    • Rosati, F.1    De Santis, R.2
  • 33
    • 0033058681 scopus 로고    scopus 로고
    • Sperm treatment with extracellular ATP increases fertilization rates in in-vitro fertilization for male factor infertility
    • Rossato M., La Sala G.B., Balasini M., Taricco F., Galeazzi C., Ferlin A., Foresta C. Sperm treatment with extracellular ATP increases fertilization rates in in-vitro fertilization for male factor infertility. Hum. Reprod. 14:1999;694-697.
    • (1999) Hum. Reprod. , vol.14 , pp. 694-697
    • Rossato, M.1    La Sala, G.B.2    Balasini, M.3    Taricco, F.4    Galeazzi, C.5    Ferlin, A.6    Foresta, C.7
  • 34
    • 0001042739 scopus 로고
    • The presence of serum antibodies in the serum of two patients with oligospermia
    • Rümke P. The presence of serum antibodies in the serum of two patients with oligospermia. Vox Sang. 4:1954;135-140.
    • (1954) Vox Sang. , vol.4 , pp. 135-140
    • Rümke, P.1
  • 35
    • 0027219775 scopus 로고
    • High-molecular-weight protease complexes (proteasomes) of sperm of the ascidian, Halocynthia roretzi: Isolation, characterization and physiological roles in fertilization
    • Saitoh Y., Sawada H., Yokosawa H. High-molecular-weight protease complexes (proteasomes) of sperm of the ascidian, Halocynthia roretzi isolation, characterization and physiological roles in fertilization . Dev. Biol. 158:1993;238-244.
    • (1993) Dev. Biol. , vol.158 , pp. 238-244
    • Saitoh, Y.1    Sawada, H.2    Yokosawa, H.3
  • 36
    • 0036348395 scopus 로고    scopus 로고
    • Ascidian sperm lysin system
    • Sawada H. Ascidian sperm lysin system. Zool. Sci. 19:2002;139-151.
    • (2002) Zool. Sci. , vol.19 , pp. 139-151
    • Sawada, H.1
  • 37
    • 0029800324 scopus 로고    scopus 로고
    • Substrate specificity of ascidian sperm trypsin-like proteases, spermosin and acrosin
    • Sawada H., Someno T. Substrate specificity of ascidian sperm trypsin-like proteases, spermosin and acrosin. Mol. Reprod. Dev. 45:1996;240-243.
    • (1996) Mol. Reprod. Dev. , vol.45 , pp. 240-243
    • Sawada, H.1    Someno, T.2
  • 38
    • 0010043214 scopus 로고    scopus 로고
    • Self-nonself recognition and lysin system in fertilization of the ascidian Halocynthia roretzi
    • H. Sawada, H. Yokosawa, & C.C. Lambert. Tokyo: Springer-Verlag
    • Sawada H., Yokosawa H. Self-nonself recognition and lysin system in fertilization of the ascidian Halocynthia roretzi. Sawada H., Yokosawa H., Lambert C.C. The Biology of Ascidians. 2001;18-23 Springer-Verlag, Tokyo.
    • (2001) The Biology of Ascidians , pp. 18-23
    • Sawada, H.1    Yokosawa, H.2
  • 39
    • 0020471079 scopus 로고
    • Evidence for acrosin-like enzyme in sperm extract and its involvement in fertilization of the ascidian, Halocynthia roretzi
    • Sawada H., Yokosawa H., Hoshi M., Ishii S. Evidence for acrosin-like enzyme in sperm extract and its involvement in fertilization of the ascidian, Halocynthia roretzi. Gamete Res. 5:1982;291-301.
    • (1982) Gamete Res. , vol.5 , pp. 291-301
    • Sawada, H.1    Yokosawa, H.2    Hoshi, M.3    Ishii, S.4
  • 40
    • 0021103905 scopus 로고
    • Ascidian sperm chymotrypsin-like enzyme; Participation in fertilization
    • Sawada H., Yokosawa H., Hoshi M., Ishii S. Ascidian sperm chymotrypsin-like enzyme; participation in fertilization. Experientia. 39:1983;377-378.
    • (1983) Experientia , vol.39 , pp. 377-378
    • Sawada, H.1    Yokosawa, H.2    Hoshi, M.3    Ishii, S.4
  • 41
    • 0021759356 scopus 로고
    • Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata), Halocynthia roretzi: Evidence for the presence of spermosin, a novel acrosin-like enzyme
    • Sawada H., Yokosawa H., Ishii S. Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata), Halocynthia roretzi evidence for the presence of spermosin, a novel acrosin-like enzyme . J. Biol. Chem. 259:1984;2900-2904.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2900-2904
    • Sawada, H.1    Yokosawa, H.2    Ishii, S.3
  • 42
    • 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. 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. 105:1984;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
  • 43
    • 0030585338 scopus 로고    scopus 로고
    • Localization, expression, and the role in fertilization of spermosin, an ascidian sperm trypsin-like protease
    • Sawada H., Iwasaki K., Kihara-Negishi F., Ariga H., Yokosawa H. Localization, expression, and the role in fertilization of spermosin, an ascidian sperm trypsin-like protease. Biochem. Biophys. Res. Commun. 222:1996;499-504.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 499-504
    • Sawada, H.1    Iwasaki, K.2    Kihara-Negishi, F.3    Ariga, H.4    Yokosawa, H.5
  • 45
    • 0036255128 scopus 로고    scopus 로고
    • Localization and roles in fertilization of sperm proteasomes in the ascidian Halocynthia roretzi
    • Sawada H., Takahashi Y., Fujino J., Flores S.Y., Yokosawa H. Localization and roles in fertilization of sperm proteasomes in the ascidian Halocynthia roretzi. Mol. Reprod. Dev. 62:2002;271-276.
    • (2002) Mol. Reprod. Dev. , vol.62 , pp. 271-276
    • Sawada, H.1    Takahashi, Y.2    Fujino, J.3    Flores, S.Y.4    Yokosawa, H.5
  • 46
    • 0035012044 scopus 로고    scopus 로고
    • A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis
    • Sutovsky P., Moreno R., Ramalho-Santos J., Dominko T., Thompson W.E., Schatten G. A putative, ubiquitin-dependent mechanism for the recognition and elimination of defective spermatozoa in the mammalian epididymis. J. Cell Sci. 114:2001;1665-1675.
    • (2001) J. Cell Sci. , vol.114 , pp. 1665-1675
    • Sutovsky, P.1    Moreno, R.2    Ramalho-Santos, J.3    Dominko, T.4    Thompson, W.E.5    Schatten, G.6
  • 47
    • 0036165849 scopus 로고    scopus 로고
    • Ubiquitin-dependent sperm quality control mechanism recognizes spermatozoa with DNA defects as revealed by dual ubiquitin-TUNEL assay
    • Sutovsky P., Neuber E., Schatten G. Ubiquitin-dependent sperm quality control mechanism recognizes spermatozoa with DNA defects as revealed by dual ubiquitin-TUNEL assay. Mol. Reprod. Dev. 61:2002;406-413.
    • (2002) Mol. Reprod. Dev. , vol.61 , pp. 406-413
    • Sutovsky, P.1    Neuber, E.2    Schatten, G.3
  • 48
    • 0031887332 scopus 로고    scopus 로고
    • Proteasomes: Structure and biology
    • Tanaka K. Proteasomes structure and biology . J. Biochem. (Tokyo). 123:1998;195-204.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 195-204
    • Tanaka, K.1
  • 49
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets procedure and some applications . Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


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